Biotin
Antibodies
Antibody Specificity
Avidin
Antibody Formation
Antibodies, Neutralizing
Carbon-Nitrogen Ligases
Antibody Affinity
Streptavidin
Fluorescent Antibody Technique
Antibodies, Anti-Idiotypic
Binding Sites, Antibody
Methylmalonyl-CoA Decarboxylase
Antibodies, Neoplasm
Antibodies, Antinuclear
Cross Reactions
Molecular Sequence Data
Amino Acid Sequence
Immunoglobulin M
Autoantibodies
Pyruvate Carboxylase
Neutralization Tests
Antigen-Antibody Reactions
Antibodies, Bispecific
Mice, Inbred BALB C
Valerates
Single-Chain Antibodies
Antibodies, Blocking
Immunoglobulin G
Biotinidase
Antigen-Antibody Complex
Immunoglobulin Fab Fragments
Carbon-Carbon Ligases
Antibodies, Heterophile
Antibodies, Catalytic
Rabbits
Acetyl-CoA Carboxylase
Immunoglobulin A
Antibodies, Monoclonal, Humanized
Fluorescent Antibody Technique, Indirect
Fatty Acid Synthase, Type II
Carboxyl and Carbamoyl Transferases
Hybridomas
Immune Sera
Epitope Mapping
Immunoenzyme Techniques
Antibodies, Antiphospholipid
Immunization
Pimelic Acids
Escherichia coli
Enzyme-Linked Immunosorbent Assay
Blotting, Western
Electrophoresis, Polyacrylamide Gel
Base Sequence
Antigens, Surface
Immunoassay
Immunization, Passive
Immunohistochemistry
Cells, Cultured
Protein Binding
Hoof and Claw
Immunoblotting
Immunoglobulin Fragments
Multiple Carboxylase Deficiency
Egg White
Radioimmunoassay
B-Lymphocytes
Complement Fixation Tests
Binding, Competitive
Peptide Library
Immunosorbent Techniques
Hemagglutination Tests
Hemagglutination Inhibition Tests
Antibodies, Antineutrophil Cytoplasmic
Cattle
Immunoglobulin Variable Region
Seroepidemiologic Studies
Immunoglobulin Idiotypes
Recombinant Fusion Proteins
T-Lymphocytes
Immunologic Techniques
Antigens, Neoplasm
Sensitivity and Specificity
Flow Cytometry
Binding Sites
Cloning, Molecular
Peptide Fragments
Chromatography, Affinity
Radioimmunodetection
Haptens
Tissue Distribution
Antibody Diversity
Biotinidase Deficiency
Vitamin B Deficiency
Peptides
Glycoproteins
Species Specificity
Iodine Radioisotopes
Hepatitis C Antibodies
Isoantibodies
Immunoglobulin Isotypes
Immunoglobulins
Carboxy-Lyases
Antibodies, Monoclonal, Murine-Derived
Radioimmunotherapy
Vaccination
Ligases
Hepatitis B Antibodies
Immunodiffusion
Immunity, Maternally-Acquired
Mice, Inbred C57BL
Complement System Proteins
Lupus Erythematosus, Systemic
Membrane Proteins
Carrier Proteins
Protein Conformation
Lymphocytes
Models, Molecular
Mutation
Autoantigens
Precipitin Tests
Cell Membrane
Antigens, Protozoan
Pantothenic Acid
Holocarboxylase Synthetase Deficiency
Biotin is a water-soluble vitamin, also known as Vitamin B7 or Vitamin H. It is a cofactor for several enzymes involved in metabolism, particularly in the synthesis and breakdown of fatty acids, amino acids, and carbohydrates. Biotin plays a crucial role in maintaining healthy skin, hair, nails, nerves, and liver function. It is found in various foods such as nuts, seeds, whole grains, milk, and vegetables. Biotin deficiency is rare but can occur in people with malnutrition, alcoholism, pregnancy, or certain genetic disorders.
Antibodies are proteins produced by the immune system in response to the presence of a foreign substance, such as a bacterium or virus. They are capable of identifying and binding to specific antigens (foreign substances) on the surface of these invaders, marking them for destruction by other immune cells. Antibodies are also known as immunoglobulins and come in several different types, including IgA, IgD, IgE, IgG, and IgM, each with a unique function in the immune response. They are composed of four polypeptide chains, two heavy chains and two light chains, that are held together by disulfide bonds. The variable regions of the heavy and light chains form the antigen-binding site, which is specific to a particular antigen.
Antibody specificity refers to the ability of an antibody to bind to a specific epitope or antigenic determinant on an antigen. Each antibody has a unique structure that allows it to recognize and bind to a specific region of an antigen, typically a small portion of the antigen's surface made up of amino acids or sugar residues. This highly specific binding is mediated by the variable regions of the antibody's heavy and light chains, which form a pocket that recognizes and binds to the epitope.
The specificity of an antibody is determined by its unique complementarity-determining regions (CDRs), which are loops of amino acids located in the variable domains of both the heavy and light chains. The CDRs form a binding site that recognizes and interacts with the epitope on the antigen. The precise fit between the antibody's binding site and the epitope is critical for specificity, as even small changes in the structure of either can prevent binding.
Antibody specificity is important in immune responses because it allows the immune system to distinguish between self and non-self antigens. This helps to prevent autoimmune reactions where the immune system attacks the body's own cells and tissues. Antibody specificity also plays a crucial role in diagnostic tests, such as ELISA assays, where antibodies are used to detect the presence of specific antigens in biological samples.
Antibodies, viral are proteins produced by the immune system in response to an infection with a virus. These antibodies are capable of recognizing and binding to specific antigens on the surface of the virus, which helps to neutralize or destroy the virus and prevent its replication. Once produced, these antibodies can provide immunity against future infections with the same virus.
Viral antibodies are typically composed of four polypeptide chains - two heavy chains and two light chains - that are held together by disulfide bonds. The binding site for the antigen is located at the tip of the Y-shaped structure, formed by the variable regions of the heavy and light chains.
There are five classes of antibodies in humans: IgA, IgD, IgE, IgG, and IgM. Each class has a different function and is distributed differently throughout the body. For example, IgG is the most common type of antibody found in the bloodstream and provides long-term immunity against viruses, while IgA is found primarily in mucous membranes and helps to protect against respiratory and gastrointestinal infections.
In addition to their role in the immune response, viral antibodies can also be used as diagnostic tools to detect the presence of a specific virus in a patient's blood or other bodily fluids.
Bacterial antibodies are a type of antibodies produced by the immune system in response to an infection caused by bacteria. These antibodies are proteins that recognize and bind to specific antigens on the surface of the bacterial cells, marking them for destruction by other immune cells. Bacterial antibodies can be classified into several types based on their structure and function, including IgG, IgM, IgA, and IgE. They play a crucial role in the body's defense against bacterial infections and provide immunity to future infections with the same bacteria.
Monoclonal antibodies are a type of antibody that are identical because they are produced by a single clone of cells. They are laboratory-produced molecules that act like human antibodies in the immune system. They can be designed to attach to specific proteins found on the surface of cancer cells, making them useful for targeting and treating cancer. Monoclonal antibodies can also be used as a therapy for other diseases, such as autoimmune disorders and inflammatory conditions.
Monoclonal antibodies are produced by fusing a single type of immune cell, called a B cell, with a tumor cell to create a hybrid cell, or hybridoma. This hybrid cell is then able to replicate indefinitely, producing a large number of identical copies of the original antibody. These antibodies can be further modified and engineered to enhance their ability to bind to specific targets, increase their stability, and improve their effectiveness as therapeutic agents.
Monoclonal antibodies have several mechanisms of action in cancer therapy. They can directly kill cancer cells by binding to them and triggering an immune response. They can also block the signals that promote cancer growth and survival. Additionally, monoclonal antibodies can be used to deliver drugs or radiation directly to cancer cells, increasing the effectiveness of these treatments while minimizing their side effects on healthy tissues.
Monoclonal antibodies have become an important tool in modern medicine, with several approved for use in cancer therapy and other diseases. They are continuing to be studied and developed as a promising approach to treating a wide range of medical conditions.
Avidin is a protein found in the white of eggs (egg whites) and some other animal tissues. It has a high binding affinity for biotin, also known as vitamin B7 or vitamin H, which is an essential nutrient for humans and other organisms. This property makes avidin useful in various biochemical and medical applications, such as immunohistochemistry, blotting techniques, and drug delivery systems.
Biotin-avidin interactions are among the strongest non-covalent interactions known in nature, with a dissociation constant (Kd) of approximately 10^-15 M. This means that once biotin is bound to avidin, it is very difficult to separate them. In some cases, this property can be exploited to create stable and specific complexes for various applications.
However, it's worth noting that the high affinity of avidin for biotin can also have negative effects in certain contexts. For example, raw egg whites contain large amounts of avidin, which can bind to biotin in the gut and prevent its absorption if consumed in sufficient quantities. This can lead to biotin deficiency, which can cause various health problems. Cooking egg whites denatures avidin and reduces its ability to bind to biotin, making cooked eggs a safe source of biotin.
Antibody formation, also known as humoral immune response, is the process by which the immune system produces proteins called antibodies in response to the presence of a foreign substance (antigen) in the body. This process involves several steps:
1. Recognition: The antigen is recognized and bound by a type of white blood cell called a B lymphocyte or B cell, which then becomes activated.
2. Differentiation: The activated B cell undergoes differentiation to become a plasma cell, which is a type of cell that produces and secretes large amounts of antibodies.
3. Antibody production: The plasma cells produce and release antibodies, which are proteins made up of four polypeptide chains (two heavy chains and two light chains) arranged in a Y-shape. Each antibody has two binding sites that can recognize and bind to specific regions on the antigen called epitopes.
4. Neutralization or elimination: The antibodies bind to the antigens, neutralizing them or marking them for destruction by other immune cells. This helps to prevent the spread of infection and protect the body from harmful substances.
Antibody formation is an important part of the adaptive immune response, which allows the body to specifically recognize and respond to a wide variety of pathogens and foreign substances.
Neutralizing antibodies are a type of antibody that defends against pathogens such as viruses or bacteria by neutralizing their ability to infect cells. They do this by binding to specific regions on the surface proteins of the pathogen, preventing it from attaching to and entering host cells. This renders the pathogen ineffective and helps to prevent or reduce the severity of infection. Neutralizing antibodies can be produced naturally in response to an infection or vaccination, or they can be generated artificially for therapeutic purposes.
Carbon-Nitrogen (C-N) ligases are a class of enzymes that catalyze the joining of a carbon atom from a donor molecule to a nitrogen atom in an acceptor molecule through a process called ligase reaction. This type of enzyme plays a crucial role in various biological processes, including the biosynthesis of amino acids, nucleotides, and other biomolecules that contain both carbon and nitrogen atoms.
C-N ligases typically require ATP or another energy source to drive the reaction forward, as well as cofactors such as metal ions or vitamins to facilitate the chemical bond formation between the carbon and nitrogen atoms. The specificity of C-N ligases varies depending on the enzyme, with some acting only on specific donor and acceptor molecules while others have broader substrate ranges.
Examples of C-N ligases include glutamine synthetase, which catalyzes the formation of glutamine from glutamate and ammonia, and asparagine synthetase, which catalyzes the formation of asparagine from aspartate and ammonia. Understanding the function and regulation of C-N ligases is important for understanding various biological processes and developing strategies to modulate them in disease states.
Antibody affinity refers to the strength and specificity of the interaction between an antibody and its corresponding antigen at a molecular level. It is a measure of how strongly and selectively an antibody binds to its target antigen. A higher affinity indicates a more stable and specific binding, while a lower affinity suggests weaker and less specific interactions. Affinity is typically measured in terms of the dissociation constant (Kd), which describes the concentration of antigen needed to achieve half-maximal binding to an antibody. Generally, a smaller Kd value corresponds to a higher affinity, indicating a tighter and more selective bond. This parameter is crucial in the development of diagnostic and therapeutic applications, such as immunoassays and targeted therapies, where high-affinity antibodies are preferred for improved sensitivity and specificity.
Streptavidin is not a medical term per se, but rather a biochemical term used in the field of medicine and laboratory research. Streptavidin is a protein that is derived from the bacterium Streptomyces avidinii. It has a unique ability to bind very strongly and specifically to another molecule called biotin, with an association constant that is one of the strongest non-covalent interactions known in nature.
This property makes streptavidin a valuable tool in various medical and research applications such as immunoassays, histology, molecular biology, and drug delivery systems. For example, biotinylated molecules (such as antibodies, DNA, or enzymes) can be linked to streptavidin for detection, purification, or targeting purposes.
In summary, streptavidin is a bacterial protein that binds strongly and specifically to biotin, which is used in various medical and research applications as a tool for detection, purification, or targeting purposes.
The Fluorescent Antibody Technique (FAT) is a type of immunofluorescence assay used in laboratory medicine and pathology for the detection and localization of specific antigens or antibodies in tissues, cells, or microorganisms. In this technique, a fluorescein-labeled antibody is used to selectively bind to the target antigen or antibody, forming an immune complex. When excited by light of a specific wavelength, the fluorescein label emits light at a longer wavelength, typically visualized as green fluorescence under a fluorescence microscope.
The FAT is widely used in diagnostic microbiology for the identification and characterization of various bacteria, viruses, fungi, and parasites. It has also been applied in the diagnosis of autoimmune diseases and certain cancers by detecting specific antibodies or antigens in patient samples. The main advantage of FAT is its high sensitivity and specificity, allowing for accurate detection and differentiation of various pathogens and disease markers. However, it requires specialized equipment and trained personnel to perform and interpret the results.
Anti-idiotypic antibodies are a type of immune protein that recognizes and binds to the unique identifying region (idiotype) of another antibody. These antibodies are produced by the immune system as part of a regulatory feedback mechanism, where they can modulate or inhibit the activity of the original antibody. They have been studied for their potential use in immunotherapy and vaccine development.
A binding site on an antibody refers to the specific region on the surface of the antibody molecule that can recognize and bind to a specific antigen. Antibodies are proteins produced by the immune system in response to the presence of foreign substances called antigens. They have two main functions: to neutralize the harmful effects of antigens and to help eliminate them from the body.
The binding site of an antibody is located at the tips of its Y-shaped structure, formed by the variable regions of the heavy and light chains of the antibody molecule. These regions contain unique amino acid sequences that determine the specificity of the antibody for a particular antigen. The binding site can recognize and bind to a specific epitope or region on the antigen, forming an antigen-antibody complex.
The binding between the antibody and antigen is highly specific and depends on non-covalent interactions such as hydrogen bonds, van der Waals forces, and electrostatic attractions. This interaction plays a crucial role in the immune response, as it allows the immune system to recognize and eliminate pathogens and other foreign substances from the body.
HIV antibodies are proteins produced by the immune system in response to the presence of HIV (Human Immunodeficiency Virus) in the body. These antibodies are designed to recognize and bind to specific parts of the virus, known as antigens, in order to neutralize or eliminate it.
There are several types of HIV antibodies that can be produced, including:
1. Anti-HIV-1 and anti-HIV-2 antibodies: These are antibodies that specifically target the HIV-1 and HIV-2 viruses, respectively.
2. Antibodies to HIV envelope proteins: These antibodies recognize and bind to the outer envelope of the virus, which is covered in glycoprotein spikes that allow the virus to attach to and enter host cells.
3. Antibodies to HIV core proteins: These antibodies recognize and bind to the interior of the viral particle, where the genetic material of the virus is housed.
The presence of HIV antibodies in the blood can be detected through a variety of tests, including enzyme-linked immunosorbent assay (ELISA) and Western blot. A positive test result for HIV antibodies indicates that an individual has been infected with the virus, although it may take several weeks or months after infection for the antibodies to become detectable.
An epitope is a specific region on the surface of an antigen (a molecule that can trigger an immune response) that is recognized by an antibody, B-cell receptor, or T-cell receptor. It is also commonly referred to as an antigenic determinant. Epitopes are typically composed of linear amino acid sequences or conformational structures made up of discontinuous amino acids in the antigen. They play a crucial role in the immune system's ability to differentiate between self and non-self molecules, leading to the targeted destruction of foreign substances like viruses and bacteria. Understanding epitopes is essential for developing vaccines, diagnostic tests, and immunotherapies.
Methylmalonyl-CoA decarboxylase is a mitochondrial enzyme that plays a crucial role in the metabolism of certain amino acids and fatty acids. Specifically, it catalyzes the conversion of methylmalonyl-CoA to propionyl-CoA through the decarboxylation of the thioester bond.
The reaction is as follows:
Methylmalonyl-CoA → Propionyl-CoA + CO2
This enzyme requires biotin as a cofactor, and its activity is reduced in individuals with methylmalonic acidemia, a rare inherited metabolic disorder caused by mutations in the MMAB or MCEE genes that encode subunits of the methylmalonyl-CoA decarboxylase enzyme complex.
Deficiency of this enzyme leads to an accumulation of methylmalonic acid and methylmalonyl-CoA, which can cause metabolic acidosis, hyperammonemia, and other symptoms associated with the disorder.
'Antibodies, Neoplasm' is a medical term that refers to abnormal antibodies produced by neoplastic cells, which are cells that have undergone uncontrolled division and form a tumor or malignancy. These antibodies can be produced in large quantities and may have altered structures or functions compared to normal antibodies.
Neoplastic antibodies can arise from various types of malignancies, including leukemias, lymphomas, and multiple myeloma. In some cases, these abnormal antibodies can interfere with the normal functioning of the immune system and contribute to the progression of the disease.
In addition, neoplastic antibodies can also be used as tumor markers for diagnostic purposes. For example, certain types of monoclonal gammopathy, such as multiple myeloma, are characterized by the overproduction of a single type of immunoglobulin, which can be detected in the blood or urine and used to monitor the disease.
Overall, 'Antibodies, Neoplasm' is a term that encompasses a wide range of abnormal antibodies produced by neoplastic cells, which can have significant implications for both the diagnosis and treatment of malignancies.
Antibodies, protozoan, refer to the immune system's response to an infection caused by a protozoan organism. Protozoa are single-celled microorganisms that can cause various diseases in humans, such as malaria, giardiasis, and toxoplasmosis.
When the body is infected with a protozoan, the immune system responds by producing specific proteins called antibodies. Antibodies are produced by a type of white blood cell called a B-cell, and they recognize and bind to specific antigens on the surface of the protozoan organism.
There are five main types of antibodies: IgA, IgD, IgE, IgG, and IgM. Each type of antibody has a different role in the immune response. For example, IgG is the most common type of antibody and provides long-term immunity to previously encountered pathogens. IgM is the first antibody produced in response to an infection and is important for activating the complement system, which helps to destroy the protozoan organism.
Overall, the production of antibodies against protozoan organisms is a critical part of the immune response and helps to protect the body from further infection.
Antinuclear antibodies (ANA) are a type of autoantibody that target structures found in the nucleus of a cell. These antibodies are produced by the immune system and attack the body's own cells and tissues, leading to inflammation and damage. The presence of ANA is often used as a marker for certain autoimmune diseases, such as systemic lupus erythematosus (SLE), Sjogren's syndrome, rheumatoid arthritis, scleroderma, and polymyositis.
ANA can be detected through a blood test called the antinuclear antibody test. A positive result indicates the presence of ANA in the blood, but it does not necessarily mean that a person has an autoimmune disease. Further testing is usually needed to confirm a diagnosis and determine the specific type of autoantibodies present.
It's important to note that ANA can also be found in healthy individuals, particularly as they age. Therefore, the test results should be interpreted in conjunction with other clinical findings and symptoms.
Cross reactions, in the context of medical diagnostics and immunology, refer to a situation where an antibody or a immune response directed against one antigen also reacts with a different antigen due to similarities in their molecular structure. This can occur in allergy testing, where a person who is allergic to a particular substance may have a positive test result for a different but related substance because of cross-reactivity between them. For example, some individuals who are allergic to birch pollen may also have symptoms when eating certain fruits, such as apples, due to cross-reactive proteins present in both.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
Immunoglobulin M (IgM) is a type of antibody that is primarily found in the blood and lymph fluid. It is the first antibody to be produced in response to an initial exposure to an antigen, making it an important part of the body's primary immune response. IgM antibodies are large molecules that are composed of five basic units, giving them a pentameric structure. They are primarily found on the surface of B cells as membrane-bound immunoglobulins (mlgM), where they function as receptors for antigens. Once an mlgM receptor binds to an antigen, it triggers the activation and differentiation of the B cell into a plasma cell that produces and secretes large amounts of soluble IgM antibodies.
IgM antibodies are particularly effective at agglutination (clumping) and complement activation, which makes them important in the early stages of an immune response to help clear pathogens from the bloodstream. However, they are not as stable or long-lived as other types of antibodies, such as IgG, and their levels tend to decline after the initial immune response has occurred.
In summary, Immunoglobulin M (IgM) is a type of antibody that plays a crucial role in the primary immune response to antigens by agglutination and complement activation. It is primarily found in the blood and lymph fluid, and it is produced by B cells after they are activated by an antigen.
Autoantibodies are defined as antibodies that are produced by the immune system and target the body's own cells, tissues, or organs. These antibodies mistakenly identify certain proteins or molecules in the body as foreign invaders and attack them, leading to an autoimmune response. Autoantibodies can be found in various autoimmune diseases such as rheumatoid arthritis, lupus, and thyroiditis. The presence of autoantibodies can also be used as a diagnostic marker for certain conditions.
Fungal antibodies are a type of protein called immunoglobulins that are produced by the immune system in response to the presence of fungi in the body. These antibodies are specifically designed to recognize and bind to antigens on the surface of fungal cells, marking them for destruction by other immune cells.
There are several types of fungal antibodies, including IgA, IgG, IgM, and IgE, each with a specific role in the immune response. For example, IgG antibodies are the most common type of antibody found in the blood and provide long-term immunity to fungi, while IgE antibodies are associated with allergic reactions to fungi.
Fungal antibodies can be measured in the blood or other bodily fluids to help diagnose fungal infections, monitor the effectiveness of treatment, or assess immune function in individuals who are at risk for fungal infections, such as those with weakened immune systems due to HIV/AIDS, cancer, or organ transplantation.
Pyruvate carboxylase is a biotin-containing enzyme that plays a crucial role in gluconeogenesis, the process of generating new glucose molecules from non-carbohydrate sources. The enzyme catalyzes the conversion of pyruvate to oxaloacetate, an important intermediate in several metabolic pathways, particularly in the liver, kidneys, and brain.
The reaction catalyzed by pyruvate carboxylase is as follows:
Pyruvate + CO2 + ATP + H2O → Oxaloacetate + ADP + Pi + 2H+
In this reaction, pyruvate reacts with bicarbonate (HCO3-) to form oxaloacetate, consuming one molecule of ATP in the process. The generation of oxaloacetate provides a key entry point for non-carbohydrate precursors, such as lactate and certain amino acids, to enter the gluconeogenic pathway.
Pyruvate carboxylase deficiency is a rare but severe genetic disorder that can lead to neurological impairment and developmental delays due to the disruption of energy metabolism in the brain.
Neutralization tests are a type of laboratory assay used in microbiology and immunology to measure the ability of a substance, such as an antibody or antitoxin, to neutralize the activity of a toxin or infectious agent. In these tests, the substance to be tested is mixed with a known quantity of the toxin or infectious agent, and the mixture is then incubated under controlled conditions. After incubation, the mixture is tested for residual toxicity or infectivity using a variety of methods, such as cell culture assays, animal models, or biochemical assays.
The neutralization titer is then calculated based on the highest dilution of the test substance that completely neutralizes the toxin or infectious agent. Neutralization tests are commonly used in the diagnosis and evaluation of immune responses to vaccines, as well as in the detection and quantification of toxins and other harmful substances.
Examples of neutralization tests include the serum neutralization test for measles antibodies, the plaque reduction neutralization test (PRNT) for dengue virus antibodies, and the cytotoxicity neutralization assay for botulinum neurotoxins.
Sulfurtransferases are a group of enzymes that catalyze the transfer of a sulfur group from one molecule to another. These enzymes play a crucial role in various biological processes, including the detoxification of harmful compounds and the synthesis of important metabolites. They can be found in many organisms, from bacteria to humans.
In humans, there are several types of sulfurtransferases, including cysteine conjugate beta-lyase, rhodanese, and 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase. These enzymes have different substrates and functions, but they all share the ability to transfer a sulfur group from one molecule to another.
For example, rhodanese is an enzyme that transfers a sulfur atom from thiosulfate to cyanide, converting it to less toxic thiocyanate. This reaction is important in the detoxification of cyanide in the body.
Sulfurtransferases are also involved in the synthesis of various metabolites, such as iron-sulfur clusters and molybdenum cofactor, which are essential for the function of many enzymes.
Deficiencies or mutations in sulfurtransferase genes can lead to various diseases and disorders, highlighting their importance in human health.
An antigen-antibody reaction is a specific immune response that occurs when an antigen (a foreign substance, such as a protein or polysaccharide on the surface of a bacterium or virus) comes into contact with a corresponding antibody (a protective protein produced by the immune system in response to the antigen). The antigen and antibody bind together, forming an antigen-antibody complex. This interaction can neutralize the harmful effects of the antigen, mark it for destruction by other immune cells, or activate complement proteins to help eliminate the antigen from the body. Antigen-antibody reactions are a crucial part of the adaptive immune response and play a key role in the body's defense against infection and disease.
Bispecific antibodies are a type of artificial protein that have been engineered to recognize and bind to two different antigens simultaneously. They are created by combining two separate antibody molecules, each with a unique binding site, into a single entity. This allows the bispecific antibody to link two cells or proteins together, bringing them into close proximity and facilitating various biological processes.
In the context of medicine and immunotherapy, bispecific antibodies are being investigated as a potential treatment for cancer and other diseases. For example, a bispecific antibody can be designed to recognize a specific tumor-associated antigen on the surface of cancer cells, while also binding to a component of the immune system, such as a T cell. This brings the T cell into close contact with the cancer cell, activating the immune system and triggering an immune response against the tumor.
Bispecific antibodies have several potential advantages over traditional monoclonal antibodies, which only recognize a single antigen. By targeting two different epitopes or antigens, bispecific antibodies can increase the specificity and affinity of the interaction, reducing off-target effects and improving therapeutic efficacy. Additionally, bispecific antibodies can bring together multiple components of the immune system, amplifying the immune response and enhancing the destruction of cancer cells.
Overall, bispecific antibodies represent a promising new class of therapeutics that have the potential to revolutionize the treatment of cancer and other diseases. However, further research is needed to fully understand their mechanisms of action and optimize their clinical use.
BALB/c is an inbred strain of laboratory mouse that is widely used in biomedical research. The strain was developed at the Institute of Cancer Research in London by Henry Baldwin and his colleagues in the 1920s, and it has since become one of the most commonly used inbred strains in the world.
BALB/c mice are characterized by their black coat color, which is determined by a recessive allele at the tyrosinase locus. They are also known for their docile and friendly temperament, making them easy to handle and work with in the laboratory.
One of the key features of BALB/c mice that makes them useful for research is their susceptibility to certain types of tumors and immune responses. For example, they are highly susceptible to developing mammary tumors, which can be induced by chemical carcinogens or viral infection. They also have a strong Th2-biased immune response, which makes them useful models for studying allergic diseases and asthma.
BALB/c mice are also commonly used in studies of genetics, neuroscience, behavior, and infectious diseases. Because they are an inbred strain, they have a uniform genetic background, which makes it easier to control for genetic factors in experiments. Additionally, because they have been bred in the laboratory for many generations, they are highly standardized and reproducible, making them ideal subjects for scientific research.
"Valerates" is not a recognized medical term. However, it may refer to a salt or ester of valeric acid, which is a carboxylic acid with the formula CH3CH2CH2CO2H. Valeric acid and its salts and esters are used in pharmaceuticals and perfumes. Valerates can have a sedative effect and are sometimes used as a treatment for anxiety or insomnia. One example is sodium valerate, which is used in the manufacture of some types of medical-grade polyester. Another example is diethyl valerate, an ester of valeric acid that is used as a flavoring agent and solvent.
Single-chain antibodies (scFvs) are small, artificial protein molecules that contain the antigen-binding sites of immunoglobulins. They are formed by linking the variable regions of the heavy and light chains of an antibody via a flexible peptide linker, creating a single polypeptide chain. This design allows scFvs to maintain the specificity of traditional antibodies while being significantly smaller in size, more stable, and easier to produce. They have various applications in research, diagnostics, and therapeutics, including targeted drug delivery, tumor imaging, and the development of novel therapies for cancer and other diseases.
Blocking antibodies are a type of antibody that binds to a specific antigen but does not cause the immune system to directly attack the antigen. Instead, blocking antibodies prevent the antigen from interacting with other molecules or receptors, effectively "blocking" its activity. This can be useful in therapeutic settings, where blocking antibodies can be used to inhibit the activity of harmful proteins or toxins.
For example, some blocking antibodies have been developed to target and block the activity of specific cytokines, which are signaling molecules involved in inflammation and immune responses. By blocking the interaction between the cytokine and its receptor, these antibodies can help to reduce inflammation and alleviate symptoms in certain autoimmune diseases or chronic inflammatory conditions.
It's important to note that while blocking antibodies can be useful for therapeutic purposes, they can also have unintended consequences if they block the activity of essential proteins or molecules. Therefore, careful consideration and testing are required before using blocking antibodies as a treatment.
Immunoglobulin G (IgG) is a type of antibody, which is a protective protein produced by the immune system in response to foreign substances like bacteria or viruses. IgG is the most abundant type of antibody in human blood, making up about 75-80% of all antibodies. It is found in all body fluids and plays a crucial role in fighting infections caused by bacteria, viruses, and toxins.
IgG has several important functions:
1. Neutralization: IgG can bind to the surface of bacteria or viruses, preventing them from attaching to and infecting human cells.
2. Opsonization: IgG coats the surface of pathogens, making them more recognizable and easier for immune cells like neutrophils and macrophages to phagocytose (engulf and destroy) them.
3. Complement activation: IgG can activate the complement system, a group of proteins that work together to help eliminate pathogens from the body. Activation of the complement system leads to the formation of the membrane attack complex, which creates holes in the cell membranes of bacteria, leading to their lysis (destruction).
4. Antibody-dependent cellular cytotoxicity (ADCC): IgG can bind to immune cells like natural killer (NK) cells and trigger them to release substances that cause target cells (such as virus-infected or cancerous cells) to undergo apoptosis (programmed cell death).
5. Immune complex formation: IgG can form immune complexes with antigens, which can then be removed from the body through various mechanisms, such as phagocytosis by immune cells or excretion in urine.
IgG is a critical component of adaptive immunity and provides long-lasting protection against reinfection with many pathogens. It has four subclasses (IgG1, IgG2, IgG3, and IgG4) that differ in their structure, function, and distribution in the body.
Biotinidase is an enzyme that is responsible for the release of biotin, a vital nutrient, from proteins in the body. Biotin is essential for various metabolic processes, including the synthesis of fatty acids and glucose. Biotinidase deficiency can lead to serious health problems, such as seizures, developmental delays, and hearing and vision loss. Therefore, biotinidase levels are often measured in newborn screening tests to identify babies who may be at risk for this rare but treatable condition.
An antigen-antibody complex is a type of immune complex that forms when an antibody binds to a specific antigen. An antigen is any substance that triggers an immune response, while an antibody is a protein produced by the immune system to neutralize or destroy foreign substances like antigens.
When an antibody binds to an antigen, it forms a complex that can be either soluble or insoluble. Soluble complexes are formed when the antigen is small and can move freely through the bloodstream. Insoluble complexes, on the other hand, are formed when the antigen is too large to move freely, such as when it is part of a bacterium or virus.
The formation of antigen-antibody complexes plays an important role in the immune response. Once formed, these complexes can be recognized and cleared by other components of the immune system, such as phagocytes, which help to prevent further damage to the body. However, in some cases, the formation of large numbers of antigen-antibody complexes can lead to inflammation and tissue damage, contributing to the development of certain autoimmune diseases.
Immunoglobulin (Ig) Fab fragments are the antigen-binding portions of an antibody that result from the digestion of the whole antibody molecule by enzymes such as papain. An antibody, also known as an immunoglobulin, is a Y-shaped protein produced by the immune system to identify and neutralize foreign substances like bacteria, viruses, or toxins. The antibody has two identical antigen-binding sites, located at the tips of the two shorter arms, which can bind specifically to a target antigen.
Fab fragments are formed when an antibody is cleaved by papain, resulting in two Fab fragments and one Fc fragment. Each Fab fragment contains one antigen-binding site, composed of a variable region (Fv) and a constant region (C). The Fv region is responsible for the specificity and affinity of the antigen binding, while the C region contributes to the effector functions of the antibody.
Fab fragments are often used in various medical applications, such as immunodiagnostics and targeted therapies, due to their ability to bind specifically to target antigens without triggering an immune response or other effector functions associated with the Fc region.
Carbon-carbon ligases are a type of enzyme that catalyze the formation of carbon-carbon bonds between two molecules. These enzymes play important roles in various biological processes, including the biosynthesis of natural products and the metabolism of carbohydrates and lipids.
Carbon-carbon ligases can be classified into several categories based on the type of reaction they catalyze. For example, aldolases catalyze the condensation of an aldehyde or ketone with another molecule to form a new carbon-carbon bond and a new carbonyl group. Other examples include the polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs), which are large multienzyme complexes that catalyze the sequential addition of activated carbon units to form complex natural products.
Carbon-carbon ligases are important targets for drug discovery and development, as they play critical roles in the biosynthesis of many disease-relevant molecules. Inhibitors of these enzymes have shown promise as potential therapeutic agents for a variety of diseases, including cancer, infectious diseases, and metabolic disorders.
Heterophile antibodies are a type of antibody that can react with antigens from more than one source, rather than being specific to a single antigen. They are produced in response to an initial infection or immunization, but can also cross-react with antigens from unrelated organisms or substances. A common example of heterophile antibodies are those that are produced in response to Epstein-Barr virus (EBV) infection, which can cause infectious mononucleosis. These antibodies, known as Paul-Bunnell antibodies, can agglutinate (clump together) sheep or horse red blood cells, which is the basis for a diagnostic test for EBV infection called the Monospot test. However, it's important to note that not all cases of infectious mononucleosis are caused by EBV, and other infections or conditions can also cause the production of heterophile antibodies, leading to false-positive results.
Catalytic antibodies, also known as abzymes or catalytic immune proteins, are a type of antibody that possesses enzymatic activity. They are capable of accelerating specific chemical reactions in a manner similar to traditional enzymes. This unique property arises from the ability of certain antibodies to bind substrates and promote their conversion into products through a series of chemical transformations.
Catalytic antibodies are generated by immunizing an organism with a transition state analogue, a molecule that mimics the high-energy, transient structure of a substrate during a chemical reaction. The immune system recognizes this analogue as foreign and produces antibodies against it. Some of these antibodies will bind to the transition state analogue in a way that stabilizes its geometry and lowers the energy barrier for the conversion of the substrate into the product. This results in the formation of a catalytic antibody, which can then accelerate this specific chemical reaction when presented with the appropriate substrate.
These specialized antibodies have attracted significant interest in the fields of chemistry, biochemistry, and immunology due to their potential applications in various areas, including drug design, diagnostics, and environmental monitoring. However, it is important to note that catalytic antibodies are still a subject of ongoing research, and their use as practical tools in these applications is not yet widespread.
I believe there may be some confusion in your question. "Rabbits" is a common name used to refer to the Lagomorpha species, particularly members of the family Leporidae. They are small mammals known for their long ears, strong legs, and quick reproduction.
However, if you're referring to "rabbits" in a medical context, there is a term called "rabbit syndrome," which is a rare movement disorder characterized by repetitive, involuntary movements of the fingers, resembling those of a rabbit chewing. It is also known as "finger-chewing chorea." This condition is usually associated with certain medications, particularly antipsychotics, and typically resolves when the medication is stopped or adjusted.
Acetyl-CoA carboxylase (ACCA) is a biotin-dependent enzyme that plays a crucial role in fatty acid synthesis. It catalyzes the conversion of acetyl-CoA to malonyl-CoA, which is the first and rate-limiting step in the synthesis of long-chain fatty acids. The reaction catalyzed by ACCA is as follows:
acetyl-CoA + HCO3- + ATP + 2H+ --> malonyl-CoA + CoA + ADP + Pi + 2H2O
ACCA exists in two isoforms, a cytosolic form (ACC1) and a mitochondrial form (ACC2). ACC1 is primarily involved in fatty acid synthesis, while ACC2 is responsible for the regulation of fatty acid oxidation. The activity of ACCA is regulated by several factors, including phosphorylation/dephosphorylation, allosteric regulation, and transcriptional regulation. Dysregulation of ACCA has been implicated in various metabolic disorders, such as obesity, insulin resistance, and non-alcoholic fatty liver disease.
Immunoglobulin A (IgA) is a type of antibody that plays a crucial role in the immune function of the human body. It is primarily found in external secretions, such as saliva, tears, breast milk, and sweat, as well as in mucous membranes lining the respiratory and gastrointestinal tracts. IgA exists in two forms: a monomeric form found in serum and a polymeric form found in secretions.
The primary function of IgA is to provide immune protection at mucosal surfaces, which are exposed to various environmental antigens, such as bacteria, viruses, parasites, and allergens. By doing so, it helps prevent the entry and colonization of pathogens into the body, reducing the risk of infections and inflammation.
IgA functions by binding to antigens present on the surface of pathogens or allergens, forming immune complexes that can neutralize their activity. These complexes are then transported across the epithelial cells lining mucosal surfaces and released into the lumen, where they prevent the adherence and invasion of pathogens.
In summary, Immunoglobulin A (IgA) is a vital antibody that provides immune defense at mucosal surfaces by neutralizing and preventing the entry of harmful antigens into the body.
Monoclonal antibodies are laboratory-produced proteins that mimic the immune system's ability to fight off harmful antigens such as viruses and cancer cells. They are created by fusing a single B cell (the type of white blood cell responsible for producing antibodies) with a tumor cell, resulting in a hybrid cell called a hybridoma. This hybridoma can then be cloned to produce a large number of identical cells, all producing the same antibody, hence "monoclonal."
Humanized monoclonal antibodies are a type of monoclonal antibody that have been genetically engineered to include human components. This is done to reduce the risk of an adverse immune response in patients receiving the treatment. In this process, the variable region of the mouse monoclonal antibody, which contains the antigen-binding site, is grafted onto a human constant region. The resulting humanized monoclonal antibody retains the ability to bind to the target antigen while minimizing the immunogenicity associated with murine (mouse) antibodies.
In summary, "antibodies, monoclonal, humanized" refers to a type of laboratory-produced protein that mimics the immune system's ability to fight off harmful antigens, but with reduced immunogenicity due to the inclusion of human components in their structure.
The Fluorescent Antibody Technique (FAT), Indirect is a type of immunofluorescence assay used to detect the presence of specific antigens in a sample. In this method, the sample is first incubated with a primary antibody that binds to the target antigen. After washing to remove unbound primary antibodies, a secondary fluorescently labeled antibody is added, which recognizes and binds to the primary antibody. This indirect labeling approach allows for amplification of the signal, making it more sensitive than direct methods. The sample is then examined under a fluorescence microscope to visualize the location and amount of antigen based on the emitted light from the fluorescent secondary antibody. It's commonly used in diagnostic laboratories for detection of various bacteria, viruses, and other antigens in clinical specimens.
Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.
Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.
The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.
Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.
Fatty acid synthase type II (FASN2) is an alternative form of fatty acid synthase, which is a multi-functional enzyme complex responsible for the de novo synthesis of palmitate, a 16-carbon saturated fatty acid. In contrast to the classical type I fatty acid synthase (FASN), which is found in the cytoplasm and exists as a homodimer, FASN2 is localized in the mitochondria and consists of individual, monofunctional enzymes that catalyze each step of the fatty acid synthesis process.
The type II fatty acid synthase system includes several enzymes: acetyl-CoA carboxylase (ACC), which provides malonyl-CoA; 3-ketoacyl-CoA thiolase, which catalyzes the initial condensation of acetyl-CoA and malonyl-CoA to form acetoacetyl-CoA; 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase (HAD), which catalyzes the reduction, dehydration, and isomerization of acetoacetyl-CoA to form hydroxybutyryl-CoA; 3-ketoacyl-CoA reductase, which reduces hydroxybutyryl-CoA to butyryl-CoA; and enoyl-CoA reductase (ECR), which catalyzes the final reduction of butyryl-CoA to palmitate.
FASN2 is involved in various cellular processes, including energy metabolism, lipid biosynthesis, and protein acetylation. Dysregulation of FASN2 has been implicated in several diseases, such as cancer, obesity, and neurodegenerative disorders.
Carboxyl transferases and carbamoyl transferases are two types of enzymes that play a crucial role in various metabolic pathways by transferring a carboxyl or carbamoyl group from one molecule to another. Here are the medical definitions for both:
1. Carboxyl Transferases: These are a class of enzymes that catalyze the transfer of a carboxyl group (-COOH) from one molecule to another. They play an essential role in several metabolic processes, such as the synthesis and degradation of amino acids, carbohydrates, lipids, and other biomolecules. One example of a carboxyl transferase is pyruvate carboxylase, which catalyzes the addition of a carboxyl group to pyruvate, forming oxaloacetate in the gluconeogenesis pathway.
2. Carbamoyl Transferases: These are enzymes that facilitate the transfer of a carbamoyl group (-CONH2) from one molecule to another. They participate in various metabolic reactions, including the synthesis of essential compounds like arginine, pyrimidines, and urea. An example of a carbamoyl transferase is ornithine carbamoyltransferase (OCT), which catalyzes the transfer of a carbamoyl group from carbamoyl phosphate to ornithine during the urea cycle.
Both carboxyl and carbamoyl transferases are vital for maintaining proper cellular function and homeostasis in living organisms, including humans. Dysregulation or deficiency of these enzymes can lead to various metabolic disorders and diseases.
A hybridoma is a type of hybrid cell that is created in a laboratory by fusing a cancer cell (usually a B cell) with a normal immune cell. The resulting hybrid cell combines the ability of the cancer cell to grow and divide indefinitely with the ability of the immune cell to produce antibodies, which are proteins that help the body fight infection.
Hybridomas are commonly used to produce monoclonal antibodies, which are identical copies of a single antibody produced by a single clone of cells. These antibodies can be used for a variety of purposes, including diagnostic tests and treatments for diseases such as cancer and autoimmune disorders.
To create hybridomas, B cells are first isolated from the spleen or blood of an animal that has been immunized with a specific antigen (a substance that triggers an immune response). The B cells are then fused with cancer cells using a chemical agent such as polyethylene glycol. The resulting hybrid cells are called hybridomas and are grown in culture medium, where they can be selected for their ability to produce antibodies specific to the antigen of interest. These antibody-producing hybridomas can then be cloned to produce large quantities of monoclonal antibodies.
'Immune sera' refers to the serum fraction of blood that contains antibodies produced in response to an antigenic stimulus, such as a vaccine or an infection. These antibodies are proteins known as immunoglobulins, which are secreted by B cells (a type of white blood cell) and can recognize and bind to specific antigens. Immune sera can be collected from an immunized individual and used as a source of passive immunity to protect against infection or disease. It is often used in research and diagnostic settings to identify or measure the presence of specific antigens or antibodies.
A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.
Epitope mapping is a technique used in immunology to identify the specific portion or regions (called epitopes) on an antigen that are recognized and bind to antibodies or T-cell receptors. This process helps to understand the molecular basis of immune responses against various pathogens, allergens, or transplanted tissues.
Epitope mapping can be performed using different methods such as:
1. Peptide scanning: In this method, a series of overlapping peptides spanning the entire length of the antigen are synthesized and tested for their ability to bind to antibodies or T-cell receptors. The peptide that shows binding is considered to contain the epitope.
2. Site-directed mutagenesis: In this approach, specific amino acids within the antigen are altered, and the modified antigens are tested for their ability to bind to antibodies or T-cell receptors. This helps in identifying the critical residues within the epitope.
3. X-ray crystallography and NMR spectroscopy: These techniques provide detailed information about the three-dimensional structure of antigen-antibody complexes, allowing for accurate identification of epitopes at an atomic level.
The results from epitope mapping can be useful in various applications, including vaccine design, diagnostic test development, and understanding the basis of autoimmune diseases.
Immunoenzyme techniques are a group of laboratory methods used in immunology and clinical chemistry that combine the specificity of antibody-antigen reactions with the sensitivity and amplification capabilities of enzyme reactions. These techniques are primarily used for the detection, quantitation, or identification of various analytes (such as proteins, hormones, drugs, viruses, or bacteria) in biological samples.
In immunoenzyme techniques, an enzyme is linked to an antibody or antigen, creating a conjugate. This conjugate then interacts with the target analyte in the sample, forming an immune complex. The presence and amount of this immune complex can be visualized or measured by detecting the enzymatic activity associated with it.
There are several types of immunoenzyme techniques, including:
1. Enzyme-linked Immunosorbent Assay (ELISA): A widely used method for detecting and quantifying various analytes in a sample. In ELISA, an enzyme is attached to either the capture antibody or the detection antibody. After the immune complex formation, a substrate is added that reacts with the enzyme, producing a colored product that can be measured spectrophotometrically.
2. Immunoblotting (Western blot): A method used for detecting specific proteins in a complex mixture, such as a protein extract from cells or tissues. In this technique, proteins are separated by gel electrophoresis and transferred to a membrane, where they are probed with an enzyme-conjugated antibody directed against the target protein.
3. Immunohistochemistry (IHC): A method used for detecting specific antigens in tissue sections or cells. In IHC, an enzyme-conjugated primary or secondary antibody is applied to the sample, and the presence of the antigen is visualized using a chromogenic substrate that produces a colored product at the site of the antigen-antibody interaction.
4. Immunofluorescence (IF): A method used for detecting specific antigens in cells or tissues by employing fluorophore-conjugated antibodies. The presence of the antigen is visualized using a fluorescence microscope.
5. Enzyme-linked immunosorbent assay (ELISA): A method used for detecting and quantifying specific antigens or antibodies in liquid samples, such as serum or culture supernatants. In ELISA, an enzyme-conjugated detection antibody is added after the immune complex formation, and a substrate is added that reacts with the enzyme to produce a colored product that can be measured spectrophotometrically.
These techniques are widely used in research and diagnostic laboratories for various applications, including protein characterization, disease diagnosis, and monitoring treatment responses.
Antiphospholipid antibodies are a type of autoantibody that targets and binds to certain proteins found in the blood that attach to phospholipids (a type of fat molecule). These antibodies are associated with an increased risk of developing antiphospholipid syndrome, a disorder characterized by abnormal blood clotting.
There are several types of antiphospholipid antibodies, including:
1. Lupus anticoagulant: This type of antiphospholipid antibody can interfere with blood clotting tests and may increase the risk of thrombosis (blood clots) in both arteries and veins.
2. Anticardiolipin antibodies: These antibodies target a specific phospholipid called cardiolipin, which is found in the inner membrane of mitochondria. High levels of anticardiolipin antibodies are associated with an increased risk of thrombosis and pregnancy complications such as recurrent miscarriage.
3. Anti-β2 glycoprotein I antibodies: These antibodies target a protein called β2 glycoprotein I, which binds to negatively charged phospholipids on the surface of cells. High levels of anti-β2 glycoprotein I antibodies are associated with an increased risk of thrombosis and pregnancy complications.
The exact mechanism by which antiphospholipid antibodies cause blood clotting is not fully understood, but it is thought to involve the activation of platelets, the inhibition of natural anticoagulants, and the promotion of inflammation. Antiphospholipid syndrome can be treated with medications that thin the blood or prevent clots from forming, such as aspirin, warfarin, or heparin.
Immunization is defined medically as the process where an individual is made immune or resistant to an infectious disease, typically through the administration of a vaccine. The vaccine stimulates the body's own immune system to recognize and fight off the specific disease-causing organism, thereby preventing or reducing the severity of future infections with that organism.
Immunization can be achieved actively, where the person is given a vaccine to trigger an immune response, or passively, where antibodies are transferred to the person through immunoglobulin therapy. Immunizations are an important part of preventive healthcare and have been successful in controlling and eliminating many infectious diseases worldwide.
I'm sorry for any confusion, but "Pimelic Acids" is not a recognized medical term or concept in physiology, pathology, or pharmacology. It appears to be a term used in chemistry and biochemistry, referring to a specific type of organic compound known as a dicarboxylic acid with a seven-carbon backbone.
In biochemistry, pimelic acid may be involved in various metabolic processes, such as the synthesis of certain amino acids and lipids. However, it is not typically considered a medical term or diagnostic marker in clinical settings. If you're looking for information related to a specific medical condition or treatment, I would be happy to help if you could provide more context!
An antigen is a substance (usually a protein) that is recognized as foreign by the immune system and stimulates an immune response, leading to the production of antibodies or activation of T-cells. Antigens can be derived from various sources, including bacteria, viruses, fungi, parasites, and tumor cells. They can also come from non-living substances such as pollen, dust mites, or chemicals.
Antigens contain epitopes, which are specific regions on the antigen molecule that are recognized by the immune system. The immune system's response to an antigen depends on several factors, including the type of antigen, its size, and its location in the body.
In general, antigens can be classified into two main categories:
1. T-dependent antigens: These require the help of T-cells to stimulate an immune response. They are typically larger, more complex molecules that contain multiple epitopes capable of binding to both MHC class II molecules on antigen-presenting cells and T-cell receptors on CD4+ T-cells.
2. T-independent antigens: These do not require the help of T-cells to stimulate an immune response. They are usually smaller, simpler molecules that contain repetitive epitopes capable of cross-linking B-cell receptors and activating them directly.
Understanding antigens and their properties is crucial for developing vaccines, diagnostic tests, and immunotherapies.
'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.
While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.
E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.
An Enzyme-Linked Immunosorbent Assay (ELISA) is a type of analytical biochemistry assay used to detect and quantify the presence of a substance, typically a protein or peptide, in a liquid sample. It takes its name from the enzyme-linked antibodies used in the assay.
In an ELISA, the sample is added to a well containing a surface that has been treated to capture the target substance. If the target substance is present in the sample, it will bind to the surface. Next, an enzyme-linked antibody specific to the target substance is added. This antibody will bind to the captured target substance if it is present. After washing away any unbound material, a substrate for the enzyme is added. If the enzyme is present due to its linkage to the antibody, it will catalyze a reaction that produces a detectable signal, such as a color change or fluorescence. The intensity of this signal is proportional to the amount of target substance present in the sample, allowing for quantification.
ELISAs are widely used in research and clinical settings to detect and measure various substances, including hormones, viruses, and bacteria. They offer high sensitivity, specificity, and reproducibility, making them a reliable choice for many applications.
Western blotting is a laboratory technique used in molecular biology to detect and quantify specific proteins in a mixture of many different proteins. This technique is commonly used to confirm the expression of a protein of interest, determine its size, and investigate its post-translational modifications. The name "Western" blotting distinguishes this technique from Southern blotting (for DNA) and Northern blotting (for RNA).
The Western blotting procedure involves several steps:
1. Protein extraction: The sample containing the proteins of interest is first extracted, often by breaking open cells or tissues and using a buffer to extract the proteins.
2. Separation of proteins by electrophoresis: The extracted proteins are then separated based on their size by loading them onto a polyacrylamide gel and running an electric current through the gel (a process called sodium dodecyl sulfate-polyacrylamide gel electrophoresis or SDS-PAGE). This separates the proteins according to their molecular weight, with smaller proteins migrating faster than larger ones.
3. Transfer of proteins to a membrane: After separation, the proteins are transferred from the gel onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric current in a process called blotting. This creates a replica of the protein pattern on the gel but now immobilized on the membrane for further analysis.
4. Blocking: The membrane is then blocked with a blocking agent, such as non-fat dry milk or bovine serum albumin (BSA), to prevent non-specific binding of antibodies in subsequent steps.
5. Primary antibody incubation: A primary antibody that specifically recognizes the protein of interest is added and allowed to bind to its target protein on the membrane. This step may be performed at room temperature or 4°C overnight, depending on the antibody's properties.
6. Washing: The membrane is washed with a buffer to remove unbound primary antibodies.
7. Secondary antibody incubation: A secondary antibody that recognizes the primary antibody (often coupled to an enzyme or fluorophore) is added and allowed to bind to the primary antibody. This step may involve using a horseradish peroxidase (HRP)-conjugated or alkaline phosphatase (AP)-conjugated secondary antibody, depending on the detection method used later.
8. Washing: The membrane is washed again to remove unbound secondary antibodies.
9. Detection: A detection reagent is added to visualize the protein of interest by detecting the signal generated from the enzyme-conjugated or fluorophore-conjugated secondary antibody. This can be done using chemiluminescent, colorimetric, or fluorescent methods.
10. Analysis: The resulting image is analyzed to determine the presence and quantity of the protein of interest in the sample.
Western blotting is a powerful technique for identifying and quantifying specific proteins within complex mixtures. It can be used to study protein expression, post-translational modifications, protein-protein interactions, and more. However, it requires careful optimization and validation to ensure accurate and reproducible results.
Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.
In this process:
1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.
EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.
Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.
A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.
Surface antigens are molecules found on the surface of cells that can be recognized by the immune system as being foreign or different from the host's own cells. Antigens are typically proteins or polysaccharides that are capable of stimulating an immune response, leading to the production of antibodies and activation of immune cells such as T-cells.
Surface antigens are important in the context of infectious diseases because they allow the immune system to identify and target infected cells for destruction. For example, viruses and bacteria often display surface antigens that are distinct from those found on host cells, allowing the immune system to recognize and attack them. In some cases, these surface antigens can also be used as targets for vaccines or other immunotherapies.
In addition to their role in infectious diseases, surface antigens are also important in the context of cancer. Tumor cells often display abnormal surface antigens that differ from those found on normal cells, allowing the immune system to potentially recognize and attack them. However, tumors can also develop mechanisms to evade the immune system, making it difficult to mount an effective response.
Overall, understanding the properties and behavior of surface antigens is crucial for developing effective immunotherapies and vaccines against infectious diseases and cancer.
Bacterial antigens are substances found on the surface or produced by bacteria that can stimulate an immune response in a host organism. These antigens can be proteins, polysaccharides, teichoic acids, lipopolysaccharides, or other molecules that are recognized as foreign by the host's immune system.
When a bacterial antigen is encountered by the host's immune system, it triggers a series of responses aimed at eliminating the bacteria and preventing infection. The host's immune system recognizes the antigen as foreign through the use of specialized receptors called pattern recognition receptors (PRRs), which are found on various immune cells such as macrophages, dendritic cells, and neutrophils.
Once a bacterial antigen is recognized by the host's immune system, it can stimulate both the innate and adaptive immune responses. The innate immune response involves the activation of inflammatory pathways, the recruitment of immune cells to the site of infection, and the production of antimicrobial peptides.
The adaptive immune response, on the other hand, involves the activation of T cells and B cells, which are specific to the bacterial antigen. These cells can recognize and remember the antigen, allowing for a more rapid and effective response upon subsequent exposures.
Bacterial antigens are important in the development of vaccines, as they can be used to stimulate an immune response without causing disease. By identifying specific bacterial antigens that are associated with virulence or pathogenicity, researchers can develop vaccines that target these antigens and provide protection against infection.
An immunoassay is a biochemical test that measures the presence or concentration of a specific protein, antibody, or antigen in a sample using the principles of antibody-antigen reactions. It is commonly used in clinical laboratories to diagnose and monitor various medical conditions such as infections, hormonal disorders, allergies, and cancer.
Immunoassays typically involve the use of labeled reagents, such as enzymes, radioisotopes, or fluorescent dyes, that bind specifically to the target molecule. The amount of label detected is proportional to the concentration of the target molecule in the sample, allowing for quantitative analysis.
There are several types of immunoassays, including enzyme-linked immunosorbent assay (ELISA), radioimmunoassay (RIA), fluorescence immunoassay (FIA), and chemiluminescent immunoassay (CLIA). Each type has its own advantages and limitations, depending on the sensitivity, specificity, and throughput required for a particular application.
Passive immunization is a type of temporary immunity that is transferred to an individual through the injection of antibodies produced outside of the body, rather than through the active production of antibodies in the body in response to vaccination or infection. This can be done through the administration of preformed antibodies, such as immune globulins, which contain a mixture of antibodies that provide immediate protection against specific diseases.
Passive immunization is often used in situations where individuals have been exposed to a disease and do not have time to develop their own active immune response, or in cases where individuals are unable to produce an adequate immune response due to certain medical conditions. It can also be used as a short-term measure to provide protection until an individual can receive a vaccination that will confer long-term immunity.
Passive immunization provides immediate protection against disease, but the protection is typically short-lived, lasting only a few weeks or months. This is because the transferred antibodies are gradually broken down and eliminated by the body over time. In contrast, active immunization confers long-term immunity through the production of memory cells that can mount a rapid and effective immune response upon re-exposure to the same pathogen in the future.
Immunohistochemistry (IHC) is a technique used in pathology and laboratory medicine to identify specific proteins or antigens in tissue sections. It combines the principles of immunology and histology to detect the presence and location of these target molecules within cells and tissues. This technique utilizes antibodies that are specific to the protein or antigen of interest, which are then tagged with a detection system such as a chromogen or fluorophore. The stained tissue sections can be examined under a microscope, allowing for the visualization and analysis of the distribution and expression patterns of the target molecule in the context of the tissue architecture. Immunohistochemistry is widely used in diagnostic pathology to help identify various diseases, including cancer, infectious diseases, and immune-mediated disorders.
"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.
Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.
It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.
Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.
In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.
Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.
I'm sorry for any confusion, but "Hoof and Claw" is not a medical term or condition. The term "hoof" refers to the hard covering on the toes of animals such as horses, cows, and other ungulates, while "claw" refers to the sharp nail-like structure found on the toes of animals such as cats, dogs, and birds.
If you have any questions related to medical terminology or health concerns, I would be happy to try to help answer them for you.
Immunoblotting, also known as western blotting, is a laboratory technique used in molecular biology and immunogenetics to detect and quantify specific proteins in a complex mixture. This technique combines the electrophoretic separation of proteins by gel electrophoresis with their detection using antibodies that recognize specific epitopes (protein fragments) on the target protein.
The process involves several steps: first, the protein sample is separated based on size through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Next, the separated proteins are transferred onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric field. The membrane is then blocked with a blocking agent to prevent non-specific binding of antibodies.
After blocking, the membrane is incubated with a primary antibody that specifically recognizes the target protein. Following this, the membrane is washed to remove unbound primary antibodies and then incubated with a secondary antibody conjugated to an enzyme such as horseradish peroxidase (HRP) or alkaline phosphatase (AP). The enzyme catalyzes a colorimetric or chemiluminescent reaction that allows for the detection of the target protein.
Immunoblotting is widely used in research and clinical settings to study protein expression, post-translational modifications, protein-protein interactions, and disease biomarkers. It provides high specificity and sensitivity, making it a valuable tool for identifying and quantifying proteins in various biological samples.
Immunoglobulin fragments refer to the smaller protein units that are formed by the digestion or break-down of an intact immunoglobulin, also known as an antibody. Immunoglobulins are large Y-shaped proteins produced by the immune system to identify and neutralize foreign substances such as pathogens or toxins. They consist of two heavy chains and two light chains, held together by disulfide bonds.
The digestion or break-down of an immunoglobulin can occur through enzymatic cleavage, which results in the formation of distinct fragments. The most common immunoglobulin fragments are:
1. Fab (Fragment, antigen binding) fragments: These are formed by the digestion of an intact immunoglobulin using the enzyme papain. Each Fab fragment contains a single antigen-binding site, consisting of a portion of one heavy chain and one light chain. The Fab fragments retain their ability to bind to specific antigens.
2. Fc (Fragment, crystallizable) fragments: These are formed by the digestion of an intact immunoglobulin using the enzyme pepsin or through the natural breakdown process in the body. The Fc fragment contains the constant region of both heavy chains and is responsible for effector functions such as complement activation, binding to Fc receptors on immune cells, and antibody-dependent cellular cytotoxicity (ADCC).
These immunoglobulin fragments play crucial roles in various immune responses and diagnostic applications. For example, Fab fragments can be used in immunoassays for the detection of specific antigens, while Fc fragments can mediate effector functions that help eliminate pathogens or damaged cells from the body.
In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."
1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.
2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.
3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.
4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).
Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.
An antigen is any substance that can stimulate an immune response, particularly the production of antibodies. Viral antigens are antigens that are found on or produced by viruses. They can be proteins, glycoproteins, or carbohydrates present on the surface or inside the viral particle.
Viral antigens play a crucial role in the immune system's recognition and response to viral infections. When a virus infects a host cell, it may display its antigens on the surface of the infected cell. This allows the immune system to recognize and target the infected cells for destruction, thereby limiting the spread of the virus.
Viral antigens are also important targets for vaccines. Vaccines typically work by introducing a harmless form of a viral antigen to the body, which then stimulates the production of antibodies and memory T-cells that can recognize and respond quickly and effectively to future infections with the actual virus.
It's worth noting that different types of viruses have different antigens, and these antigens can vary between strains of the same virus. This is why there are often different vaccines available for different viral diseases, and why flu vaccines need to be updated every year to account for changes in the circulating influenza virus strains.
Multiple carboxylase deficiency (MCD) is a rare genetic disorder that affects the body's ability to metabolize certain amino acids, particularly those that contain sulfur. It is caused by mutations in the genes responsible for producing enzymes involved in the biotin-dependent carboxylation reactions, which are critical for various metabolic processes in the body.
There are two major types of MCD:
1. Profound multiple carboxylase deficiency (also known as Type II biotinidase deficiency): This form is more severe and is caused by a defect in the holocarboxylase synthetase enzyme, which is responsible for attaching biotin to several carboxylases.
2. Biotin-responsive multiple carboxylase deficiency (also known as Type I biotinidase deficiency): This form is milder and is caused by a defect in the biotinidase enzyme, which recycles biotin in the body. However, it can be treated with biotin supplementation.
Symptoms of MCD may include:
* Developmental delay
* Seizures
* Hypotonia (low muscle tone)
* Ataxia (lack of coordination)
* Rash
* Hair loss
* Acidosis (high levels of acid in the body)
* Coma and even death, if left untreated
Early diagnosis and treatment with biotin supplementation can significantly improve outcomes for individuals with MCD.
The "egg white" is the common name for the clear, protein-rich liquid contained within an egg. In medical or scientific terms, it is known as the albumen. The albumen is composed mainly of water and proteins, including ovalbumin, conalbumin, ovomucoid, and lysozyme. It also contains small amounts of carbohydrates, vitamins, and minerals.
The egg white provides nutrition and protection for the developing embryo in fertilized eggs. In culinary uses, it is often consumed as a source of high-quality protein and is used in various dishes due to its ability to foam, gel, and bind ingredients together. It is also utilized in the production of vaccines and other medical products.
Radioimmunoassay (RIA) is a highly sensitive analytical technique used in clinical and research laboratories to measure concentrations of various substances, such as hormones, vitamins, drugs, or tumor markers, in biological samples like blood, urine, or tissues. The method relies on the specific interaction between an antibody and its corresponding antigen, combined with the use of radioisotopes to quantify the amount of bound antigen.
In a typical RIA procedure, a known quantity of a radiolabeled antigen (also called tracer) is added to a sample containing an unknown concentration of the same unlabeled antigen. The mixture is then incubated with a specific antibody that binds to the antigen. During the incubation period, the antibody forms complexes with both the radiolabeled and unlabeled antigens.
After the incubation, the unbound (free) radiolabeled antigen is separated from the antibody-antigen complexes, usually through a precipitation or separation step involving centrifugation, filtration, or chromatography. The amount of radioactivity in the pellet (containing the antibody-antigen complexes) is then measured using a gamma counter or other suitable radiation detection device.
The concentration of the unlabeled antigen in the sample can be determined by comparing the ratio of bound to free radiolabeled antigen in the sample to a standard curve generated from known concentrations of unlabeled antigen and their corresponding bound/free ratios. The higher the concentration of unlabeled antigen in the sample, the lower the amount of radiolabeled antigen that will bind to the antibody, resulting in a lower bound/free ratio.
Radioimmunoassays offer high sensitivity, specificity, and accuracy, making them valuable tools for detecting and quantifying low levels of various substances in biological samples. However, due to concerns about radiation safety and waste disposal, alternative non-isotopic immunoassay techniques like enzyme-linked immunosorbent assays (ELISAs) have become more popular in recent years.
Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.
Bacterial proteins can be classified into different categories based on their function, such as:
1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.
Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.
B-lymphocytes, also known as B-cells, are a type of white blood cell that plays a key role in the immune system's response to infection. They are responsible for producing antibodies, which are proteins that help to neutralize or destroy pathogens such as bacteria and viruses.
When a B-lymphocyte encounters a pathogen, it becomes activated and begins to divide and differentiate into plasma cells, which produce and secrete large amounts of antibodies specific to the antigens on the surface of the pathogen. These antibodies bind to the pathogen, marking it for destruction by other immune cells such as neutrophils and macrophages.
B-lymphocytes also have a role in presenting antigens to T-lymphocytes, another type of white blood cell involved in the immune response. This helps to stimulate the activation and proliferation of T-lymphocytes, which can then go on to destroy infected cells or help to coordinate the overall immune response.
Overall, B-lymphocytes are an essential part of the adaptive immune system, providing long-lasting immunity to previously encountered pathogens and helping to protect against future infections.
Complement fixation tests are a type of laboratory test used in immunology and serology to detect the presence of antibodies in a patient's serum. These tests are based on the principle of complement activation, which is a part of the immune response. The complement system consists of a group of proteins that work together to help eliminate pathogens from the body.
In a complement fixation test, the patient's serum is mixed with a known antigen and complement proteins. If the patient has antibodies against the antigen, they will bind to it and activate the complement system. This results in the consumption or "fixation" of the complement proteins, which are no longer available to participate in a secondary reaction.
A second step involves adding a fresh source of complement proteins and a dye-labeled antibody that recognizes a specific component of the complement system. If complement was fixed during the first step, it will not be available for this secondary reaction, and the dye-labeled antibody will remain unbound. Conversely, if no antibodies were present in the patient's serum, the complement proteins would still be available for the second reaction, leading to the binding of the dye-labeled antibody.
The mixture is then examined under a microscope or using a spectrophotometer to determine whether the dye-labeled antibody has bound. If it has not, this indicates that the patient's serum contains antibodies specific to the antigen used in the test, and a positive result is recorded.
Complement fixation tests have been widely used for the diagnosis of various infectious diseases, such as syphilis, measles, and influenza. However, they have largely been replaced by more modern serological techniques, like enzyme-linked immunosorbent assays (ELISAs) and nucleic acid amplification tests (NAATs), due to their increased sensitivity, specificity, and ease of use.
"Competitive binding" is a term used in pharmacology and biochemistry to describe the behavior of two or more molecules (ligands) competing for the same binding site on a target protein or receptor. In this context, "binding" refers to the physical interaction between a ligand and its target.
When a ligand binds to a receptor, it can alter the receptor's function, either activating or inhibiting it. If multiple ligands compete for the same binding site, they will compete to bind to the receptor. The ability of each ligand to bind to the receptor is influenced by its affinity for the receptor, which is a measure of how strongly and specifically the ligand binds to the receptor.
In competitive binding, if one ligand is present in high concentrations, it can prevent other ligands with lower affinity from binding to the receptor. This is because the higher-affinity ligand will have a greater probability of occupying the binding site and blocking access to the other ligands. The competition between ligands can be described mathematically using equations such as the Langmuir isotherm, which describes the relationship between the concentration of ligand and the fraction of receptors that are occupied by the ligand.
Competitive binding is an important concept in drug development, as it can be used to predict how different drugs will interact with their targets and how they may affect each other's activity. By understanding the competitive binding properties of a drug, researchers can optimize its dosage and delivery to maximize its therapeutic effect while minimizing unwanted side effects.
A peptide library is a collection of a large number of peptides, which are short chains of amino acids. Each peptide in the library is typically composed of a defined length and sequence, and may contain a variety of different amino acids. Peptide libraries can be synthesized using automated techniques and are often used in scientific research to identify potential ligands (molecules that bind to specific targets) or to study the interactions between peptides and other molecules.
In a peptide library, each peptide is usually attached to a solid support, such as a resin bead, and the entire library can be created using split-and-pool synthesis techniques. This allows for the rapid and efficient synthesis of a large number of unique peptides, which can then be screened for specific activities or properties.
Peptide libraries are used in various fields such as drug discovery, proteomics, and molecular biology to identify potential therapeutic targets, understand protein-protein interactions, and develop new diagnostic tools.
In the field of medicine, "time factors" refer to the duration of symptoms or time elapsed since the onset of a medical condition, which can have significant implications for diagnosis and treatment. Understanding time factors is crucial in determining the progression of a disease, evaluating the effectiveness of treatments, and making critical decisions regarding patient care.
For example, in stroke management, "time is brain," meaning that rapid intervention within a specific time frame (usually within 4.5 hours) is essential to administering tissue plasminogen activator (tPA), a clot-busting drug that can minimize brain damage and improve patient outcomes. Similarly, in trauma care, the "golden hour" concept emphasizes the importance of providing definitive care within the first 60 minutes after injury to increase survival rates and reduce morbidity.
Time factors also play a role in monitoring the progression of chronic conditions like diabetes or heart disease, where regular follow-ups and assessments help determine appropriate treatment adjustments and prevent complications. In infectious diseases, time factors are crucial for initiating antibiotic therapy and identifying potential outbreaks to control their spread.
Overall, "time factors" encompass the significance of recognizing and acting promptly in various medical scenarios to optimize patient outcomes and provide effective care.
Immunosorbent techniques are a group of laboratory methods used in immunology and clinical chemistry to isolate or detect specific proteins, antibodies, or antigens from a complex mixture. These techniques utilize the specific binding properties of antibodies or antigens to capture and concentrate target molecules.
The most common immunosorbent technique is the Enzyme-Linked Immunosorbent Assay (ELISA), which involves coating a solid surface with a capture antibody, allowing the sample to bind, washing away unbound material, and then detecting bound antigens or antibodies using an enzyme-conjugated detection reagent. The enzyme catalyzes a colorimetric reaction that can be measured and quantified, providing a sensitive and specific assay for the target molecule.
Other immunosorbent techniques include Radioimmunoassay (RIA), Immunofluorescence Assay (IFA), and Lateral Flow Immunoassay (LFIA). These methods have wide-ranging applications in research, diagnostics, and drug development.
Hemagglutination tests are laboratory procedures used to detect the presence of antibodies or antigens in a sample, typically in blood serum. These tests rely on the ability of certain substances, such as viruses or bacteria, to agglutinate (clump together) red blood cells.
In a hemagglutination test, a small amount of the patient's serum is mixed with a known quantity of red blood cells that have been treated with a specific antigen. If the patient has antibodies against that antigen in their serum, they will bind to the antigens on the red blood cells and cause them to agglutinate. This clumping can be observed visually, indicating a positive test result.
Hemagglutination tests are commonly used to diagnose infectious diseases caused by viruses or bacteria that have hemagglutinating properties, such as influenza, parainfluenza, and HIV. They can also be used in blood typing and cross-matching before transfusions.
Hemagglutination inhibition (HI) tests are a type of serological assay used in medical laboratories to detect and measure the amount of antibodies present in a patient's serum. These tests are commonly used to diagnose viral infections, such as influenza or HIV, by identifying the presence of antibodies that bind to specific viral antigens and prevent hemagglutination (the agglutination or clumping together of red blood cells).
In an HI test, a small amount of the patient's serum is mixed with a known quantity of the viral antigen, which has been treated to attach to red blood cells. If the patient's serum contains antibodies that bind to the viral antigen, they will prevent the antigen from attaching to the red blood cells and inhibit hemagglutination. The degree of hemagglutination inhibition can be measured and used to estimate the amount of antibody present in the patient's serum.
HI tests are relatively simple and inexpensive to perform, but they have some limitations. For example, they may not detect early-stage infections before the body has had a chance to produce antibodies, and they may not be able to distinguish between different strains of the same virus. Nonetheless, HI tests remain an important tool for diagnosing viral infections and monitoring immune responses to vaccination or infection.
Antineutrophil cytoplasmic antibodies (ANCAs) are a type of autoantibody that specifically target certain proteins in the cytoplasm of neutrophils, which are a type of white blood cell. These antibodies are associated with several types of vasculitis, which is inflammation of the blood vessels.
There are two main types of ANCAs: perinuclear ANCAs (p-ANCAs) and cytoplasmic ANCAs (c-ANCAs). p-ANCAs are directed against myeloperoxidase, a protein found in neutrophil granules, while c-ANCAs target proteinase 3, another protein found in neutrophil granules.
The presence of ANCAs in the blood can indicate an increased risk for developing certain types of vasculitis, such as granulomatosis with polyangiitis (GPA), eosinophilic granulomatosis with polyangiitis (EGPA), and microscopic polyangiitis (MPA). ANCA testing is often used in conjunction with other clinical findings to help diagnose and manage these conditions.
It's important to note that while the presence of ANCAs can indicate an increased risk for vasculitis, not everyone with ANCAs will develop the condition. Additionally, ANCAs can also be found in some individuals without any associated disease, so their presence should be interpreted in the context of other clinical findings.
"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.
The Immunoglobulin (Ig) variable region is the antigen-binding part of an antibody, which is highly variable in its amino acid sequence and therefore specific to a particular epitope (the site on an antigen that is recognized by the antigen-binding site of an antibody). This variability is generated during the process of V(D)J recombination in the maturation of B cells, allowing for a diverse repertoire of antibodies to be produced and recognizing a wide range of potential pathogens.
The variable region is composed of several sub-regions including:
1. The heavy chain variable region (VH)
2. The light chain variable region (VL)
3. The heavy chain joining region (JH)
4. The light chain joining region (JL)
These regions are further divided into framework regions and complementarity-determining regions (CDRs). The CDRs, particularly CDR3, contain the most variability and are primarily responsible for antigen recognition.
Seroepidemiologic studies are a type of epidemiological study that measures the presence and levels of antibodies in a population's blood serum to investigate the prevalence, distribution, and transmission of infectious diseases. These studies help to identify patterns of infection and immunity within a population, which can inform public health policies and interventions.
Seroepidemiologic studies typically involve collecting blood samples from a representative sample of individuals in a population and testing them for the presence of antibodies against specific pathogens. The results are then analyzed to estimate the prevalence of infection and immunity within the population, as well as any factors associated with increased or decreased risk of infection.
These studies can provide valuable insights into the spread of infectious diseases, including emerging and re-emerging infections, and help to monitor the effectiveness of vaccination programs. Additionally, seroepidemiologic studies can also be used to investigate the transmission dynamics of infectious agents, such as identifying sources of infection or tracking the spread of antibiotic resistance.
Immunoglobulin idiotypes refer to the unique antigenic determinants found on the variable regions of an immunoglobulin (antibody) molecule. These determinants are specific to each individual antibody and can be used to distinguish between different antibodies produced by a single individual or between antibodies produced by different individuals.
The variable region of an antibody is responsible for recognizing and binding to a specific antigen. The amino acid sequence in this region varies between different antibodies, and it is these variations that give rise to the unique idiotypes. Idiotypes can be used as markers to study the immune response, including the clonal selection and affinity maturation of B cells during an immune response.
Immunoglobulin idiotypes are also important in the development of monoclonal antibodies for therapeutic use. By identifying and isolating a specific antibody with the desired idiotype, it is possible to produce large quantities of identical antibodies that can be used to treat various diseases, including cancer and autoimmune disorders.
Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.
The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.
Examples of recombinant fusion proteins include:
1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment
T-lymphocytes, also known as T-cells, are a type of white blood cell that plays a key role in the adaptive immune system's response to infection. They are produced in the bone marrow and mature in the thymus gland. There are several different types of T-cells, including CD4+ helper T-cells, CD8+ cytotoxic T-cells, and regulatory T-cells (Tregs).
CD4+ helper T-cells assist in activating other immune cells, such as B-lymphocytes and macrophages. They also produce cytokines, which are signaling molecules that help coordinate the immune response. CD8+ cytotoxic T-cells directly kill infected cells by releasing toxic substances. Regulatory T-cells help maintain immune tolerance and prevent autoimmune diseases by suppressing the activity of other immune cells.
T-lymphocytes are important in the immune response to viral infections, cancer, and other diseases. Dysfunction or depletion of T-cells can lead to immunodeficiency and increased susceptibility to infections. On the other hand, an overactive T-cell response can contribute to autoimmune diseases and chronic inflammation.
Immunologic techniques are a group of laboratory methods that utilize the immune system's ability to recognize and respond to specific molecules, known as antigens. These techniques are widely used in medicine, biology, and research to detect, measure, or identify various substances, including proteins, hormones, viruses, bacteria, and other antigens.
Some common immunologic techniques include:
1. Enzyme-linked Immunosorbent Assay (ELISA): A sensitive assay used to detect and quantify antigens or antibodies in a sample. This technique uses an enzyme linked to an antibody or antigen, which reacts with a substrate to produce a colored product that can be measured and quantified.
2. Immunofluorescence: A microscopic technique used to visualize the location of antigens or antibodies in tissues or cells. This technique uses fluorescent dyes conjugated to antibodies, which bind to specific antigens and emit light when excited by a specific wavelength of light.
3. Western Blotting: A laboratory technique used to detect and identify specific proteins in a sample. This technique involves separating proteins based on their size using electrophoresis, transferring them to a membrane, and then probing the membrane with antibodies that recognize the protein of interest.
4. Immunoprecipitation: A laboratory technique used to isolate and purify specific antigens or antibodies from a complex mixture. This technique involves incubating the mixture with an antibody that recognizes the antigen or antibody of interest, followed by precipitation of the antigen-antibody complex using a variety of methods.
5. Radioimmunoassay (RIA): A sensitive assay used to detect and quantify antigens or antibodies in a sample. This technique uses radioactively labeled antigens or antibodies, which bind to specific antigens or antibodies in the sample, allowing for detection and quantification using a scintillation counter.
These techniques are important tools in medical diagnosis, research, and forensic science.
Neoplasm antigens, also known as tumor antigens, are substances that are produced by cancer cells (neoplasms) and can stimulate an immune response. These antigens can be proteins, carbohydrates, or other molecules that are either unique to the cancer cells or are overexpressed or mutated versions of normal cellular proteins.
Neoplasm antigens can be classified into two main categories: tumor-specific antigens (TSAs) and tumor-associated antigens (TAAs). TSAs are unique to cancer cells and are not expressed by normal cells, while TAAs are present at low levels in normal cells but are overexpressed or altered in cancer cells.
TSAs can be further divided into viral antigens and mutated antigens. Viral antigens are produced when cancer is caused by a virus, such as human papillomavirus (HPV) in cervical cancer. Mutated antigens are the result of genetic mutations that occur during cancer development and are unique to each patient's tumor.
Neoplasm antigens play an important role in the immune response against cancer. They can be recognized by the immune system, leading to the activation of immune cells such as T cells and natural killer (NK) cells, which can then attack and destroy cancer cells. However, cancer cells often develop mechanisms to evade the immune response, allowing them to continue growing and spreading.
Understanding neoplasm antigens is important for the development of cancer immunotherapies, which aim to enhance the body's natural immune response against cancer. These therapies include checkpoint inhibitors, which block proteins that inhibit T cell activation, and therapeutic vaccines, which stimulate an immune response against specific tumor antigens.
Sensitivity and specificity are statistical measures used to describe the performance of a diagnostic test or screening tool in identifying true positive and true negative results.
* Sensitivity refers to the proportion of people who have a particular condition (true positives) who are correctly identified by the test. It is also known as the "true positive rate" or "recall." A highly sensitive test will identify most or all of the people with the condition, but may also produce more false positives.
* Specificity refers to the proportion of people who do not have a particular condition (true negatives) who are correctly identified by the test. It is also known as the "true negative rate." A highly specific test will identify most or all of the people without the condition, but may also produce more false negatives.
In medical testing, both sensitivity and specificity are important considerations when evaluating a diagnostic test. High sensitivity is desirable for screening tests that aim to identify as many cases of a condition as possible, while high specificity is desirable for confirmatory tests that aim to rule out the condition in people who do not have it.
It's worth noting that sensitivity and specificity are often influenced by factors such as the prevalence of the condition in the population being tested, the threshold used to define a positive result, and the reliability and validity of the test itself. Therefore, it's important to consider these factors when interpreting the results of a diagnostic test.
Flow cytometry is a medical and research technique used to measure physical and chemical characteristics of cells or particles, one cell at a time, as they flow in a fluid stream through a beam of light. The properties measured include:
* Cell size (light scatter)
* Cell internal complexity (granularity, also light scatter)
* Presence or absence of specific proteins or other molecules on the cell surface or inside the cell (using fluorescent antibodies or other fluorescent probes)
The technique is widely used in cell counting, cell sorting, protein engineering, biomarker discovery and monitoring disease progression, particularly in hematology, immunology, and cancer research.
In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.
The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.
In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.
Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:
1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.
Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.
A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.
Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.
Affinity chromatography is a type of chromatography technique used in biochemistry and molecular biology to separate and purify proteins based on their biological characteristics, such as their ability to bind specifically to certain ligands or molecules. This method utilizes a stationary phase that is coated with a specific ligand (e.g., an antibody, antigen, receptor, or enzyme) that selectively interacts with the target protein in a sample.
The process typically involves the following steps:
1. Preparation of the affinity chromatography column: The stationary phase, usually a solid matrix such as agarose beads or magnetic beads, is modified by covalently attaching the ligand to its surface.
2. Application of the sample: The protein mixture is applied to the top of the affinity chromatography column, allowing it to flow through the stationary phase under gravity or pressure.
3. Binding and washing: As the sample flows through the column, the target protein selectively binds to the ligand on the stationary phase, while other proteins and impurities pass through. The column is then washed with a suitable buffer to remove any unbound proteins and contaminants.
4. Elution of the bound protein: The target protein can be eluted from the column using various methods, such as changing the pH, ionic strength, or polarity of the buffer, or by introducing a competitive ligand that displaces the bound protein.
5. Collection and analysis: The eluted protein fraction is collected and analyzed for purity and identity, often through techniques like SDS-PAGE or mass spectrometry.
Affinity chromatography is a powerful tool in biochemistry and molecular biology due to its high selectivity and specificity, enabling the efficient isolation of target proteins from complex mixtures. However, it requires careful consideration of the binding affinity between the ligand and the protein, as well as optimization of the elution conditions to minimize potential damage or denaturation of the purified protein.
Radioimmunodetection (RID) is a medical diagnostic technique that combines the specificity of antibodies with the sensitivity of radioisotopes to detect and locate antigens or tumor markers within the body. This technique involves labeling antibodies with radioactive isotopes, which are then introduced into the patient's body. The labeled antibodies bind to the target antigens, allowing for their detection and localization using external gamma cameras.
The process typically begins with the production of monoclonal or polyclonal antibodies that specifically recognize and bind to a particular antigen associated with a disease or condition. These antibodies are then labeled with radioisotopes such as technetium-99m, iodine-131, or indium-111, which emit gamma rays that can be detected by external imaging devices.
Once the labeled antibodies have been administered to the patient, they circulate throughout the body and bind to their respective antigens. The bound radioactive antibodies can then be imaged using a gamma camera or single-photon emission computed tomography (SPECT) scanner, providing information about the location, size, and distribution of the target antigens within the body.
Radioimmunodetection has been widely used in the detection and monitoring of various malignancies, including cancerous tumors and metastases, as well as inflammatory and infectious diseases. It offers several advantages over other diagnostic techniques, such as high sensitivity, specificity, and non-invasiveness, making it an essential tool in modern medical imaging and diagnostics.
A hapten is a small molecule that can elicit an immune response only when it is attached to a larger carrier protein. On its own, a hapten is too small to be recognized by the immune system as a foreign substance. However, when it binds to a carrier protein, it creates a new antigenic site that can be detected by the immune system. This process is known as haptenization.
Haptens are important in the study of immunology and allergies because they can cause an allergic response when they bind to proteins in the body. For example, certain chemicals found in cosmetics, drugs, or industrial products can act as haptens and trigger an allergic reaction when they come into contact with the skin or mucous membranes. The resulting immune response can cause symptoms such as rash, itching, or inflammation.
Haptens can also be used in the development of vaccines and diagnostic tests, where they are attached to carrier proteins to stimulate an immune response and produce specific antibodies that can be measured or used for therapy.
Tissue distribution, in the context of pharmacology and toxicology, refers to the way that a drug or xenobiotic (a chemical substance found within an organism that is not naturally produced by or expected to be present within that organism) is distributed throughout the body's tissues after administration. It describes how much of the drug or xenobiotic can be found in various tissues and organs, and is influenced by factors such as blood flow, lipid solubility, protein binding, and the permeability of cell membranes. Understanding tissue distribution is important for predicting the potential effects of a drug or toxin on different parts of the body, and for designing drugs with improved safety and efficacy profiles.
Antibody diversity refers to the variety of different antibodies that an organism can produce in response to exposure to various antigens. This diversity is generated through a process called V(D)J recombination, which occurs during the development of B cells in the bone marrow.
The variable regions of heavy and light chains of antibody molecules are generated by the random selection and rearrangement of gene segments (V, D, and J) from different combinations. This results in a unique antigen-binding site for each antibody molecule, allowing the immune system to recognize and respond to a vast array of potential pathogens.
Further diversity is generated through the processes of somatic hypermutation and class switch recombination, which introduce additional changes in the variable regions of antibodies during an immune response. These processes allow for the affinity maturation of antibodies, where the binding strength between the antibody and antigen is increased over time, leading to a more effective immune response.
Overall, antibody diversity is critical for the adaptive immune system's ability to recognize and respond to a wide range of pathogens and protect against infection and disease.
Biotinidase deficiency is a genetic disorder that affects the body's ability to recycle and reuse biotin, a type of B vitamin. Biotinidase is an enzyme that helps release biotin from proteins in the food we eat and recycle it for use by the body.
In people with biotinidase deficiency, the biotinidase enzyme is either partially or completely missing, leading to a decrease in available biotin. This can result in a variety of symptoms, including seizures, developmental delays, hearing and vision loss, skin rashes, hair loss, and muscle weakness.
There are two main types of biotinidase deficiency: partial deficiency and profound deficiency. Partial deficiency means that some biotinidase activity is present, but not enough to prevent symptoms. Profound deficiency means that there is little or no biotinidase activity, resulting in more severe symptoms.
Biotinidase deficiency can be diagnosed through a blood test that measures the level of biotinidase enzyme activity. Treatment typically involves taking biotin supplements to replace the missing biotin and prevent symptoms from developing or worsening. With early diagnosis and treatment, people with biotinidase deficiency can often lead normal lives.
Vitamin B deficiency refers to a condition where an individual's body lacks adequate amounts of one or more essential Vitamin B compounds, including Vitamin B1 (thiamin), Vitamin B2 (riboflavin), Vitamin B3 (niacin), Vitamin B5 (pantothenic acid), Vitamin B6 (pyridoxine), Vitamin B7 (biotin), Vitamin B9 (folate), and Vitamin B12 (cobalamin). These water-soluble vitamins play crucial roles in various bodily functions, such as energy production, nerve function, DNA repair, and the formation of red blood cells.
Deficiency in any of these Vitamin B compounds can lead to specific health issues. For instance:
1. Vitamin B1 (thiamin) deficiency can cause beriberi, a condition characterized by muscle weakness, peripheral neuropathy, and heart failure.
2. Vitamin B2 (riboflavin) deficiency may result in ariboflavinosis, which presents with inflammation of the mouth and tongue, anemia, and skin disorders.
3. Vitamin B3 (niacin) deficiency can lead to pellagra, marked by diarrhea, dermatitis, dementia, and, if left untreated, death.
4. Vitamin B5 (pantothenic acid) deficiency is rare but can cause acne-like skin lesions and neurological symptoms.
5. Vitamin B6 (pyridoxine) deficiency may result in anemia, peripheral neuropathy, seizures, and skin disorders.
6. Vitamin B7 (biotin) deficiency can cause hair loss, skin rashes, and neurological symptoms.
7. Vitamin B9 (folate) deficiency can lead to megaloblastic anemia, neural tube defects in fetuses during pregnancy, and increased homocysteine levels, which may contribute to cardiovascular disease.
8. Vitamin B12 (cobalamin) deficiency can cause pernicious anemia, characterized by fatigue, weakness, neurological symptoms, and, if left untreated, irreversible nerve damage.
Deficiencies in these vitamins can arise from inadequate dietary intake, malabsorption syndromes, or certain medications that interfere with absorption or metabolism. It is essential to maintain a balanced diet and consider supplementation if necessary under the guidance of a healthcare professional.
Peptides are short chains of amino acid residues linked by covalent bonds, known as peptide bonds. They are formed when two or more amino acids are joined together through a condensation reaction, which results in the elimination of a water molecule and the formation of an amide bond between the carboxyl group of one amino acid and the amino group of another.
Peptides can vary in length from two to about fifty amino acids, and they are often classified based on their size. For example, dipeptides contain two amino acids, tripeptides contain three, and so on. Oligopeptides typically contain up to ten amino acids, while polypeptides can contain dozens or even hundreds of amino acids.
Peptides play many important roles in the body, including serving as hormones, neurotransmitters, enzymes, and antibiotics. They are also used in medical research and therapeutic applications, such as drug delivery and tissue engineering.
Glycoproteins are complex proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. These glycans are linked to the protein through asparagine residues (N-linked) or serine/threonine residues (O-linked). Glycoproteins play crucial roles in various biological processes, including cell recognition, cell-cell interactions, cell adhesion, and signal transduction. They are widely distributed in nature and can be found on the outer surface of cell membranes, in extracellular fluids, and as components of the extracellular matrix. The structure and composition of glycoproteins can vary significantly depending on their function and location within an organism.
Species specificity is a term used in the field of biology, including medicine, to refer to the characteristic of a biological entity (such as a virus, bacterium, or other microorganism) that allows it to interact exclusively or preferentially with a particular species. This means that the biological entity has a strong affinity for, or is only able to infect, a specific host species.
For example, HIV is specifically adapted to infect human cells and does not typically infect other animal species. Similarly, some bacterial toxins are species-specific and can only affect certain types of animals or humans. This concept is important in understanding the transmission dynamics and host range of various pathogens, as well as in developing targeted therapies and vaccines.
Iodine radioisotopes are radioactive isotopes of the element iodine, which decays and emits radiation in the form of gamma rays. Some commonly used iodine radioisotopes include I-123, I-125, I-131. These radioisotopes have various medical applications such as in diagnostic imaging, therapy for thyroid disorders, and cancer treatment.
For example, I-131 is commonly used to treat hyperthyroidism and differentiated thyroid cancer due to its ability to destroy thyroid tissue. On the other hand, I-123 is often used in nuclear medicine scans of the thyroid gland because it emits gamma rays that can be detected by a gamma camera, allowing for detailed images of the gland's structure and function.
It is important to note that handling and administering radioisotopes require specialized training and safety precautions due to their radiation-emitting properties.
Hepatitis C antibodies are proteins produced by the immune system in response to an infection with the hepatitis C virus (HCV). Detection of these antibodies in the blood indicates a past or present HCV infection. However, it does not necessarily mean that the person is currently infected, as antibodies can persist for years even after the virus has been cleared from the body. Additional tests are usually needed to confirm whether the infection is still active and to guide treatment decisions.
Isoantibodies are antibodies produced by the immune system that recognize and react to antigens (markers) found on the cells or tissues of another individual of the same species. These antigens are typically proteins or carbohydrates present on the surface of red blood cells, but they can also be found on other cell types.
Isoantibodies are formed when an individual is exposed to foreign antigens, usually through blood transfusions, pregnancy, or tissue transplantation. The exposure triggers the immune system to produce specific antibodies against these antigens, which can cause a harmful immune response if the individual receives another transfusion or transplant from the same donor in the future.
There are two main types of isoantibodies:
1. Agglutinins: These are IgM antibodies that cause red blood cells to clump together (agglutinate) when mixed with the corresponding antigen. They develop rapidly after exposure and can cause immediate transfusion reactions or hemolytic disease of the newborn in pregnant women.
2. Hemolysins: These are IgG antibodies that destroy red blood cells by causing their membranes to become more permeable, leading to lysis (bursting) of the cells and release of hemoglobin into the plasma. They take longer to develop but can cause delayed transfusion reactions or hemolytic disease of the newborn in pregnant women.
Isoantibodies are detected through blood tests, such as the crossmatch test, which determines compatibility between a donor's and recipient's blood before transfusions or transplants.
Immunoglobulins, also known as antibodies, are proteins produced by the immune system to recognize and neutralize foreign substances like pathogens or antigens. The term "immunoglobulin isotypes" refers to the different classes of immunoglobulins that share a similar structure but have distinct functions and properties.
There are five main isotypes of immunoglobulins in humans, namely IgA, IgD, IgE, IgG, and IgM. Each isotype has a unique heavy chain constant region (CH) that determines its effector functions, such as binding to Fc receptors, complement activation, or protection against pathogens.
IgA is primarily found in external secretions like tears, saliva, and breast milk, providing localized immunity at mucosal surfaces. IgD is expressed on the surface of B cells and plays a role in their activation and differentiation. IgE is associated with allergic responses and binds to mast cells and basophils, triggering the release of histamine and other mediators of inflammation.
IgG is the most abundant isotype in serum and has several subclasses (IgG1, IgG2, IgG3, and IgG4) that differ in their effector functions. IgG can cross the placenta, providing passive immunity to the fetus. IgM is the first antibody produced during an immune response and is primarily found in the bloodstream, where it forms large pentameric complexes that are effective at agglutination and complement activation.
Overall, immunoglobulin isotypes play a crucial role in the adaptive immune response, providing specific and diverse mechanisms for recognizing and neutralizing foreign substances.
Immunoglobulins (Igs), also known as antibodies, are glycoprotein molecules produced by the immune system's B cells in response to the presence of foreign substances, such as bacteria, viruses, and toxins. These Y-shaped proteins play a crucial role in identifying and neutralizing pathogens and other antigens, thereby protecting the body against infection and disease.
Immunoglobulins are composed of four polypeptide chains: two identical heavy chains and two identical light chains, held together by disulfide bonds. The variable regions of these chains form the antigen-binding sites, which recognize and bind to specific epitopes on antigens. Based on their heavy chain type, immunoglobulins are classified into five main isotypes or classes: IgA, IgD, IgE, IgG, and IgM. Each class has distinct functions in the immune response, such as providing protection in different body fluids and tissues, mediating hypersensitivity reactions, and aiding in the development of immunological memory.
In medical settings, immunoglobulins can be administered therapeutically to provide passive immunity against certain diseases or to treat immune deficiencies, autoimmune disorders, and other conditions that may benefit from immunomodulation.
Carboxy-lyases are a class of enzymes that catalyze the removal of a carboxyl group from a substrate, often releasing carbon dioxide in the process. These enzymes play important roles in various metabolic pathways, such as the biosynthesis and degradation of amino acids, sugars, and other organic compounds.
Carboxy-lyases are classified under EC number 4.2 in the Enzyme Commission (EC) system. They can be further divided into several subclasses based on their specific mechanisms and substrates. For example, some carboxy-lyases require a cofactor such as biotin or thiamine pyrophosphate to facilitate the decarboxylation reaction, while others do not.
Examples of carboxy-lyases include:
1. Pyruvate decarboxylase: This enzyme catalyzes the conversion of pyruvate to acetaldehyde and carbon dioxide during fermentation in yeast and other organisms.
2. Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO): This enzyme is essential for photosynthesis in plants and some bacteria, as it catalyzes the fixation of carbon dioxide into an organic molecule during the Calvin cycle.
3. Phosphoenolpyruvate carboxylase: Found in plants, algae, and some bacteria, this enzyme plays a role in anaplerotic reactions that replenish intermediates in the citric acid cycle. It catalyzes the conversion of phosphoenolpyruvate to oxaloacetate and inorganic phosphate.
4. Aspartate transcarbamylase: This enzyme is involved in the biosynthesis of pyrimidines, a class of nucleotides. It catalyzes the transfer of a carboxyl group from carbamoyl aspartate to carbamoyl phosphate, forming cytidine triphosphate (CTP) and fumarate.
5. Urocanase: Found in animals, this enzyme is involved in histidine catabolism. It catalyzes the conversion of urocanate to formiminoglutamate and ammonia.
Monoclonal murine-derived antibodies are a type of laboratory-produced antibody that is identical in structure, having been derived from a single clone of cells. These antibodies are created using mouse cells and are therefore composed entirely of mouse immune proteins. They are designed to bind specifically to a particular target protein or antigen, making them useful tools for research, diagnostic testing, and therapeutic applications.
Monoclonal antibodies offer several advantages over polyclonal antibodies (which are derived from multiple clones of cells and can recognize multiple epitopes on an antigen). Monoclonal antibodies have a consistent and uniform structure, making them more reliable for research and diagnostic purposes. They also have higher specificity and affinity for their target antigens, allowing for more sensitive detection and measurement.
However, there are some limitations to using monoclonal murine-derived antibodies in therapeutic applications. Because they are composed entirely of mouse proteins, they can elicit an immune response in humans, leading to the production of human anti-mouse antibodies (HAMA) that can neutralize their effectiveness. To overcome this limitation, researchers have developed chimeric and humanized monoclonal antibodies that incorporate human protein sequences, reducing the risk of an immune response.
Radioimmunotherapy (RIT) is a medical treatment that combines the specificity of antibodies and the therapeutic effects of radiation to target and destroy cancer cells. It involves the use of radioactive isotopes, which are attached to monoclonal antibodies, that recognize and bind to antigens expressed on the surface of cancer cells. Once bound, the radioactivity emitted from the isotope irradiates the cancer cells, causing damage to their DNA and leading to cell death. This targeted approach helps minimize radiation exposure to healthy tissues and reduces side effects compared to conventional radiotherapy techniques. RIT has been used in the treatment of various hematological malignancies, such as non-Hodgkin lymphoma, and is being investigated for solid tumors as well.
Vaccination is a simple, safe, and effective way to protect people against harmful diseases, before they come into contact with them. It uses your body's natural defenses to build protection to specific infections and makes your immune system stronger.
A vaccination usually contains a small, harmless piece of a virus or bacteria (or toxins produced by these germs) that has been made inactive or weakened so it won't cause the disease itself. This piece of the germ is known as an antigen. When the vaccine is introduced into the body, the immune system recognizes the antigen as foreign and produces antibodies to fight it.
If a person then comes into contact with the actual disease-causing germ, their immune system will recognize it and immediately produce antibodies to destroy it. The person is therefore protected against that disease. This is known as active immunity.
Vaccinations are important for both individual and public health. They prevent the spread of contagious diseases and protect vulnerable members of the population, such as young children, the elderly, and people with weakened immune systems who cannot be vaccinated or for whom vaccination is not effective.
Ligases are a group of enzymes that catalyze the formation of a covalent bond between two molecules, usually involving the joining of two nucleotides in a DNA or RNA strand. They play a crucial role in various biological processes such as DNA replication, repair, and recombination. In DNA ligases, the enzyme seals nicks or breaks in the phosphodiester backbone of the DNA molecule by catalyzing the formation of an ester bond between the 3'-hydroxyl group and the 5'-phosphate group of adjacent nucleotides. This process is essential for maintaining genomic integrity and stability.
Hepatitis B antibodies are proteins produced by the immune system in response to the presence of the Hepatitis B virus. There are two main types of Hepatitis B antibodies:
1. Hepatitis B surface antibody (anti-HBs): This is produced when a person has recovered from a Hepatitis B infection or has been successfully vaccinated against the virus. The presence of anti-HBs indicates immunity to Hepatitis B.
2. Hepatitis B core antibody (anti-HBC): This is produced during a Hepatitis B infection and remains present for life, even after the infection has been cleared. However, the presence of anti-HBC alone does not indicate immunity to Hepatitis B, as it can also be present in people who have a chronic Hepatitis B infection.
It's important to note that testing for Hepatitis B antibodies is typically done through blood tests and can help determine whether a person has been infected with the virus, has recovered from an infection, or has been vaccinated against it.
Immunodiffusion is a laboratory technique used in immunology to detect and measure the presence of specific antibodies or antigens in a sample. It is based on the principle of diffusion, where molecules move from an area of high concentration to an area of low concentration until they reach equilibrium. In this technique, a sample containing an unknown quantity of antigen or antibody is placed in a gel or agar medium that contains a known quantity of antibody or antigen, respectively.
The two substances then diffuse towards each other and form a visible precipitate at the point where they meet and reach equivalence, which indicates the presence and quantity of the specific antigen or antibody in the sample. There are several types of immunodiffusion techniques, including radial immunodiffusion (RID) and double immunodiffusion (Ouchterlony technique). These techniques are widely used in diagnostic laboratories to identify and measure various antigens and antibodies, such as those found in infectious diseases, autoimmune disorders, and allergic reactions.
The spleen is an organ in the upper left side of the abdomen, next to the stomach and behind the ribs. It plays multiple supporting roles in the body:
1. It fights infection by acting as a filter for the blood. Old red blood cells are recycled in the spleen, and platelets and white blood cells are stored there.
2. The spleen also helps to control the amount of blood in the body by removing excess red blood cells and storing platelets.
3. It has an important role in immune function, producing antibodies and removing microorganisms and damaged red blood cells from the bloodstream.
The spleen can be removed without causing any significant problems, as other organs take over its functions. This is known as a splenectomy and may be necessary if the spleen is damaged or diseased.
Maternally-acquired immunity (MAI) refers to the passive immunity that is transferred from a mother to her offspring, typically through the placenta during pregnancy or through breast milk after birth. This immunity is temporary and provides protection to the newborn or young infant against infectious agents, such as bacteria and viruses, based on the mother's own immune experiences and responses.
In humans, maternally-acquired immunity is primarily mediated by the transfer of antibodies called immunoglobulins (IgG) across the placenta to the fetus during pregnancy. This process begins around the 20th week of gestation and continues until birth, providing the newborn with a range of protective antibodies against various pathogens. After birth, additional protection is provided through breast milk, which contains secretory immunoglobulin A (IgA) that helps to prevent infections in the infant's gastrointestinal and respiratory tracts.
Maternally-acquired immunity is an essential mechanism for protecting newborns and young infants, who have not yet developed their own active immune responses. However, it is important to note that maternally-acquired antibodies can also interfere with the infant's response to certain vaccines, as they may neutralize the vaccine antigens before the infant's immune system has a chance to mount its own response. This is one reason why some vaccines are not recommended for young infants and why the timing of vaccinations may be adjusted in cases where maternally-acquired immunity is present.
C57BL/6 (C57 Black 6) is an inbred strain of laboratory mouse that is widely used in biomedical research. The term "inbred" refers to a strain of animals where matings have been carried out between siblings or other closely related individuals for many generations, resulting in a population that is highly homozygous at most genetic loci.
The C57BL/6 strain was established in 1920 by crossing a female mouse from the dilute brown (DBA) strain with a male mouse from the black strain. The resulting offspring were then interbred for many generations to create the inbred C57BL/6 strain.
C57BL/6 mice are known for their robust health, longevity, and ease of handling, making them a popular choice for researchers. They have been used in a wide range of biomedical research areas, including studies of cancer, immunology, neuroscience, cardiovascular disease, and metabolism.
One of the most notable features of the C57BL/6 strain is its sensitivity to certain genetic modifications, such as the introduction of mutations that lead to obesity or impaired glucose tolerance. This has made it a valuable tool for studying the genetic basis of complex diseases and traits.
Overall, the C57BL/6 inbred mouse strain is an important model organism in biomedical research, providing a valuable resource for understanding the genetic and molecular mechanisms underlying human health and disease.
Insulin antibodies are proteins produced by the immune system that recognize and bind to insulin. They are typically formed in response to an exposure to exogenous insulin, such as in people with diabetes who use insulin therapy. In some cases, the presence of insulin antibodies can affect insulin absorption, distribution, metabolism, and elimination, leading to variable insulin requirements, reduced glycemic control, and potentially an increased risk of hypoglycemia or hyperglycemia. However, not all individuals with insulin antibodies experience clinical consequences, and the significance of their presence can vary between individuals.
The complement system is a group of proteins found in the blood and on the surface of cells that when activated, work together to help eliminate pathogens such as bacteria, viruses, and fungi from the body. The proteins are normally inactive in the bloodstream. When they encounter an invading microorganism or foreign substance, a series of reactions take place leading to the activation of the complement system. Activation results in the production of effector molecules that can punch holes in the cell membranes of pathogens, recruit and activate immune cells, and help remove debris and dead cells from the body.
There are three main pathways that can lead to complement activation: the classical pathway, the lectin pathway, and the alternative pathway. Each pathway involves a series of proteins that work together in a cascade-like manner to amplify the response and generate effector molecules. The three main effector molecules produced by the complement system are C3b, C4b, and C5b. These molecules can bind to the surface of pathogens, marking them for destruction by other immune cells.
Complement proteins also play a role in the regulation of the immune response. They help to prevent excessive activation of the complement system, which could damage host tissues. Dysregulation of the complement system has been implicated in a number of diseases, including autoimmune disorders and inflammatory conditions.
In summary, Complement System Proteins are a group of proteins that play a crucial role in the immune response by helping to eliminate pathogens and regulate the immune response. They can be activated through three different pathways, leading to the production of effector molecules that mark pathogens for destruction. Dysregulation of the complement system has been linked to various diseases.
Systemic Lupus Erythematosus (SLE) is a complex autoimmune disease that can affect almost any organ or system in the body. In SLE, the immune system produces an exaggerated response, leading to the production of autoantibodies that attack the body's own cells and tissues, causing inflammation and damage. The symptoms and severity of SLE can vary widely from person to person, but common features include fatigue, joint pain, skin rashes (particularly a "butterfly" rash across the nose and cheeks), fever, hair loss, and sensitivity to sunlight.
Systemic lupus erythematosus can also affect the kidneys, heart, lungs, brain, blood vessels, and other organs, leading to a wide range of symptoms such as kidney dysfunction, chest pain, shortness of breath, seizures, and anemia. The exact cause of SLE is not fully understood, but it is believed to involve a combination of genetic, environmental, and hormonal factors. Treatment typically involves medications to suppress the immune system and manage symptoms, and may require long-term management by a team of healthcare professionals.
Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:
1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction
Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:
1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.
Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).
Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).
Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.
Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.
Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.
Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.
Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.
Lymphocytes are a type of white blood cell that is an essential part of the immune system. They are responsible for recognizing and responding to potentially harmful substances such as viruses, bacteria, and other foreign invaders. There are two main types of lymphocytes: B-lymphocytes (B-cells) and T-lymphocytes (T-cells).
B-lymphocytes produce antibodies, which are proteins that help to neutralize or destroy foreign substances. When a B-cell encounters a foreign substance, it becomes activated and begins to divide and differentiate into plasma cells, which produce and secrete large amounts of antibodies. These antibodies bind to the foreign substance, marking it for destruction by other immune cells.
T-lymphocytes, on the other hand, are involved in cell-mediated immunity. They directly attack and destroy infected cells or cancerous cells. T-cells can also help to regulate the immune response by producing chemical signals that activate or inhibit other immune cells.
Lymphocytes are produced in the bone marrow and mature in either the bone marrow (B-cells) or the thymus gland (T-cells). They circulate throughout the body in the blood and lymphatic system, where they can be found in high concentrations in lymph nodes, the spleen, and other lymphoid organs.
Abnormalities in the number or function of lymphocytes can lead to a variety of immune-related disorders, including immunodeficiency diseases, autoimmune disorders, and cancer.
Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.
Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.
Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.
A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.
Autoantigens are substances that are typically found in an individual's own body, but can stimulate an immune response because they are recognized as foreign by the body's own immune system. In autoimmune diseases, the immune system mistakenly attacks and damages healthy tissues and organs because it recognizes some of their components as autoantigens. These autoantigens can be proteins, DNA, or other molecules that are normally present in the body but have become altered or exposed due to various factors such as infection, genetics, or environmental triggers. The immune system then produces antibodies and activates immune cells to attack these autoantigens, leading to tissue damage and inflammation.
A precipitin test is a type of immunodiagnostic test used to detect and measure the presence of specific antibodies or antigens in a patient's serum. The test is based on the principle of antigen-antibody interaction, where the addition of an antigen to a solution containing its corresponding antibody results in the formation of an insoluble immune complex known as a precipitin.
In this test, a small amount of the patient's serum is added to a solution containing a known antigen or antibody. If the patient has antibodies or antigens that correspond to the added reagent, they will bind and form a visible precipitate. The size and density of the precipitate can be used to quantify the amount of antibody or antigen present in the sample.
Precipitin tests are commonly used in the diagnosis of various infectious diseases, autoimmune disorders, and allergies. They can also be used in forensic science to identify biological samples. However, they have largely been replaced by more modern immunological techniques such as enzyme-linked immunosorbent assays (ELISAs) and radioimmunoassays (RIAs).
A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.
Antigens are substances (usually proteins) found on the surface of cells, or viruses, that can be recognized by the immune system and stimulate an immune response. In the context of protozoa, antigens refer to the specific proteins or other molecules found on the surface of these single-celled organisms that can trigger an immune response in a host organism.
Protozoa are a group of microscopic eukaryotic organisms that include a diverse range of species, some of which can cause diseases in humans and animals. When a protozoan infects a host, the host's immune system recognizes the protozoan antigens as foreign and mounts an immune response to eliminate the infection. This response involves the activation of various types of immune cells, such as T-cells and B-cells, which recognize and target the protozoan antigens.
Understanding the nature of protozoan antigens is important for developing vaccines and other immunotherapies to prevent or treat protozoan infections. For example, researchers have identified specific antigens on the surface of the malaria parasite that are recognized by the human immune system and have used this information to develop vaccine candidates. However, many protozoan infections remain difficult to prevent or treat, and further research is needed to identify new targets for vaccines and therapies.
Pantothenic Acid, also known as Vitamin B5, is a water-soluble vitamin that plays a vital role in the metabolism of proteins, carbohydrates, and fats. It is essential for the synthesis of coenzyme A (CoA), which is involved in various biochemical reactions in the body, including energy production, fatty acid synthesis, and cholesterol metabolism.
Pantothenic Acid is widely distributed in foods, including meat, poultry, fish, whole grains, legumes, and vegetables. Deficiency of this vitamin is rare but can lead to symptoms such as fatigue, irritability, sleep disturbances, muscle cramps, and gastrointestinal problems.
In addition to its role in metabolism, Pantothenic Acid also has potential benefits for wound healing, reducing inflammation, and supporting the immune system.
Holocarboxylase Synthetase Deficiency (HCD) is a rare genetic disorder of biotin metabolism, characterized by the body's inability to properly utilize the vitamin biotin. Biotin plays a crucial role in various essential functions, such as the breakdown of fats, proteins, and carbohydrates, as well as the regulation of gene expression.
Holocarboxylase synthetase is an enzyme responsible for attaching biotin to four different carboxylases, which are necessary for these vital processes. In Holocarboxylase Synthetase Deficiency, this enzyme is either partially or completely nonfunctional due to mutations in the HLCS gene.
The symptoms of HCD can vary widely but often include:
1. Feeding difficulties and poor growth in infancy
2. Severe metabolic acidosis
3. Ketoacidosis
4. Delayed development
5. Hypotonia (low muscle tone)
6. Skin rashes
7. Hair loss
8. Neurological symptoms, such as seizures and ataxia (loss of coordination and balance)
If left untreated, Holocarboxylase Synthetase Deficiency can lead to severe complications, including developmental delays, neurological damage, and even death. However, with early diagnosis and proper treatment involving biotin supplementation, many of these symptoms can be managed, and the progression of the disorder can be slowed or stopped.
Erythrocytes, also known as red blood cells (RBCs), are the most common type of blood cell in circulating blood in mammals. They are responsible for transporting oxygen from the lungs to the body's tissues and carbon dioxide from the tissues to the lungs.
Erythrocytes are formed in the bone marrow and have a biconcave shape, which allows them to fold and bend easily as they pass through narrow blood vessels. They do not have a nucleus or mitochondria, which makes them more flexible but also limits their ability to reproduce or repair themselves.
In humans, erythrocytes are typically disc-shaped and measure about 7 micrometers in diameter. They contain the protein hemoglobin, which binds to oxygen and gives blood its red color. The lifespan of an erythrocyte is approximately 120 days, after which it is broken down in the liver and spleen.
Abnormalities in erythrocyte count or function can lead to various medical conditions, such as anemia, polycythemia, and sickle cell disease.
Potato virus Y
Immunostaining
Antibody microarray
Biotinylation
Biotin PEG2 amine
Thymidine kinase in clinical chemistry
Artificial metalloenzyme
Iodine (131 I) derlotuximab biotin
Fluorescence in situ hybridization
Immunoperoxidase
Tethered particle motion
DOTA (chelator)
90Y-DOTA-biotin
ELISpot
Chromosome combing
Bioconjugation
Digoxigenin
Jane Osbourn
Polymer-protein hybrid
Meir Wilchek
Protein A
Chromogenic in situ hybridization
Contrast-enhanced ultrasound
Hybridization probe
Collagen hybridizing peptide
SBP-tag
Reverse phase protein lysate microarray
Zinc finger chimera
CITE-Seq
Index of oncology articles
Anti-Mouse IgG (whole molecule)−Biotin antibody produced in goat
Biotin Anti-C5b-9 antibody [aE11] (ab237699) | Abcam
CCL5 (RANTES) Polyclonal Antibody, Biotin, PeproTech , Invitrogen 1 mg; | Fisher Scientific
SQLE Antibody [Biotin] (NBP2-98542B): Novus Biologicals
PIK3AP1 Monoclonal Antibody (OTI6H6), Biotin (TA700418) ...
CD36 Monoclonal Antibody (OTI4H7), Biotin (TA700031)
Alexa Fluor® 680-Monoclonal Mouse Anti-Biotin Antibody | JIR
FCGRT Antibody, Biotin conjugated | CSB-PA851443LD01MOV | Cusabio
TNFSF14 Antibody, Biotin conjugated | CSB-PA06825D0Rb | Cusabio
TotalSeq™-C0436 anti-Biotin Antibody, Biotin, 1D4-C5
Biotin anti-human CD14 Antibody anti-CD14 - 63D3
Biotin-Fab Goat Anti-Mouse IgG2c, Fcγ Secondary Antibody | JIR
LIPG Mouse Monoclonal Antibody (Biotin conjugated) [Clone ID: OTI4A8] - TA501047AM | OriGene
HNRPM (HNRNPM) Mouse Monoclonal Antibody (Biotin conjugated) [Clone ID: OTI4C9] - TA803306AM | OriGene
Anti-HLA-G antibody [MEM-G/9] (Biotin) (GTX78333) | GeneTex
Biotin-Linked Monoclonal Antibody to Interleukin 6 (IL6) | LAA079Hu72 | Cloud-Clone
TRIM15 Antibody - middle region : Biotin (ARP58130 P050-Biotin) | Aviva Systems Biology | Avivasysbio.com
Anti-MAPK7 / ERK5 Antibody | Rabbit anti-Human Polyclonal Biotin | LSBio
Anti-POPDC2 Antibody | Rabbit anti-Human Polyclonal Biotin WB | LSBio
BCMA (human) monoclonal antibody (Vicky-1) (biotin conjugate) - ALX-804-151B - Enzo Life Sciences
Anti-Hu CD4 Biotin - EXBIO Antibodies
Histonet] Has anyone used a biotin block in their antibody diluent?
Anti-MERTK Goat Polyclonal Antibody (Biotin) | VWR
PPP4C Polyclonal Antibody, Biotin Conjugated - Bioss
anti-Homo sapiens (Human) PTH Antibody, Biotin conjugated raised in Rabbit - Cusabio
C10orf91 Polyclonal Antibody, Biotin Conjugated | EpigenTek
IGBP1 Polyclonal Antibody, Biotin Conjugated - Bioss
Anti-Biotin Antibody SPM375 | V9113 NSJ Bioreagents
DNAJC22 antibody (Biotin), biotin, rabbit, Polyclonal | Labstore
Conjugate5
- Secondary Antibodies are available in a variety of formats and conjugate types. (rockland.com)
- When choosing a secondary antibody product, consideration must be given to species and immunoglobulin specificity, conjugate type, fragment and chain specificity, level of cross-reactivity, and host-species source and fragment composition. (rockland.com)
- Anti-Mouse IgG Fc Fragment-Biotin Conjugate Polyclonal antibody can be used for Western blot, immunohistochemistry on frozen slices or parrafin fixed tissues. (igganti.com)
- 26-6401-05 biological source: goat conjugate: peroxidase conjugate antibody form: purified immunoglobulin antibody product type: secondary antibodies clone: polyclonal species reactivity: rabbit concentration: 1. (caslab.com)
- 15-30120 biological source: rabbit Quality Level: 100 conjugate: peroxidase conjugate antibody form: affinity purified immunoglobulin antibody product type: secondary antibodies clone: polyclonal species. (caslab.com)
Reactivity1
- It also confirms the tive samples, 12 negative samples and 16 presence of infection in patients with incon- with indeterminate results by confirma- clusive antibody reactivity. (who.int)
Primary-antibodies2
- Primary Antibodies are guaranteed for 1 year from date of receipt. (novusbio.com)
- FabuLights are suggested for labeling primary antibodies to be used in immunofluorescence or histochemical experiments. (jacksonimmuno.com)
Conjugation1
- 271-16873 Description: APC-Cy7 tandem-labeled goat anti-rabbit IgG (H+L) Application: FC, IF Catlog: 16873 Clone Type: polyclonal Conjugation: APC/Cy7 Product Type: Antibodies Secondary Shipping. (caslab.com)
Immunogen2
- Biotinylated sheep immunoglobulin was used as the immunogen for this anti-Biotin antibody. (nsjbio.com)
- 89-GT15051-100 Product name Anti-Islet 1 antibody Description Rabbit polyclonal to Islet 1 Host species Rabbit Specificity ab20670 might also detect rat and human Islet 2 protein as the immunogen used to raise this. (caslab.com)
Anti-Biotin Antibody7
- The anti-biotin antibody can be used as a second-step reagent for detecting biotinylated targets. (biolegend.com)
- IHC: Formalin-fixed, paraffin-embedded human tonsil stained with biotinylated Lambda Light Chain Ab probe followed by anti-Biotin antibody (SPM375). (nsjbio.com)
- This anti-Biotin antibody is available for research use only. (nsjbio.com)
- Anti-biotin antibody may be substituted to decrease this noise. (nsjbio.com)
- The optimal dilution of the anti-Biotin antibody for each application should be determined by the researcher. (nsjbio.com)
- Store the anti-Biotin antibody at 2-8oC (with azide) or aliquot and store at -20oC or colder (without azide). (nsjbio.com)
- Anti-Biotin Antibody Conjugated to Gold (40 nm) is a high quality anti-Biotin antibodies or streptavidin conjugated to gold nanoparticles (40 nm). (moleculardepot.com)
Species3
- The antibody may cross-react with other mouse IgG subclasses or with immunoglobulins from other species. (jacksonimmuno.com)
- Please also provide information about species, application, dilution and obtained result for the reviewed antibody. (agrisera.com)
- Mouse or mice from the Mus musculus species are used for production of mouse monoclonal antibodies or mabs and as research model for humans in your lab. (igganti.com)
Conjugates3
- IgG fraction Monoclonal Mouse Anti-Biotin may be used either as direct conjugates, or for more sensitivity, they can be used unconjugated followed by a conjugated anti-mouse IgG (H+L) for signal enhancement . (jacksonimmuno.com)
- TotalSeq™ is BioLegend's brand of antibody-oligonucleotide conjugates, to enable simultaneous analysis of proteins and mRNA in single cells. (biolegend.com)
- If you buy Antibodies supplied by QED Biosciences they should be stored frozen at - 24°C for long term storage and for short term at + 5°C.Biotin conjugates can be detected by horseradish peroxidase, alkaline phosphatase substrates or anti biotin conjugated antibodies. (igganti.com)
Monoclonal antibodies2
- Abcam is leading the way in addressing this with our range of recombinant monoclonal antibodies and knockout edited cell lines for gold-standard validation. (abcam.com)
- Explore our solutions for multiple applications - vaccines, monoclonal antibodies, recombinant proteins, cell or gene therapy. (vwr.com)
Datasheet1
- If an Invitrogen™ antibody doesn't perform as described on our website or datasheet,we'll replace the product at no cost to you, or provide you with a credit for a future purchase. (thermofisher.com)
Antigen9
- Based on antigen-binding assay and/or ELISA, the antibody reacts with the Fc portion of mouse IgG2c but not with the Fab portion of mouse immunoglobulins. (jacksonimmuno.com)
- These antibodies are monovalent, containing only a single antigen binding site. (jacksonimmuno.com)
- See our complete line of Immunohistochemistry Reagents including antigen retrieval solutions, blocking agents ABC Detection Kits and polymers, biotinylated secondary antibodies, substrates and more. (lsbio.com)
- The antibody MEM-241 recognizes an extracellular epitope of CD4 antigen, a 55 kDa transmebrane glycoprotein expressed on a subset of T lymphocytes ("helper" T-cells) and also on monocytes, tissue macrophages and granulocytes. (exbio.cz)
- I plan on decreasing my antigen retrieval time, as someone has told me that an antigen retrieval that is too vigorous may cause the unmasking of biotin, and its subsequent staining. (utsouthwestern.edu)
- The IgG antibody has 2 antigen binding sites. (igganti.com)
- This antibody can be antigen purified or protein A or G purified. (igganti.com)
- Particle-enhanced assays were based on the reaction between a soluble analyte and the corresponding antigen or antibody bound to polystyrene particles. (cdc.gov)
- CRP present in the test sample forms an antigen-antibody complex with the latex particles. (cdc.gov)
FITC1
- CusabioFCGRT Antibody, FITC conjugated is Available at Gentaur Genprice with the fastest delivery.Online Order Payment is possible or send. (joplink.net)
Proteins4
- No antibody was detected against mouse IgM or against non-immunoglobulin serum proteins. (jacksonimmuno.com)
- ChromaLINK Biotin Maleimide incorporates UV-traceable biotin onto thiol containing proteins, peptides and/or antibodies. (vectorlabs.com)
- Labeling of proteins with ChromaLINK Biotin eliminates the need to carry out cumbersome and time-consuming HABA assays often employed to quantify biotin incorporation. (vectorlabs.com)
- 519-BA1039-1 SKU/Catalog Number: BA1039 Product Description: This antibody is purified from antiserum by immunoaffinity chromatography which removes essentially all goat serum proteins, except the specific. (caslab.com)
Streptavidin10
- This is especially notable when Biotin-SP conjugated antibodies are used with alkaline phosphatase-conjugated streptavidin. (jacksonimmuno.com)
- Apparently, the long spacer extends the biotin moiety away from the antibody surface, making it more accessible to binding sites on streptavidin. (jacksonimmuno.com)
- We offer streptavidin and Mouse Anti-Biotin conjugated to fluorophores and enzymes. (jacksonimmuno.com)
- Flow cytometry analysis (surface staining) of human peripheral blood cells with anti-human CD4 (MEM-241) biotin, streptavidin-APC. (exbio.cz)
- Avidin and Streptavidin bind to the small biotin and are couple to HRP or AP for ELISA. (igganti.com)
- To break the streptavidin Biotin bond we suggest to use a 6 molar guanidine HCl solution with acidity of pH 1.6. (igganti.com)
- The extended PEG3 linker preserves biotin/streptavidin affinity and maintains protein solubility after modification while the maleimide functional group (d), efficiently modifies thiols in aqueous buffers. (vectorlabs.com)
- The arrays were stained with streptavidin-phycoerythrin and biotinylated anti-streptavidin antibodies. (cdc.gov)
- Immunometric assays employing the streptavidin-biotin system are widely used to measure hormones. (medscape.com)
- If biotin interference is suspected, we propose either using a different assay not based on the streptavidin-biotin system or repeating the analyses after stopping biotin supplementation for one week. (medscape.com)
Reagent6
- To maximize performance, it is strongly recommended that the reagent be titrated for each application, and that you centrifuge the antibody dilution before adding to the cells at 14,000xg at 2 - 8°C for 10 minutes. (biolegend.com)
- Biotinylated antibodies require an additional reagent for visualization. (jacksonimmuno.com)
- The antibody MEM-G/9 is standard reagent thoroughly validated during 3rd International Conference on HLA-G (Paris, 2003). (genetex.com)
- The reagent is free of unconjugated biotin. (genetex.com)
- This reagent permits direct spectroscopic quantification of incorporated biotin. (vectorlabs.com)
- The Antibody Ihg And Ihm reagent is RUO (Research Use Only) to test human serum or cell culture lab samples. (putyourcolours.pl)
Rabbit Polyclonal Antibody2
Catalog1
- The following product was used in this experiment: PIK3AP1 Monoclonal Antibody (OTI6H6), Biotin, TrueMAB™ from Thermo Fisher Scientific, catalog # TA700418. (thermofisher.com)
Reagents1
- Igm Antibody Laboratories manufactures the antibody ihg and ihm reagents distributed by Genprice. (putyourcolours.pl)
Protein5
- Biotin (vitamin B7 or vitamin H) is essential for cell growth and the metabolization of fat and protein. (biolegend.com)
- Biotin-SP is our trade name for biotin with a 6-atom spacer positioned between biotin and the protein to which it is conjugated. (jacksonimmuno.com)
- It recognizes both the free and protein-conjugated (either soluble or cell bound) form of biotin. (nsjbio.com)
- Various biotin-to-protein mole equivalents (5X, 10X and 20X) were used. (vectorlabs.com)
- Avidin, a protein found in egg whites, binds strongly to biotin, impairing the absorption of the vitamin, leading to severe biotin deficiency in those who consume excessive amounts of raw eggs. (medscape.com)
Dilution2
- Optimal dilution of this antibody should be experimentally determined. (novusbio.com)
- This antibody needs to be stored at + 4°C in a fridge short term in a concentrated dilution. (igganti.com)
Concentration2
- Sandwich ELISA: To detect hRANTES by sandwich ELISA (using 100 μL/well antibody solution) a concentration of 0.25-1.0 μg/mL of this antibody is required. (fishersci.com)
- Western Blot: To detect hRANTES by Western Blot analysis this antibody can be used at a concentration of 0.1-0.2 μg/mL. (fishersci.com)
Assays4
- Guinea Pig anti-Rabbit IgG, Biotin conjugated is a secondary antibody which binds to all rabbit IgGs in immunological assays . (agrisera.com)
- Because different antibodies recognize different fragments, no standard currently exists for osteocalcin assays. (medscape.com)
- HCV-specific antibodies were detected in 376 (67.3%) serum samples using third-gen- eration enzyme immunoassay and confirmatory immunoblot assays. (who.int)
- However, these assays are susceptible to interference in patients taking biotin supplementations. (medscape.com)
Peptides1
- Fragment peptides for polyclonals give monoclonal like antibodies as the epitope is very small. (igganti.com)
Products2
- We don't routinely measure the number of biotins with our antibody products but the number of biotin molecules range from 3-6 molecules per antibody. (biolegend.com)
- Other Antibody products are available in stock. (putyourcolours.pl)
Recombinant1
- This biotinylated polyclonal antibody, in conjunction with PeproTech Polyclonal Anti-Human RANTES (500-P36) as a capture antibody, allows the detection of at least 0.2-0.4 ng/well of Recombinant hRANTES. (fishersci.com)
Immunoglobulin1
- Immunoglobulin gamma, IgG, mouse monoclonal H&L chain clones or rabbit, goat polyclonal antibodies have 4 parts. (igganti.com)
Serum4
- Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-biotin, anti-Rabbit Serum, Cat IgG, Cat IgG F(ab')2 and Cat Serum. (rockland.com)
- Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-biotin, anti-Rabbit Serum, Guinea Pig IgG, Guinea Pig IgG F(c) and Guinea Pig Serum. (rockland.com)
- They represent 70% or more of serum antibodies. (igganti.com)
- As illustrated, bovine Serum Albumin (100 ul @ 1 mg/ml) was labeled at 0, 5, 10, and 20 mole equivalents using ChromaLINK Biotin Maleimide. (vectorlabs.com)
Immunology1
- Anti-Cat IgG F(ab')2 antibody is ideal for investigators in Immunology, Cancer, and Microbiology research. (rockland.com)
Water Soluble1
- Deficiency of biotin, a water-soluble B vitamin, may occur from nutritional causes, but more commonly results from deficiencies of enzymes involved in biotin homeostasis (e.g. biotinidase deficiency ). (medscape.com)
Reacts3
- It was subsequently shown that this antibody also cross reacts with the C5b-8 complex and purified C8 alpha-gamma. (abcam.com)
- This antibody reacts with native form of human HLA-G1 on the cell surface as well as with soluble HLA-G5 isoform in its beta2-microglobulin associated form. (genetex.com)
- The maleimide group reacts with free thiol groups on biomolecules and surfaces, such as the hinge region of antibodies after mild reduction of sulfhydryl groups with TCEP or DTT. (vectorlabs.com)
Mouse1
- A dilute solution of test sample was mixed with latex particles coated with mouse monoclonal anti-CRP antibodies. (cdc.gov)
Thyroid funct1
- If you take biotin, talk to your provider before you have any thyroid function tests. (medlineplus.gov)
Detection3
- PIK3AP1 ELISA with 7A11 Capture (TA600423) and 6H6 Detection (TA700418) Antibodies. (thermofisher.com)
- Early detection and treatment with pharmacologic doses of biotin are important to prevent the development of irreversible complications. (medscape.com)
- The former was utilized for detection of anti-HCV antibodies while the Before the introduction of screening of latter was used for HCV-RNA detection and blood donors for hepatitis C virus (HCV), subsequent genotyping/subtyping. (who.int)
Azide free1
- For storage sodium azide is added or you can call us to request azide free antibody preparations. (igganti.com)
Affinity chromatography2
- Anti-Human RANTES (CCL5)-specific antibody was purified by affinity chromatography and then biotinylated. (fishersci.com)
- The antibody was purified by affinity chromatography and conjugated with biotin under optimal conditions. (biolegend.com)
Molecule2
- Biotin is a bicyclic molecule composed of a ureido ring fused with a tetrahydrothiophene ring. (medscape.com)
- Antibodies that recognize both the large amino-terminal mid-molecule fragment and the intact molecule appear to provide superior clinical information. (medscape.com)
Covalently2
- Through this carboxyl group, biotin is linked covalently to the β-amino group of lysine in 5 carboxylases that play critical roles in intermediary metabolism. (medscape.com)
- For the quantification of CRP, particles consisting of a polystyrene core and a hydrophilic shell were used in order to link anti-CRP antibodies covalently. (cdc.gov)
High affinity2
- It has a very high affinity for biotin and is excellent for use in various amplification techniques. (nsjbio.com)
- The ureido ring is involved in the high affinity binding of biotin to avidin, a glycoprotein found in egg-white. (medscape.com)
Application1
- This antibody is excellent antibody for FC application. (exbio.cz)
Gene1
- Recent studies support a role for biotin in cell proliferation, DNA repair, epigenetic gene regulation as well as normal immune function. (medscape.com)
Vitamin3
- Chronic alcoholics and those on long-term anticonvulsants could develop biotin deficiency because of impaired intestinal uptake of the vitamin. (medscape.com)
- The vitamin biotin (B7) can affect the results of many thyroid hormone tests. (medlineplus.gov)
- The patient was taking an investigational "vitamin" therapy, which turned out to be biotin, prescribed at a dose of 100 mg tid as part of a trial of high-dose biotin in X-linked adrenomyeloneuropathy. (medscape.com)
Immunoassays2
- When Biotin-SP-conjugated antibodies are used in enzyme immunoassays, there is an increase in sensitivity compared to biotin-conjugated antibodies without the spacer. (jacksonimmuno.com)
- Note: Hepatitis B virus serologies measured using biotin-based immunoassays should be interpreted with caution in MS patients using high-dose biotin, as false positives have been reported in these patients. (who.int)
Supplementation1
- Supplementation with biotin leads to clinical improvement in most cases. (medscape.com)