Epitope Mapping
Amino Acid Sequence
Molecular Sequence Data
Antibodies
Antibody Specificity
Binding Sites, Antibody
Antibodies, Neutralizing
Chromosome Mapping
Cross Reactions
Epitopes, B-Lymphocyte
Antibody Formation
Peptide Library
Immunodominant Epitopes
Antibody Affinity
Enzyme-Linked Immunosorbent Assay
Neutralization Tests
Peptide Fragments
Autoantibodies
Epitopes, T-Lymphocyte
Fluorescent Antibody Technique
Mice, Inbred BALB C
Peptide Mapping
Peptides
Binding, Competitive
Antigen-Antibody Reactions
Models, Molecular
Immunoglobulin G
Antibodies, Anti-Idiotypic
Hybridomas
Autoantigens
Base Sequence
Antigen-Antibody Complex
Recombinant Fusion Proteins
Protein Conformation
Blotting, Western
Immunoglobulin Fab Fragments
Rabbits
Antibodies, Neoplasm
Immunization
Protein Structure, Tertiary
Immune Sera
Antibodies, Antinuclear
Protein Binding
Binding Sites
Immunoblotting
Species Specificity
Cloning, Molecular
Sequence Homology, Amino Acid
T-Lymphocytes
Viral Envelope Proteins
Immunoglobulin M
HIV Antigens
Surface Plasmon Resonance
Antigens, Surface
HIV Envelope Protein gp120
Electrophoresis, Polyacrylamide Gel
HIV-1
Escherichia coli
Single-Chain Antibodies
Mutation
Immunoglobulin Variable Region
Cattle
Antibodies, Bispecific
Allergens
B-Lymphocytes
Immunoglobulin E
Antibodies, Blocking
Restriction Mapping
Sequence Alignment
Cells, Cultured
Flow Cytometry
Protein Array Analysis
Mice, Inbred C57BL
Protein Structure, Secondary
Glycoproteins
Lymphocyte Activation
Mutagenesis, Site-Directed
Microscopy, Immunoelectron
Antibodies, Heterophile
Fluorescent Antibody Technique, Indirect
Immunoglobulin A
Antibodies, Catalytic
Bacterial Outer Membrane Proteins
Lupus Erythematosus, Systemic
Brain Mapping
Antigens, Neoplasm
Gene Library
Antibodies, Monoclonal, Humanized
Immunoenzyme Techniques
Structure-Activity Relationship
T-Lymphocytes, Cytotoxic
Membrane Proteins
Amino Acid Substitution
Swine
Chickens
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.
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.
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.
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.
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.
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.
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.
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.
Chromosome mapping, also known as physical mapping, is the process of determining the location and order of specific genes or genetic markers on a chromosome. This is typically done by using various laboratory techniques to identify landmarks along the chromosome, such as restriction enzyme cutting sites or patterns of DNA sequence repeats. The resulting map provides important information about the organization and structure of the genome, and can be used for a variety of purposes, including identifying the location of genes associated with genetic diseases, studying evolutionary relationships between organisms, and developing genetic markers for use in breeding or forensic applications.
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.
An epitope is a specific region on an antigen (a substance that triggers an immune response) that is recognized and bound by an antibody or a B-lymphocyte (a type of white blood cell that produces antibodies). Epitopes are also sometimes referred to as antigenic determinants.
B-lymphocytes, or B cells, are a type of immune cell that plays a key role in the humoral immune response. They produce and secrete antibodies, which are proteins that recognize and bind to specific epitopes on antigens. When a B cell encounters an antigen, it binds to the antigen at its surface receptor, which recognizes a specific epitope on the antigen. This binding activates the B cell, causing it to divide and differentiate into plasma cells, which produce and secrete large amounts of antibody that is specific for the epitope on the antigen.
The ability of an antibody or a B cell to recognize and bind to a specific epitope is determined by the structure of the variable region of the antibody or B cell receptor. The variable region is made up of several loops of amino acids, called complementarity-determining regions (CDRs), that form a binding site for the antigen. The CDRs are highly variable in sequence and length, allowing them to recognize and bind to a wide variety of different epitopes.
In summary, an epitope is a specific region on an antigen that is recognized and bound by an antibody or a B-lymphocyte. The ability of an antibody or a B cell to recognize and bind to a specific epitope is determined by the structure of the variable region of the antibody or B cell receptor.
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.
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.
Immunodominant epitopes refer to specific regions or segments on an antigen (a molecule that can trigger an immune response) that are particularly effective at stimulating an immune response. These epitopes are often the parts of the antigen that are most recognized by the immune system, and as a result, they elicit a strong response from immune cells such as T-cells or B-cells.
In the context of T-cell responses, immunodominant epitopes are typically short peptide sequences (usually 8-15 amino acids long) that are presented to T-cells by major histocompatibility complex (MHC) molecules on the surface of antigen-presenting cells. The T-cell receptor recognizes and binds to these epitopes, triggering a cascade of immune responses aimed at eliminating the pathogen or foreign substance that contains the antigen.
In some cases, immunodominant epitopes may be the primary targets of vaccines or other immunotherapies, as they can elicit strong and protective immune responses. However, in other cases, immunodominant epitopes may also be associated with immune evasion or tolerance, where the immune system fails to mount an effective response against a pathogen or cancer cell. Understanding the properties and behavior of immunodominant epitopes is therefore crucial for developing effective vaccines and immunotherapies.
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.
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.
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.
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.
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.
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.
An epitope is a specific region on an antigen (a substance that triggers an immune response) that is recognized and bound by an antibody or a T-cell receptor. In the case of T-lymphocytes, which are a type of white blood cell that plays a central role in cell-mediated immunity, epitopes are typically presented on the surface of infected cells in association with major histocompatibility complex (MHC) molecules.
T-lymphocytes recognize and respond to epitopes through their T-cell receptors (TCRs), which are membrane-bound proteins that can bind to specific epitopes presented on the surface of infected cells. There are two main types of T-lymphocytes: CD4+ T-cells, also known as helper T-cells, and CD8+ T-cells, also known as cytotoxic T-cells.
CD4+ T-cells recognize epitopes presented in the context of MHC class II molecules, which are typically expressed on the surface of professional antigen-presenting cells such as dendritic cells, macrophages, and B-cells. CD4+ T-cells help to coordinate the immune response by producing cytokines that activate other immune cells.
CD8+ T-cells recognize epitopes presented in the context of MHC class I molecules, which are expressed on the surface of almost all nucleated cells. CD8+ T-cells are able to directly kill infected cells by releasing cytotoxic granules that contain enzymes that can induce apoptosis (programmed cell death) in the target cell.
In summary, epitopes are specific regions on antigens that are recognized and bound by T-lymphocytes through their T-cell receptors. CD4+ T-cells recognize epitopes presented in the context of MHC class II molecules, while CD8+ T-cells recognize epitopes presented in the context of MHC class I molecules.
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.
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.
Peptide mapping is a technique used in proteomics and analytical chemistry to analyze and identify the sequence and structure of peptides or proteins. This method involves breaking down a protein into smaller peptide fragments using enzymatic or chemical digestion, followed by separation and identification of these fragments through various analytical techniques such as liquid chromatography (LC) and mass spectrometry (MS).
The resulting peptide map serves as a "fingerprint" of the protein, providing information about its sequence, modifications, and structure. Peptide mapping can be used for a variety of applications, including protein identification, characterization of post-translational modifications, and monitoring of protein degradation or cleavage.
In summary, peptide mapping is a powerful tool in proteomics that enables the analysis and identification of proteins and their modifications at the peptide level.
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.
"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.
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.
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.
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.
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 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.
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 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.
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.
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.
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.
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
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.
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.
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.
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.
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.
'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.
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.
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.
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.
Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.
'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.
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.
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.
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.
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.
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.
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.
Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.
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.
Viral envelope proteins are structural proteins found in the envelope that surrounds many types of viruses. These proteins play a crucial role in the virus's life cycle, including attachment to host cells, fusion with the cell membrane, and entry into the host cell. They are typically made up of glycoproteins and are often responsible for eliciting an immune response in the host organism. The exact structure and function of viral envelope proteins vary between different types of viruses.
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.
HIV antigens refer to the proteins present on the surface or within the human immunodeficiency virus (HIV), which can stimulate an immune response in the infected individual. These antigens are recognized by the host's immune system, specifically by CD4+ T cells and antibodies, leading to their activation and production. Two significant HIV antigens are the HIV-1 p24 antigen and the gp120/gp41 envelope proteins. The p24 antigen is a capsid protein found within the viral particle, while the gp120/gp41 complex forms the viral envelope and facilitates viral entry into host cells. Detection of HIV antigens in clinical settings, such as in the ELISA or Western blot tests, helps diagnose HIV infection and monitor disease progression.
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.
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.
Surface Plasmon Resonance (SPR) is a physical phenomenon that occurs at the interface between a metal and a dielectric material, when electromagnetic radiation (usually light) is shone on it. It involves the collective oscillation of free electrons in the metal, known as surface plasmons, which are excited by the incident light. The resonance condition is met when the momentum and energy of the photons match those of the surface plasmons, leading to a strong absorption of light and an evanescent wave that extends into the dielectric material.
In the context of medical diagnostics and research, SPR is often used as a sensitive and label-free detection technique for biomolecular interactions. By immobilizing one binding partner (e.g., a receptor or antibody) onto the metal surface and flowing the other partner (e.g., a ligand or antigen) over it, changes in the refractive index at the interface can be measured in real-time as the plasmons are disturbed by the presence of bound molecules. This allows for the quantification of binding affinities, kinetics, and specificity with high sensitivity and selectivity.
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.
HIV Envelope Protein gp120 is a glycoprotein that is a major component of the outer envelope of the Human Immunodeficiency Virus (HIV). It plays a crucial role in the viral infection process. The "gp" stands for glycoprotein.
The gp120 protein is responsible for binding to CD4 receptors on the surface of human immune cells, particularly T-helper cells or CD4+ cells. This binding initiates the fusion process that allows the virus to enter and infect the cell.
After attachment, a series of conformational changes occur in the gp120 and another envelope protein, gp41, leading to the formation of a bridge between the viral and cell membranes, which ultimately results in the virus entering the host cell.
The gp120 protein is also one of the primary targets for HIV vaccine design due to its critical role in the infection process and its surface location, making it accessible to the immune system. However, its high variability and ability to evade the immune response have posed significant challenges in developing an effective HIV vaccine.
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.
Membrane glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. They are integral components of biological membranes, spanning the lipid bilayer and playing crucial roles in various cellular processes.
The glycosylation of these proteins occurs in the endoplasmic reticulum (ER) and Golgi apparatus during protein folding and trafficking. The attached glycans can vary in structure, length, and composition, which contributes to the diversity of membrane glycoproteins.
Membrane glycoproteins can be classified into two main types based on their orientation within the lipid bilayer:
1. Type I (N-linked): These glycoproteins have a single transmembrane domain and an extracellular N-terminus, where the oligosaccharides are predominantly attached via asparagine residues (Asn-X-Ser/Thr sequon).
2. Type II (C-linked): These glycoproteins possess two transmembrane domains and an intracellular C-terminus, with the oligosaccharides linked to tryptophan residues via a mannose moiety.
Membrane glycoproteins are involved in various cellular functions, such as:
* Cell adhesion and recognition
* Receptor-mediated signal transduction
* Enzymatic catalysis
* Transport of molecules across membranes
* Cell-cell communication
* Immunological responses
Some examples of membrane glycoproteins include cell surface receptors (e.g., growth factor receptors, cytokine receptors), adhesion molecules (e.g., integrins, cadherins), and transporters (e.g., ion channels, ABC transporters).
HIV-1 (Human Immunodeficiency Virus type 1) is a species of the retrovirus genus that causes acquired immunodeficiency syndrome (AIDS). It is primarily transmitted through sexual contact, exposure to infected blood or blood products, and from mother to child during pregnancy, childbirth, or breastfeeding. HIV-1 infects vital cells in the human immune system, such as CD4+ T cells, macrophages, and dendritic cells, leading to a decline in their numbers and weakening of the immune response over time. This results in the individual becoming susceptible to various opportunistic infections and cancers that ultimately cause death if left untreated. HIV-1 is the most prevalent form of HIV worldwide and has been identified as the causative agent of the global AIDS pandemic.
'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.
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.
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.
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.
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.
"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.
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.
An allergen is a substance that can cause an allergic reaction in some people. These substances are typically harmless to most people, but for those with allergies, the immune system mistakenly identifies them as threats and overreacts, leading to the release of histamines and other chemicals that cause symptoms such as itching, sneezing, runny nose, rashes, hives, and difficulty breathing. Common allergens include pollen, dust mites, mold spores, pet dander, insect venom, and certain foods or medications. When a person comes into contact with an allergen, they may experience symptoms that range from mild to severe, depending on the individual's sensitivity to the substance and the amount of exposure.
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.
Immunoglobulin E (IgE) is a type of antibody that plays a key role in the immune response to parasitic infections and allergies. It is produced by B cells in response to stimulation by antigens, such as pollen, pet dander, or certain foods. Once produced, IgE binds to receptors on the surface of mast cells and basophils, which are immune cells found in tissues and blood respectively. When an individual with IgE antibodies encounters the allergen again, the cross-linking of IgE molecules bound to the FcεRI receptor triggers the release of mediators such as histamine, leukotrienes, prostaglandins, and various cytokines from these cells. These mediators cause the symptoms of an allergic reaction, such as itching, swelling, and redness. IgE also plays a role in protecting against certain parasitic infections by activating eosinophils, which can kill the parasites.
In summary, Immunoglobulin E (IgE) is a type of antibody that plays a crucial role in the immune response to allergens and parasitic infections, it binds to receptors on the surface of mast cells and basophils, when an individual with IgE antibodies encounters the allergen again, it triggers the release of mediators from these cells causing the symptoms of an allergic reaction.
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.
Restriction mapping is a technique used in molecular biology to identify the location and arrangement of specific restriction endonuclease recognition sites within a DNA molecule. Restriction endonucleases are enzymes that cut double-stranded DNA at specific sequences, producing fragments of various lengths. By digesting the DNA with different combinations of these enzymes and analyzing the resulting fragment sizes through techniques such as agarose gel electrophoresis, researchers can generate a restriction map - a visual representation of the locations and distances between recognition sites on the DNA molecule. This information is crucial for various applications, including cloning, genome analysis, and genetic engineering.
An antigen is any substance that can stimulate an immune response, leading to the production of antibodies or activation of immune cells. In plants, antigens are typically found on the surface of plant cells and may be derived from various sources such as:
1. Pathogens: Plant pathogens like bacteria, viruses, fungi, and oomycetes have unique molecules on their surfaces that can serve as antigens for the plant's immune system. These antigens are recognized by plant pattern recognition receptors (PRRs) and trigger an immune response.
2. Endogenous proteins: Some plant proteins, when expressed in abnormal locations or quantities, can be recognized as foreign by the plant's immune system and elicit an immune response. These proteins may serve as antigens and are involved in self/non-self recognition.
3. Glycoproteins: Plant cell surface glycoproteins, which contain carbohydrate moieties, can also act as antigens. They play a role in plant-microbe interactions and may be recognized by both the plant's immune system and pathogens.
4. Allergens: Certain plant proteins can cause allergic reactions in humans and animals when ingested or inhaled. These proteins, known as allergens, can also serve as antigens for the human immune system, leading to the production of IgE antibodies and triggering an allergic response.
5. Transgenic proteins: In genetically modified plants, new proteins introduced through genetic engineering may be recognized as foreign by the plant's immune system or even by the human immune system in some cases. These transgenic proteins can serve as antigens and have been a subject of concern in relation to food safety and potential allergies.
Understanding plant antigens is crucial for developing effective strategies for plant disease management, vaccine development, and improving food safety and allergy prevention.
In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.
"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.
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.
Protein array analysis is a high-throughput technology used to detect and measure the presence and activity of specific proteins in biological samples. This technique utilizes arrays or chips containing various capture agents, such as antibodies or aptamers, that are designed to bind to specific target proteins. The sample is then added to the array, allowing the target proteins to bind to their corresponding capture agents. After washing away unbound materials, a detection system is used to identify and quantify the bound proteins. This method can be used for various applications, including protein-protein interaction studies, biomarker discovery, and drug development. The results of protein array analysis provide valuable information about the expression levels, post-translational modifications, and functional states of proteins in complex biological systems.
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.
Secondary protein structure refers to the local spatial arrangement of amino acid chains in a protein, typically described as regular repeating patterns held together by hydrogen bonds. The two most common types of secondary structures are the alpha-helix (α-helix) and the beta-pleated sheet (β-sheet). In an α-helix, the polypeptide chain twists around itself in a helical shape, with each backbone atom forming a hydrogen bond with the fourth amino acid residue along the chain. This forms a rigid rod-like structure that is resistant to bending or twisting forces. In β-sheets, adjacent segments of the polypeptide chain run parallel or antiparallel to each other and are connected by hydrogen bonds, forming a pleated sheet-like arrangement. These secondary structures provide the foundation for the formation of tertiary and quaternary protein structures, which determine the overall three-dimensional shape and function of the protein.
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.
Lymphocyte activation is the process by which B-cells and T-cells (types of lymphocytes) become activated to perform effector functions in an immune response. This process involves the recognition of specific antigens presented on the surface of antigen-presenting cells, such as dendritic cells or macrophages.
The activation of B-cells leads to their differentiation into plasma cells that produce antibodies, while the activation of T-cells results in the production of cytotoxic T-cells (CD8+ T-cells) that can directly kill infected cells or helper T-cells (CD4+ T-cells) that assist other immune cells.
Lymphocyte activation involves a series of intracellular signaling events, including the binding of co-stimulatory molecules and the release of cytokines, which ultimately result in the expression of genes involved in cell proliferation, differentiation, and effector functions. The activation process is tightly regulated to prevent excessive or inappropriate immune responses that can lead to autoimmunity or chronic inflammation.
Site-directed mutagenesis is a molecular biology technique used to introduce specific and targeted changes to a specific DNA sequence. This process involves creating a new variant of a gene or a specific region of interest within a DNA molecule by introducing a planned, deliberate change, or mutation, at a predetermined site within the DNA sequence.
The methodology typically involves the use of molecular tools such as PCR (polymerase chain reaction), restriction enzymes, and/or ligases to introduce the desired mutation(s) into a plasmid or other vector containing the target DNA sequence. The resulting modified DNA molecule can then be used to transform host cells, allowing for the production of large quantities of the mutated gene or protein for further study.
Site-directed mutagenesis is a valuable tool in basic research, drug discovery, and biotechnology applications where specific changes to a DNA sequence are required to understand gene function, investigate protein structure/function relationships, or engineer novel biological properties into existing genes or proteins.
Oligopeptides are defined in medicine and biochemistry as short chains of amino acids, typically containing fewer than 20 amino acid residues. These small peptides are important components in various biological processes, such as serving as signaling molecules, enzyme inhibitors, or structural elements in some proteins. They can be found naturally in foods and may also be synthesized for use in medical research and therapeutic applications.
Viral proteins are the proteins that are encoded by the viral genome and are essential for the viral life cycle. These proteins can be structural or non-structural and play various roles in the virus's replication, infection, and assembly process. Structural proteins make up the physical structure of the virus, including the capsid (the protein shell that surrounds the viral genome) and any envelope proteins (that may be present on enveloped viruses). Non-structural proteins are involved in the replication of the viral genome and modulation of the host cell environment to favor viral replication. Overall, a thorough understanding of viral proteins is crucial for developing antiviral therapies and vaccines.
Immunoelectron microscopy (IEM) is a specialized type of electron microscopy that combines the principles of immunochemistry and electron microscopy to detect and localize specific antigens within cells or tissues at the ultrastructural level. This technique allows for the visualization and identification of specific proteins, viruses, or other antigenic structures with a high degree of resolution and specificity.
In IEM, samples are first fixed, embedded, and sectioned to prepare them for electron microscopy. The sections are then treated with specific antibodies that have been labeled with electron-dense markers, such as gold particles or ferritin. These labeled antibodies bind to the target antigens in the sample, allowing for their visualization under an electron microscope.
There are several different methods of IEM, including pre-embedding and post-embedding techniques. Pre-embedding involves labeling the antigens before embedding the sample in resin, while post-embedding involves labeling the antigens after embedding. Post-embedding techniques are generally more commonly used because they allow for better preservation of ultrastructure and higher resolution.
IEM is a valuable tool in many areas of research, including virology, bacteriology, immunology, and cell biology. It can be used to study the structure and function of viruses, bacteria, and other microorganisms, as well as the distribution and localization of specific proteins and antigens within cells and tissues.
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.
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.
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.
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.
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.
Bacterial outer membrane proteins (OMPs) are a type of protein found in the outer membrane of gram-negative bacteria. The outer membrane is a unique characteristic of gram-negative bacteria, and it serves as a barrier that helps protect the bacterium from hostile environments. OMPs play a crucial role in maintaining the structural integrity and selective permeability of the outer membrane. They are involved in various functions such as nutrient uptake, transport, adhesion, and virulence factor secretion.
OMPs are typically composed of beta-barrel structures that span the bacterial outer membrane. These proteins can be classified into several groups based on their size, function, and structure. Some of the well-known OMP families include porins, autotransporters, and two-partner secretion systems.
Porins are the most abundant type of OMPs and form water-filled channels that allow the passive diffusion of small molecules, ions, and nutrients across the outer membrane. Autotransporters are a diverse group of OMPs that play a role in bacterial pathogenesis by secreting virulence factors or acting as adhesins. Two-partner secretion systems involve the cooperation between two proteins to transport effector molecules across the outer membrane.
Understanding the structure and function of bacterial OMPs is essential for developing new antibiotics and therapies that target gram-negative bacteria, which are often resistant to conventional treatments.
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.
Brain mapping is a broad term that refers to the techniques used to understand the structure and function of the brain. It involves creating maps of the various cognitive, emotional, and behavioral processes in the brain by correlating these processes with physical locations or activities within the nervous system. Brain mapping can be accomplished through a variety of methods, including functional magnetic resonance imaging (fMRI), positron emission tomography (PET) scans, electroencephalography (EEG), and others. These techniques allow researchers to observe which areas of the brain are active during different tasks or thoughts, helping to shed light on how the brain processes information and contributes to our experiences and behaviors. Brain mapping is an important area of research in neuroscience, with potential applications in the diagnosis and treatment of neurological and psychiatric disorders.
Capsid proteins are the structural proteins that make up the capsid, which is the protective shell of a virus. The capsid encloses the viral genome and helps to protect it from degradation and detection by the host's immune system. Capsid proteins are typically arranged in a symmetrical pattern and can self-assemble into the capsid structure when exposed to the viral genome.
The specific arrangement and composition of capsid proteins vary between different types of viruses, and they play important roles in the virus's life cycle, including recognition and binding to host cells, entry into the cell, and release of the viral genome into the host cytoplasm. Capsid proteins can also serve as targets for antiviral therapies and vaccines.
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.
A "gene library" is not a recognized term in medical genetics or molecular biology. However, the closest concept that might be referred to by this term is a "genomic library," which is a collection of DNA clones that represent the entire genetic material of an organism. These libraries are used for various research purposes, such as identifying and studying specific genes or gene functions.
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.
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.
A Structure-Activity Relationship (SAR) in the context of medicinal chemistry and pharmacology refers to the relationship between the chemical structure of a drug or molecule and its biological activity or effect on a target protein, cell, or organism. SAR studies aim to identify patterns and correlations between structural features of a compound and its ability to interact with a specific biological target, leading to a desired therapeutic response or undesired side effects.
By analyzing the SAR, researchers can optimize the chemical structure of lead compounds to enhance their potency, selectivity, safety, and pharmacokinetic properties, ultimately guiding the design and development of novel drugs with improved efficacy and reduced toxicity.
Cytotoxic T-lymphocytes, also known as CD8+ T cells, are a type of white blood cell that plays a central role in the cell-mediated immune system. They are responsible for identifying and destroying virus-infected cells and cancer cells. When a cytotoxic T-lymphocyte recognizes a specific antigen presented on the surface of an infected or malignant cell, it becomes activated and releases toxic substances such as perforins and granzymes, which can create pores in the target cell's membrane and induce apoptosis (programmed cell death). This process helps to eliminate the infected or malignant cells and prevent the spread of infection or cancer.
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).
An amino acid substitution is a type of mutation in which one amino acid in a protein is replaced by another. This occurs when there is a change in the DNA sequence that codes for a particular amino acid in a protein. The genetic code is redundant, meaning that most amino acids are encoded by more than one codon (a sequence of three nucleotides). As a result, a single base pair change in the DNA sequence may not necessarily lead to an amino acid substitution. However, if a change does occur, it can have a variety of effects on the protein's structure and function, depending on the nature of the substituted amino acids. Some substitutions may be harmless, while others may alter the protein's activity or stability, leading to disease.
"Swine" is a common term used to refer to even-toed ungulates of the family Suidae, including domestic pigs and wild boars. However, in a medical context, "swine" often appears in the phrase "swine flu," which is a strain of influenza virus that typically infects pigs but can also cause illness in humans. The 2009 H1N1 pandemic was caused by a new strain of swine-origin influenza A virus, which was commonly referred to as "swine flu." It's important to note that this virus is not transmitted through eating cooked pork products; it spreads from person to person, mainly through respiratory droplets produced when an infected person coughs or sneezes.
"Chickens" is a common term used to refer to the domesticated bird, Gallus gallus domesticus, which is widely raised for its eggs and meat. However, in medical terms, "chickens" is not a standard term with a specific definition. If you have any specific medical concern or question related to chickens, such as food safety or allergies, please provide more details so I can give a more accurate answer.
Complementary DNA (cDNA) is a type of DNA that is synthesized from a single-stranded RNA molecule through the process of reverse transcription. In this process, the enzyme reverse transcriptase uses an RNA molecule as a template to synthesize a complementary DNA strand. The resulting cDNA is therefore complementary to the original RNA molecule and is a copy of its coding sequence, but it does not contain non-coding regions such as introns that are present in genomic DNA.
Complementary DNA is often used in molecular biology research to study gene expression, protein function, and other genetic phenomena. For example, cDNA can be used to create cDNA libraries, which are collections of cloned cDNA fragments that represent the expressed genes in a particular cell type or tissue. These libraries can then be screened for specific genes or gene products of interest. Additionally, cDNA can be used to produce recombinant proteins in heterologous expression systems, allowing researchers to study the structure and function of proteins that may be difficult to express or purify from their native sources.
Bacterial display
Western blot
CD99
Immunofluorescence
Immunomics
Protein microarray
Arabinogalactan protein
FLOT1
FLOT2
Epitope
Caveolin 2
Rashna Bhandari
Rabies virus
Wnt signaling pathway
Heparan sulfate
Glypican
Glypican 3
CYP2C18
Peptide microarray
Peptide synthesis
Conformational epitope
Julie Overbaugh
Epitope mapping
Surface plasmon resonance
Dihydrolipoyl transacetylase
Pepscan
ELISpot
Ekkehard Bautz
Tamas Bartfai
MYOM1
Antibody Epitope Mapping using Biotinylated PepSets - Peptides, Peptide Synthesis, Peptide Library, Custom Peptides
Mapping of epitopes on porcine zona pellucida-3 alpha by monoclonal antibodies inhibiting oocyte-sperm interaction. | College...
Multifunctional IgG/IgM antibodies and cellular cytotoxicity are elicited by the full-length MSP1 SumayaVac-1 malaria vaccine |...
On silico peptide microarrays for high-resolution mapping of antibody epitopes and diverse protein-protein interactions -...
Bacterial display - Wikipedia
Mapping sars-cov-2 antibody epitopes in covid-19 patients with a multi-coronavirus protein microarray<...
Occupation-Associated Fatal Limbic Encephalitis Caused by Variegated Squirrel Bornavirus 1, Germany, 2013 - Volume 24, Number 6...
Mapping of epitopes on porcine zona pellucida-3 alpha by monoclonal antibodies inhibiting oocyte-sperm interaction. | College...
Selected Publications - Clinical Investigation of Host Defense Group
Anti·His Antibodies, BSA-free
Recombinant Anti-MUC1 antibody [EPR1023] KO Tested (ab109185) | Abcam
HES1 (D6P2U) Rabbit mAb | Cell Signaling Technology
Plus it
Anti-Influenza A Virus Nucleoprotein antibody [C43] (ab128193) | Abcam
RCSB PDB - 5VOB: Crystal structure of HCMV Pentamer in complex with neutralizing antibody 8I21
Drexel-SKCC/TJU Biacore S200 Surface Plasmon Resonance (SPR) Biosensor - Drexel University College of Medicine
NIOSHTIC-2 Search Results - Basic View
Versatile, Label-Free Microarray Analysis
4X PATH® Print Buffer - Grace Bio-Labs
history/2011 Therapeutic antibodies and Affibodies - The Human Protein Atlas
WikiGenes
Webinar: Beyond Epitope Mapping - POCTRN - GAITS
FITC Mouse Anti-Human IFN-γ
Pathogens | Free Full-Text | Evolutionary and Mutational Characterization of the First H5N8 Subtype Influenza A Virus in Humans
Francis Gigliotti, M.D. | UR Medicine
Camel nanobody-based B7-H3 CAR-T cells show high efficacy against large solid tumours | Nature Communications
US Patent Application for Influenza Hemagglutinin-Specific Monoclonal Antibodies for Preventing and Treating Influenza Virus...
Targeting early changes in the synovial microenvironment: a new class of immunomodulatory therapy? | Annals of the Rheumatic...
Anti-GBM Antibody Disease: Practice Essentials, Pathophysiology, Etiology
Monoclonal antibody8
- The set consisted of short overlapping peptides derived from the protein being investigated and the peptides were captured onto plate wells coated with streptavidin before completing an ELISA with each monoclonal antibody (Figure 1). (mimotopes.com)
- The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. (bdbiosciences.com)
- In another embodiment, the neutralizing antibody is a monoclonal antibody such as a mouse antibody, a humanized antibody, a chimeric antibody, or a fragment thereof. (justia.com)
- human monoclonal antibody (b96.11 huAb) and polyclonal antibodies (SMS patients' sera) were investigated. (nottingham.ac.uk)
- Anti-SUMO-2/3 Monoclonal Antibody from Cytoskeleton, Inc. (cytoskeleton.com)
- Anti-SUMO2/3 antibody is a SUMO-2/3 mouse monoclonal antibody that is part of the Signal-Seeker™ product line. (cytoskeleton.com)
- Anti-SUMO-2/3 mouse monoclonal antibody was raised against full-length recombinant SUMO-2 protein (Uniprot: P61956) combined with a proprietary mix of peptides that include CQIRFRFDGQPINE. (cytoskeleton.com)
- mostly by employing serologic methodologies and monoclonal antibody isolation and characterization. (plos.org)
Proteins13
- Antibody reactivity against overlapping 100-, 50-, and 30-amino acid fragments of SARS-CoV-2 proteins was used to identify antigenic regions. (elsevierpure.com)
- Whereas unexposed individuals had minimal reactivity against SARS-CoV-2 proteins that poorly correlated with reactivity against HCoV-NL63 and HCoV-OC43 S2 and N proteins, COVID-19 patient sera had higher correlation between SARS-CoV-2 and HCoV responses, suggesting that de novo antibodies against SARS-CoV-2 cross-react with HCoV epitopes. (elsevierpure.com)
- For the sensitivity of the three Anti·His Antibodies in detecting this panel of proteins see the figure Sensitivity of anti·His antibodies. Detection of 6xHis-tagged proteins with Anti·His Antibodies (Tetra·His Antibody in the center). A: DHFR; B: DHFR; C: thioredoxin; D: TNF-α; E: TFIIA γ ; F: chaperonin; G DNA polymerase; H: TFIIAαß; for tag location and sequences detected see table 'Proteins detected with QIA express Anti·His Antibodies'. Indicated amounts of pure 6xHis-tagged protein were applied to a nitrocellulose membrane, and detection was carried out with the Anti·His primary antibody indicated diluted 1/2000, followed by chromogenic detection with AP-conjugated rabbit anti-mouse IgG and NBT/BCIP. "> "Sensitivity of QIA express Anti·His Antibodies" ). (qiagen.com)
- The production and characterization of monoclonal antibodies against toluene diisocyanate (TDI)-conjugated proteins. (cdc.gov)
- The antibody has been shown to recognize a wide range of SUMO-2/3-targeted proteins in HeLa cell lysate (Fig. 1B) and to detect sub-nanogram amounts of recombinant SUMO-2 (Fig. 1A). (cytoskeleton.com)
- Western blots of immunoprecipitated proteins were developed using 12F3 (A) or anti-TFII-I antibody (B). (A) Star (*) and circle (o) indicate heavy and light chains of antibodies. (cytoskeleton.com)
- We sought to determine whether immune reactivity occurs between anti-SARS-CoV-2 protein antibodies and human tissue antigens, and whether molecular mimicry between COVID-19 viral proteins and human tissues could be the cause. (frontiersin.org)
- We found that SARS-CoV-2 antibodies had reactions with 28 out of 55 tissue antigens, representing a diversity of tissue groups that included barrier proteins, gastrointestinal, thyroid and neural tissues, and more. (frontiersin.org)
- We also did selective epitope mapping using BLAST and showed similarities and homology between spike, nucleoprotein, and many other SARS-CoV-2 proteins with the human tissue antigens mitochondria M2, F-actin and TPO. (frontiersin.org)
- In this mechanism, antibodies formed against SARS-CoV-2 would also bind to human tissue proteins leading to autoimmune reactivity. (frontiersin.org)
- By constant-pH Monte Carlo simulations and the PROCEEDpKa method, we have mapped the electrostatic epitopes for four monoclonal antibodies and the angiotensin-converting enzyme 2 (ACE2) on both SARS-CoV-1 and the new SARS-CoV-2 S receptor binding domain (RBD) proteins. (nih.gov)
- Octet kinetic data analysis of antibodies and target proteins in hybridoma supernatant. (opmbio.com)
- Biacore affinity analysis shows kinetic data between antibodies and target proteins. (opmbio.com)
Provided peptides1
- T-cell epitopes (Helper and Cytotoxic) are easily located using PepSets provided peptides of the correct length are used2. (mimotopes.com)
Antigen7
- This approach generates unique escape mutation profiles for each antibody which serve as a valuable resource for predicting performance of antigen tests against past, current, as well as future variants of SARS-CoV-2. (cimit.org)
- Immunization with Pneumocystis Cross-Reactive Antigen 1 (Pca1) Protects Mice against Pneumocystis Pneumonia and Generates Antibody to Pneumocystis jirovecii. (rochester.edu)
- Rational design of chimeric antigen receptor T (CAR-T) cells based on the recognition of antigenic epitopes capable of evoking the most potent CAR activation is an important objective in optimizing immune therapy. (nature.com)
- Our results highlight the importance of the specific target antigen epitope in governing optimal CAR-T activity and provide a nanobody-based B7-H3 CAR-T product for use in solid tumor therapy. (nature.com)
- Anti-glomerular basement membrane (anti-GBM) antibody disease is a rare autoimmune disorder in which circulating antibodies are directed against an antigen normally present in the GBM and alveolar basement membrane, specifically the alpha-3 chain of type IV collagen. (medscape.com)
- This extensive immune cross-reactivity between SARS-CoV-2 antibodies and different antigen groups may play a role in the multi-system disease process of COVID-19, influence the severity of the disease, precipitate the onset of autoimmunity in susceptible subgroups, and potentially exacerbate autoimmunity in subjects that have pre-existing autoimmune diseases. (frontiersin.org)
- Anti-glomerular basement membrane (anti-GBM) antibody disease is a rare autoimmune disorder in which circulating antibodies are directed against an antigen normally present in the GBM and alveolar basement membrane. (medscape.com)
Reactivity6
- Sera from confirmed COVID-19 patients as well as unexposed individuals were applied to multicoronavirus arrays to identify specific antibody reactivity. (elsevierpure.com)
- The multi-coronavirus protein microarray is a useful tool for mapping antibody reactivity in COVID-19 patients. (elsevierpure.com)
- Thus, the overall motif or GAD-6 may correspond to 523-528 aa of GAD-65 (M-S-R-L-S-K). To further define the GAD-6 epitope, sequencing or GAD-6 reactive peptides which were obtained from the successful biopanning using MI3 gene III C7C and linear 12-mers phage libraries, did not show a clear motif and did not show reactivity with GAD-6 by capture ELISA. (nottingham.ac.uk)
- The peptide sequence is conserved in mammals, birds, and amphibians, giving the antibody broad species reactivity. (cytoskeleton.com)
- The reactivity of these disease-associated autoantibodies was compared with that of antibodies raised in rats and rabbits, by immunization with various preparations derived from the 2-OADC enzymes, using immunization protocols that have successfully induced various organ-specific autoimmune diseases in animals. (edu.au)
- Moreover, the experimentally-induced antibodies in striking contrast to the natural autoantibodies showed preferential reactivity with PDC-E2 rather than with intact PDC, failed to inhibit in vitro the catalytic function of PDC, and, on peptide scanning, reacted with discrete epitopes, but at sites other than the lipoyl-binding region of PDC-E2. (edu.au)
Peptide7
- Custom synthesized biotinylated PepSets for linear antibody mapping are designed by the research scientist with help from experienced Technical Consultants at Mimotopes, and are shipped either ready to redissolve and plate or as ready-to-use plates already coated with the peptide (Figure 2). (mimotopes.com)
- This application is summarized in a separate article entitled Truncated Peptide Libraries for Cytotoxic T-Cell Epitope Mapping, available on the Mimotopes website. (mimotopes.com)
- Rodda, S.J. (2002) Peptide Libraries for T-Cell Epitope Screening and Characterization. (mimotopes.com)
- From this service, it was able to be determined that the 6 mAbs recognized specific peptide epitopes (two or three per antibody tested) that are within the extracellular domain of canine IL-4 receptor alpha. (covalx.com)
- These precise epitope investigations were performed using two different phage-displayed random peptide libraries with different characteristics (T7 phage library gene X C9C and linear 9-mers, and M13 filamentous phage library gene III C7C and linear 12-mers and gene VIII 5C4C4). (nottingham.ac.uk)
- Epitope mapping has identified that the antibody recognizes a sequence/structure within the peptide CQIRFRFDGQPINE. (cytoskeleton.com)
- The techniques for antibody analysis included immunofluorescence, immunoblotting on mitochondrial extracts, ELISAs using entire PDC, PDC-E2, or synthetic peptides, epitope mapping by peptide scanning on overlapping octameric peptides representing the human PDC-E2 sequence, affinity purification on PDC-E2, and inhibition in vitro by sera of the catalytic function of PDC. (edu.au)
Receptor7
- Clones that neutralised FBG activation of toll-like receptor 4 (TLR4), without impacting pathogenic TLR4 activation, were epitope mapped by crystallography. (bmj.com)
- The present invention discloses antibodies and blocking antibodies to canine IL-4 receptor alpha that have specific sequences and a high binding affinity for canine IL-4 receptor or α. (covalx.com)
- The present invention further discloses unique epitopes that bind to the antibodies to canine IL-4 receptor alpha. (covalx.com)
- In order to identify the epitopes that are recognized by anti-canine IL-4 receptor alpha mAbs, CovalX completed epitope mapping. (covalx.com)
- Thus, it can be suggested that because of the overlap with the epitopes recognized by the six monoclonal antibodies, there is a limited number of portions of canine Il-4 receptor alpha that these antibodies can identify within the extracellular domain. (covalx.com)
- Biacore affinity analysis of antibody and Fc receptor. (opmbio.com)
- The upper graph shows kinetic data between candidate antibodies and neonatal Fc receptor (FcRn). (opmbio.com)
Mouse monoclonal antibodies3
- Like all QIAGEN mouse monoclonal antibodies, they are prepared under serum-free conditions, which guarantees the absence of viruses, mycoplasma and contaminating immunoglobulins. (qiagen.com)
- For detection, QIA express mouse monoclonal antibodies are produced under conditions that guarantee the highest purity and activity. (qiagen.com)
- In this study, the precise epitopes in GAD-65 of three different mouse monoclonal antibodies (MoAbs) (N-terminal MoAb within amino acid residues 4-17. (nottingham.ac.uk)
Tissue culture supernatant or ascites1
- Where polyclonal antibodies are purified directly from the serum of the immunized host, and monoclonals are purified from either hybridoma-derived tissue culture supernatant or ascites, recombinant antibodies are instead purified from the tissue culture supernatants of transfected host cell lines. (cellsignal.com)
MAbs9
- By cross-competition experiments using these MAbs and several others previously described, six distinct antigenic determinants were identified and mapped. (wikigenes.org)
- Neutralizing monoclonal antibodies (MAbs), particularly those having cross-clade neutralizing activity, play a critical role in immunoprotection against various influenza A virus (IAV) infections, particularly those caused by the highly pathogenic avian influenza H5N1 virus and any future unpredictable virus strains. (justia.com)
- Neutralizing antibodies can provide a first line of defense against influenza pathogens and passive immunization with neutralizing MAbs can provide immediate effects to prevent the spread of influenza infection and mortality. (justia.com)
- Disclosed herein are neutralizing monoclonal antibodies (MAbs) specific for the surface hemagglutinin (HA) protein of the influenza H5N1 strain. (justia.com)
- For mAbs 2E2, one of the epitopes that was identified was found to have the exact same amino acid sequence as the epitope for mAbs 1 1B6. (covalx.com)
- mAbs 4D8, 1 1H2, and 1 1B6 all recognize an epitope that is from the same linear amino acid sequence. (covalx.com)
- mAbs 1 1H2, 4H3, and 2E2 all recognize another epitope that is a portion of a different linear amino acid sequence. (covalx.com)
- Finally, it was found that mAbs 4H3 and 2H2 recognize an epitope that is a portion of yet another amino acid sequence. (covalx.com)
- In this work, we evaluated 24 anti-BoNT/B monoclonal antibodies (mAbs) for their ability to inhibit the in vitro activity of BoNT/B1, /B2, /B3, /B4, and /B5 and to extract those toxins. (cdc.gov)
Sequence3
- Therefore, the M13 pVIlI 5C4C4 worked with N-terminal MoAb by expressing a relevant sequence for the N-terminal MoAb but which is unlike its epitope in GAD-65. (nottingham.ac.uk)
- Human thyroid peroxidase: complete protein sequence, chromosome mapping, and identification two alternately spliced mRNAs. (rusmedserv.com)
- The epitope recognized by clone 2H7 has been mapped to the sequence YNCEPANPSEKNSPST which lies in the large extracellular loop of human CD20. (biolegend.com)
Recognize2
- In a typical example, a library of monoclonal antibodies to a small protein, thought to recognize linear epitopes, was screened using a PepSet of biotinylated peptides (Figure 2). (mimotopes.com)
- While polyclonal antibodies are secreted by many different B cell clones and recognize multiple antigenic epitopes, monoclonals originate from a single B cell clone and are specific for just one epitope. (cellsignal.com)
Polyclonal4
- Traditional polyclonal and monoclonal antibodies are the product of normal B cell development and genetic recombination. (cellsignal.com)
- Regardless of whether an antibody is polyclonal, monoclonal or recombinant, it must always be properly validated in the intended application prior to experimental use. (cellsignal.com)
- We applied both human monoclonal anti-SARS-Cov-2 antibodies (spike protein, nucleoprotein) and rabbit polyclonal anti-SARS-Cov-2 antibodies (envelope protein, membrane protein) to 55 different tissue antigens. (frontiersin.org)
- Identification of the insulin-like growth factor I (IGF I) epitopes recognized by monoclonal and polyclonal antibodies to IGF I. Endocrinology. (medlineplus.gov)
Neutralizing antibody responses1
- Following HIV-1 infection, serum neutralizing antibody responses against the evolving autologous viral swarm are generated by the vast majority of infected subjects, usually within the first few months of infection [ 1 - 6 ]. (plos.org)
Specificity2
- At CST, we adhere to the Hallmarks of Antibody Validation™ , six complementary strategies for determining the specificity, sensitivity, and functionality of an antibody in any given assay. (cellsignal.com)
- To demonstrate specificity of staining, binding by the FITC Mouse Anti-Human IFN-γ antibody was blocked by preincubation of fixed/permeabilized cells with excess Purified Mouse Anti-Human IFN-γ antibody (Cat. (bdbiosciences.com)
Interactions1
- We also identify immunogenic surfaces important for cellular interactions by epitope mapping and functional assays. (rcsb.org)
Conformational1
- The principal targets for anti-GBM antibodies are two adjacent, conformational disulfide-bond-dependent regions in the NC1 domain of the alpha-3 chain of type IV collagen. (medscape.com)
Molecular Biology2
- Anti·His Antibodies, BSA-free are intended for molecular biology applications. (qiagen.com)
- Monoclonal antibodies to nucleic acid-containing cellular constituents: probes for molecular biology and autoimmune disease. (uiowa.edu)
Vaccine4
- The overall objective of EuroNeut-41 was to design a vaccine that raises antibodies able to prevent HIV cell fusion by blocking the virus fusion protein gp41 in its pre-fusogenic conformation. (europa.eu)
- Fifty-one vaccine candidates were designed mainly to mimic fusion intermediate conformations of gp41 and in some instance to increase exposure of the 2F5/4E10 epitopes. (europa.eu)
- The synthesis and applications of the peptides are gaining increasing popularity as a result of the developments in biotechnology and bioengineering areas and for a number of research purposes including cancer diagnosis and treatment, antibiotic drug development, epitope mapping, production of antibodies, and vaccine design. (intechopen.com)
- Broadly neutralizing HIV-1 antibodies (bNAbs) display protective potentials against experimental animal infection and thus are believed to be a key component of an effective HIV vaccine. (plos.org)
Residues3
- [ 4 ] The epitopes, designated EA and EB, are located in the NC1 domain at the amino acid residues 17-31 and 127-141, respectively. (medscape.com)
- Integral Molecular was able to identify critical binding residues for an antibody for which no mapping had been successfully done after years in development. (integralmolecular.com)
- The antigenic epitope recognized by this mAb was mapped within the residues 1-152 of EBV DNase by reacting the mAb with three distinct truncated mutants. (karger.com)
Detection3
- Anti·His Antibodies enable identification of positive expression clones by colony blotting (see figure Identification of positive expression clones by colony blotting. . "> "Identification of positive expression clones by colony blotting" ) and detection of His-tagged thioredoxin (see figure His-tagged thioredoxin detected by Penta·His Antibody in yeast cells. . "> "His-tagged thioredoxin detected by Penta·His Antibody in yeast cells" ). (qiagen.com)
- In addition, antibody detection may provide a complementary perspective, along with RT-qPCR testing, in the diagnosis of COVID-19 (24,25). (researchgate.net)
- Sera from each period ( n = 185 and n = 693) were screened in an epitope blocking enzyme immunoassay for flavivirus antibody detection. (who.int)
Affinity chromatography1
- The antibody was purified by affinity chromatography, and conjugated with PE/Cyanine7 under optimal conditions. (biolegend.com)
Recombinant protein2
- Monoclonal mouse Anti·His Antibodies (5xHis antibodies and 4xHis antibodies), like the RGS·His Antibody, BSA-free, Tetra·His Antibody, BSA-free and Penta·His Antibody, BSA-free are used to detect recombinant protein carrying His tags. (qiagen.com)
- Rapidly get your antibody or recombinant protein transiently expressed for your in vivo studies. (opmbio.com)
Serum2
- As a consequence, the identification of anti-GBM antibodies in the patient's serum or tissues is of paramount importance in the diagnosis of Goodpasture disease. (medscape.com)
- As demonstrated in Table 3, there was no significant correlation between days of symptom onset to collection of serum and antibody index/ratio to suggest waning of antibodies during the time period tested. (researchgate.net)
Amino acids6
- Disclosed herein are neutralizing antibodies with cross-neutralizing activity and cross-protective effects against divergent stains of influenza virus, which are specific for an epitope having at least 90% homology to amino acids +72-115 of the HA1 domain of H5N1 influenza virus hemagglutinin. (justia.com)
- In one embodiment disclosed herein, a neutralizing antibody specific for an epitope having at least 90% homology to amino acids +72-115 of the HA1 domain of H5N1 influenza virus hemagglutinin is provided. (justia.com)
- In another embodiment, the epitope has at least 95% or at least 98% homology to amino acids +72-115 of the HA1 domain of H5N1 influenza virus hemagglutinin. (justia.com)
- Also disclosed herein is a pharmaceutical formulation for neutralizing influenza virus comprising an antibody specific for an epitope having at least 90% homology to amino acids +72-115 of the HA1 domain of H5N1 influenza virus hemagglutinin. (justia.com)
- Also disclosed herein is a method of treating influenza virus infection in a subject in need thereof comprising administering a therapeutically effective amount of the neutralizing antibody specific for an epitope having at least 90% homology to amino acids +72-115 of the HA1 domain of H5N1 influenza virus hemagglutinin and thereby treating said influenza virus infection in said subject. (justia.com)
- Its epitope has been mapped to amino acids 155-183 (5). (ancell.com)
Rabbit2
Immunization1
- We measured neutralising antibody responses following a single immunization using pseudoviruses expressing the wild-type Spike protein or the 8 mutations found in the B.1.1.7 Spike protein. (cdc.gov)
Screening1
- All applications in biotherapeutic discovery and development such as epitope mapping and binning and antibody screening are impossible, or at least highly cumbersome, with labeled techniques. (drugdiscoverynews.com)
Species4
- The induced IgG and IgM antibodies were able to stimulate various Fc-mediated effector mechanisms associated with protection against malaria, including phagocytosis, release of reactive oxygen species, production of IFN-γ as well as complement activation and fixation. (nature.com)
- The optimal Ig concentration for an application varies by species and antibody affinity. (uiowa.edu)
- Env-based immunogens tested so far in various animal species and humans have elicited binding and autologous neutralizing antibodies but not bNAbs (with a few notable exceptions). (plos.org)
- Flavivirus antibodies were detected in 13 species, and one Australasian gannet ( Morus serrator ) from one site was positive for antibodies to Ross River virus. (who.int)
Solubility1
- Among them, 42 could be produced and characterized for solubility, oligomerization state, thermal stability, epitope exposure and structural properties. (europa.eu)
Hybridoma-based1
- In contrast, hybridoma-based systems for producing monoclonal antibodies are subject to genetic drift and instability, increasing the potential for lot-to-lot variability or loss of antibody expression. (cellsignal.com)
Viral1
- The HIV-1 envelope glycoprotein (Env) is the sole viral target of bnAbs, but is also targeted by binding, non-neutralizing antibodies. (plos.org)
Isotype2
- Anti-GBM antibodies are almost exclusively of the immunoglobulin G (IgG) isotype. (medscape.com)
- Product Name/ID: Y10b Available to For-Profits: No Alternate Antibody Name: Gene Name: Rn18s Ab Isotype: MIgG2a Gene Symbol: Antibody Registry. (uiowa.edu)
Autoimmune1
- Pulmonary and/or renal manifestations can be encountered in various conditions, such as antineutrophilic cytoplasmic antibody (ANCA)-positive vasculitis and other autoimmune disorders. (medscape.com)
Prevalence1
- Prevalence of IgM antibodies to SARS-CoV-2 was 31.4% in COVID-19 patients, 1.5% in healthcare providers, 1.3% in general workers, and 0.2% in other patients. (researchgate.net)
Flow cytometric analysis2
- The B27 antibody is useful for immunofluorescent staining and flow cytometric analysis to identify and enumerate IFN-γ producing cells within mixed cell populations. (bdbiosciences.com)
- Each lot of this antibody is quality control tested by immunofluorescent staining with flow cytometric analysis . (biolegend.com)
Ectodomain2
- In solid tumors, the B7-H3 transmembrane protein is an emerging target that harbours two distinct epitope motifs, IgC and IgV, in its ectodomain. (nature.com)
- Another design strategy was developed using gammaretroviruses backbone where 2 domains were substituted with HIV epitopes in the N-terminal part of the ectodomain and the membrane proximal external region (MPER) respectively. (europa.eu)
Methods4
- In vitro methods for producing antibodies are amenable to large-scale production, meaning antibody availability is unlikely to become a limiting factor. (cellsignal.com)
- Unlike traditional methods for antibody production, recombinant approaches avoid the need to use animals. (cellsignal.com)
- The present application is drawn to neutralizing monoclonal antibodies for preventing and treating influenza virus infection and methods of treating influenza virus infection. (justia.com)
- Methods Monoclonal antibodies recognising the fibrinogen-like globe (FBG) of tenascin-C were generated by phage display. (bmj.com)
Sensitivity1
- However, it has been previously shown that more severe disease produces a stronger antibody response, and thus our mild disease cohort may result in a lower sensitivity (26). (researchgate.net)
Recognizes1
- Antibody SMO recognizes the CD36 molecule of 88 kd (1, 3). (ancell.com)
Potent2
- In this regard, generating antibodies targeting the IgC and IgV domains of B7-H3 is helpful for identifying the potent epitope by which CARs are activated on B7-H3. (nature.com)
- Furthermore, these vaccines are limited to one or just a few strains and don't produce highly potent neutralizing antibodies or cross-reactive immunity against divergent influenza viruses. (justia.com)
Cell clones1
- We report that the variable domains of recombinant HIV-1 Env immunogens activate a large number of B cell clones that give rise to many non-neutralizing antibodies, and that removing the variable domains from the immunogen reduces the number of activated B cell lineages and leads to the development of autologous neutralizing antibodies, a step towards bNAb-production. (plos.org)
Serology1
- This information is in contrast to a study in Wuhan, China that found 10% of patients lost SARS-CoV-2 antibodies within weeks of infection (12) , although different serology tests were used in this case. (researchgate.net)
Therapeutic1
- And most recently, last month, we reported that Activiomics and Belgian biopharma UCB will apply Activiomics' Targeted In-depth Quantification of cell Signaling (TIQUAS) phospho-proteomics platform-a system that is quantitative, label-free and applicable to cell and tissue samples-in a collaborative effort to elucidate signaling mechanisms of therapeutic antibodies in relevant cell-based systems. (drugdiscoverynews.com)
Autoantibody2
- Investigation of the cryptic nature of the Goodpasture epitopes revealed 2 types of alpha-3.alpha-4.alpha-5(IV) hexamers: the autoantibody reactive M-hexamers and the autoantibody impenetrable D-hexamers. (medscape.com)
- This antibody is an autoantibody that spontaneously developed in an SLE mouse model. (uiowa.edu)
Interaction1
- Mapping of epitopes on porcine zona pellucida-3 alpha by monoclonal antibodies inhibiting oocyte-sperm interaction. (oregonstate.edu)
Inhibit2
- these antibodies inhibit cytokine release by RA synovial cells and prevent disease progression and tissue destruction during collagen-induced arthritis. (bmj.com)
- However, some antibodies inhibit or neutralize the enzymatic activity of BoNT, so the choice of antibody for toxin extraction is critical. (cdc.gov)
Structural1
- Based on physical chemical analysis and free energies estimates, we can shed some light on the involved molecular recognition processes, their clinical aspects, the implications for drug developments, and suggest structural modifications on the CR3022 antibody that would improve its binding affinities for SARS-CoV-2 and contribute to address the ongoing international health crisis. (nih.gov)
Human3
- No. 554715), then subsequently stained with 0.25 µg of FITC Mouse Anti-Human IFN-γ antibody (Cat. (bdbiosciences.com)
- Very recently, human monoclonal antibodies were approved for use on patients with COVID-19. (frontiersin.org)
- The human monoclonal antibodies used in this study are almost identical with these approved antibodies. (frontiersin.org)
Genes3
- After cloning the antibody genes into an expression vector, this is then transfected into an appropriate host cell line for antibody expression. (cellsignal.com)
- This work involves production of monoclonal antibodies, cloning of P. carinii genes (in collaboration with Dr. C.G. Haidaris and Dr. P.J. Haidaris, Departments of Microbiology and Immunology and of Medicine), and extensive use of animal models of P. carinii pneumonia. (rochester.edu)
- The two forms were equally immunogenic, but only the latter elicited neutralizing antibodies by stimulating a more restricted expansion of B cells to a narrower set of IGH/IGK/IGL-V genes that represented a small fraction (0.003-0.02%) of total B cells. (plos.org)