Immunoglobulin Fc Fragments
Receptors, Fc
Immunoglobulin G
Immunoglobulins
Immunoglobulin A
Immunoglobulin M
Immunoglobulin Fab Fragments
Immunoglobulin Fragments
Immunoglobulins, Intravenous
Immunoglobulin Heavy Chains
Staphylococcal Protein A
Binding Sites, Antibody
Peptide Fragments
Genes, Immunoglobulin
gamma-Globulins
Immunoglobulin Light Chains
Papain
Receptors, IgG
Immunoelectrophoresis
Interaction of inflammatory cells and oral microorganisms. III. Modulation of rabbit polymorphonuclear leukocyte hydrolase release response to Actinomyces viscosus and Streptococcus mutans by immunoglobulins and complement. (1/1220)
In the absence of antiserum, rabbit polymorphonuclear leukocytes (PMNs) released lysosomal enzymes in response to Actinomyces viscosus (19246) but not to Streptococcus mutans (6715). Antibodies had a marked modulating influence on these reactions. PMN hydrolase release was significantly enhanced to both organisms when specific rabbit antiserum and isolated immunoglobulin G (IgG) were included in the incubations. Immune complex F(ab')2 fragments of IgG directed against S. mutans agglutinated bacteria. Immune complexes consisting of S. mutans and F(ab')2 fragments of IgG directed against this organism were not effective as bacteria-IgG complexes in stimulating PMN release. The intensity of the release response to bacteria-IgG complexes was also diminished when PMNs were preincubated with isolated Fc fragments derived from IgG. Fresh serum as a source of complement components had no demonstrable effect on PMN release either alone or in conjuction with antiserum in these experiments. These data may be relevant to the mechanisms and consequences of the interaction of PMNs and plaque bacteria in the pathogenesis of periodontal disease. (+info)2-Deoxyglucose selectively inhibits Fc and complement receptor-mediated phagocytosis in mouse peritoneal macrophages II. Dissociation of the inhibitory effects of 2-deoxyglucose on phagocytosis and ATP generation. (2/1220)
Macrophages incubated in 2-deoxy-D-glucose (2-dG)-containing medium showed a marked decrease in cellular ATP content, and were unable to ingest IgG- and complement-coated erythrocytes via the corresponding membrane receptors for these ligands. However, the inhibitory effects of 2-dG on Fc- and C3 receptor-mediated phagocytosis were not a consequence of lowered macrophage ATP levels since addition of glucose or mannose to the culture medium restored the capacity of the macrophages to ingest IgG- and C3-coated particles without increasing ATP levels. These results indicate that Fc- and C3 receptor-mediated phagocytosis (opsonin dependent) differs qualitatively from the ingestion of latex and zymosan particles (opsonin independent); they suggest that the same regulatory molecules govern the responses of phagocytic cells to signals initiated by both the Fc and C3 receptors. The possibility that these molecules are regulated by glycosylation is discussed. (+info)The CTLA-4 gene is expressed in placental fibroblasts. (3/1220)
In order to elucidate the mechanisms that ensure survival of the allogeneic fetus, we are investigating the expression pattern of genes that are involved in peripheral self-tolerance in tissues at the maternal-fetal interface. Cytotoxic T-lymphocyte-associated protein 4 (CTLA-4) is a negative regulator of T cell activation and may modulate peripheral self-tolerance. Previously, we reported the preferential transmission of maternally-inherited shorter alleles at a 3'-UTR microsatellite locus to liveborn children, but random transmission of paternally-inherited alleles, suggesting that CTLA-4 may be involved in the maintenance of tolerance at the maternal-fetal interface. In this report, we demonstrate that CTLA-4 mRNA and protein are indeed expressed in fetal tissues at the maternal-fetal interface throughout gestation. (+info)Analysis of the interaction of monoclonal antibodies with surface IgM on neoplastic B-cells. (4/1220)
In vitro studies identified three Burkitts lymphoma cell lines, Ramos, MUTU-I and Daudi, that were growth inhibited by anti-IgM antibody. However, only Ramos and MUTU-I were sensitive to monoclonal antibodies (mAb) recognizing the Fc region of surface IgM (anti-Fc mu). Experiments using anti-Fc mu mAb (single or non-crossblocking pairs), polyclonal anti-mu Ab, and hyper-crosslinking with a secondary layer of Ab, showed that growth inhibition of B-cell lines was highly dependent on the extent of IgM crosslinking. This was confirmed by using Fab', F(ab')2 and F(ab')3 derivatives from anti-Fc mu mAb, where increasing valency caused corresponding increases in growth arrest and apoptosis, presumably as a result of more efficient BCR-crosslinking on the cell surface. The ability of a single mAb to induce growth arrest was highly dependent on epitope specificity, with mAb specific for the Fc region (C mu2-C mu4 domains) being much more effective than those recognizing the Fab region (anti-L chain, anti-Id and anti-Fd mu, or C mu1). Only when hyper-crosslinked with polyclonal anti-mouse IgG did the latter result in appreciable growth inhibition. Binding studies showed that these differences in function were not related to differences in the affinity, but probably related to intrinsic crosslinking capacity of mAb. (+info)Expression and characterization of a DNase I-Fc fusion enzyme. (5/1220)
Recombinant human deoxyribonuclease I (DNase I) is an important clinical agent that is inhaled into the airways where it degrades DNA to lower molecular weight fragments, thus reducing the viscoelasticity of sputum and improving the lung function of cystic fibrosis patients. To investigate DNases with potentially improved properties, we constructed a molecular fusion of human DNase I with the hinge and Fc region of human IgG1 heavy chain, creating a DNase I-Fc fusion protein. Infection of Sf9 insect cells with recombinant baculovirus resulted in the expression and secretion of the DNase I-Fc fusion protein. The fusion protein was purified from the culture medium using protein A affinity chromatography followed by desalting by gel filtration and was characterized by amino-terminal sequence, amino acid composition, and a variety of enzyme-linked immunosorbent assays (ELISA) and activity assays. The purified fusion contains DNase I, as determined by a DNase I ELISA and an actin-binding ELISA, and an intact antibody Fc region, which was quantified by an Fc ELISA, in a 2:1 stoichiometric ratio, respectively. The dimeric DNase I-Fc fusion was functionally active in enzymatic DNA digestion assays, albeit about 10-fold less than monomeric DNase I. Cleavage of the DNase I-Fc fusion by papain resulted in a specific activity comparable to the monomeric enzyme. Salt was inhibitory for wild type monomeric DNase I but actually enhanced the activity of the dimeric DNase I-Fc fusion. The DNase I-Fc fusion protein was also less Ca2+-dependent than DNase I itself. These results are consistent with a higher affinity of the dimeric fusion protein to DNA than monomeric DNase I. The engineered DNase I-Fc fusion protein described herein has properties that may have clinical benefits. (+info)Polymerization of IgA and IgM: roles of Cys309/Cys414 and the secretory tailpiece. (6/1220)
We have investigated how the secretory tailpiece (tp), Cys414 and the amino acids flanking Cys414 or Cys309 are involved in regulating the different polymerization of IgM and IgA to pentamers and dimers/monomers, respectively. Whereas changing the tp of IgM to that of IgA has little effect on IgM polymerization, introducing the mu tp to IgA leads to the formation of larger than wild-type IgA polymers, including pentamers and hexamer. This shows that the secretory tp can differentially regulate polymerization depending on the heavy chain context. Cys414, which is engaged in intermonomeric disulfide bonds in IgM, is not crucial for the difference in IgM and IgA polymerization; IgM with a C414S mutation forms more large polymers than IgA. Also, IgA with IgM-like mutations in the five amino acids flanking Cys309, which is homologous to Cys414, oligomerize similarly as IgA wild type. Thus, IgA appears to have an inherent tendency to form monomers and dimers that is partially regulated by the tp, while the Cys309 region has only a minor effect. We also show that complement activation by IgM is sensitive to alterations in the polymeric structure, while IgA is inactive in classical complement activation even for polymers such as pentamers and hexamers. (+info)Small-angle X-ray studies of the Fab and Fc fragments from the human immunoglobulin molecule Kol. (7/1220)
The conformation of the Fab and Fc fragments from the human immunoglobulin molecule Kol [IgI I, chi2gamma2, Gm(f)+] was studied by small-angle x-ray scattering in solution. The fragments were studied in 0.02 M Tris-HCl buffer. For the Fab fragment the radius of gyration was found to be 3.15 +/- 0.15 nm, the volume to be 75 +/- 8 nm3. For the Fc fragment the respective values were 3.15 +/- 0.15 nm for the radius of gyration and 91 +/- 8 nm3 for the volume. A large number of models were calculated for both fragments to find models which fit these data and have the same scattering curve. The models with the best agreement were compared with the models found for the crystalline state by crystal x-ray studies. (+info)A human histocompatibility leukocyte antigen (HLA)-G-specific receptor expressed on all natural killer cells. (8/1220)
Human natural killer (NK) cells express several killer cell immunoglobulin (Ig)-like receptors (KIRs) that inhibit their cytotoxicity upon recognition of human histocompatibility leukocyte antigen (HLA) class I molecules on target cells. Additional members of the KIR family, including some that deliver activation signals, have unknown ligand specificity and function. One such KIR, denoted KIR2DL4, is structurally divergent from other KIRs in the configuration of its two extracellular Ig domains and of its transmembrane and cytoplasmic domains. Here we show that recombinant soluble KIR2DL4 binds to cells expressing HLA-G but not to cells expressing other HLA class I molecules. Unlike other HLA class I-specific KIRs, which are clonally distributed on NK cells, KIR2DL4 is expressed at the surface of all NK cells. Furthermore, functional transfer of KIR2DL4 into the cell line NK-92 resulted in inhibition of lysis of target cells that express HLA-G, but not target cells that express other class I molecules including HLA-E. Therefore, given that HLA-G expression is restricted to fetal trophoblast cells, KIR2DL4 may provide important signals to maternal NK decidual cells that interact with trophoblast cells at the maternal-fetal interface during pregnancy. (+info)Immunoglobulin Fc fragments are the crystallizable fragment of an antibody that is responsible for effector functions such as engagement with Fc receptors on immune cells, activation of the complement system, and neutralization of toxins. The Fc region is located at the tail end of the Y-shaped immunoglobulin molecule, and it is made up of constant regions of the heavy chains of the antibody.
When an antibody binds to its target antigen, the Fc region can interact with other proteins in the immune system, leading to a variety of responses such as phagocytosis, antibody-dependent cellular cytotoxicity (ADCC), and complement activation. These effector functions help to eliminate pathogens and infected cells from the body.
Immunoglobulin Fc fragments can be produced artificially through enzymatic digestion of intact antibodies, resulting in a fragment that retains the ability to interact with Fc receptors and other proteins involved in immune responses. These fragments have potential therapeutic applications in a variety of diseases, including autoimmune disorders, inflammatory conditions, and cancer.
Fc receptors (FcRs) are specialized proteins found on the surface of various immune cells, including neutrophils, monocytes, macrophages, eosinophils, basophils, mast cells, and B lymphocytes. They play a crucial role in the immune response by recognizing and binding to the Fc region of antibodies (IgG, IgA, and IgE) after they have interacted with their specific antigens.
FcRs can be classified into several types based on the class of antibody they bind:
1. FcγRs - bind to the Fc region of IgG antibodies
2. FcαRs - bind to the Fc region of IgA antibodies
3. FcεRs - bind to the Fc region of IgE antibodies
The binding of antibodies to Fc receptors triggers various cellular responses, such as phagocytosis, degranulation, and antibody-dependent cellular cytotoxicity (ADCC), which contribute to the elimination of pathogens, immune complexes, and other foreign substances. Dysregulation of Fc receptor function has been implicated in several diseases, including autoimmune disorders and allergies.
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.
Immunoglobulins (Igs), also known as antibodies, are glycoprotein molecules produced by the immune system's B cells in response to the presence of foreign substances, such as bacteria, viruses, and toxins. These Y-shaped proteins play a crucial role in identifying and neutralizing pathogens and other antigens, thereby protecting the body against infection and disease.
Immunoglobulins are composed of four polypeptide chains: two identical heavy chains and two identical light chains, held together by disulfide bonds. The variable regions of these chains form the antigen-binding sites, which recognize and bind to specific epitopes on antigens. Based on their heavy chain type, immunoglobulins are classified into five main isotypes or classes: IgA, IgD, IgE, IgG, and IgM. Each class has distinct functions in the immune response, such as providing protection in different body fluids and tissues, mediating hypersensitivity reactions, and aiding in the development of immunological memory.
In medical settings, immunoglobulins can be administered therapeutically to provide passive immunity against certain diseases or to treat immune deficiencies, autoimmune disorders, and other conditions that may benefit from immunomodulation.
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.
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.
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.
Immunoglobulin fragments refer to the smaller protein units that are formed by the digestion or break-down of an intact immunoglobulin, also known as an antibody. Immunoglobulins are large Y-shaped proteins produced by the immune system to identify and neutralize foreign substances such as pathogens or toxins. They consist of two heavy chains and two light chains, held together by disulfide bonds.
The digestion or break-down of an immunoglobulin can occur through enzymatic cleavage, which results in the formation of distinct fragments. The most common immunoglobulin fragments are:
1. Fab (Fragment, antigen binding) fragments: These are formed by the digestion of an intact immunoglobulin using the enzyme papain. Each Fab fragment contains a single antigen-binding site, consisting of a portion of one heavy chain and one light chain. The Fab fragments retain their ability to bind to specific antigens.
2. Fc (Fragment, crystallizable) fragments: These are formed by the digestion of an intact immunoglobulin using the enzyme pepsin or through the natural breakdown process in the body. The Fc fragment contains the constant region of both heavy chains and is responsible for effector functions such as complement activation, binding to Fc receptors on immune cells, and antibody-dependent cellular cytotoxicity (ADCC).
These immunoglobulin fragments play crucial roles in various immune responses and diagnostic applications. For example, Fab fragments can be used in immunoassays for the detection of specific antigens, while Fc fragments can mediate effector functions that help eliminate pathogens or damaged cells from the body.
Intravenous Immunoglobulins (IVIG) are a preparation of antibodies, specifically immunoglobulins, that are derived from the plasma of healthy donors. They are administered intravenously to provide passive immunity and help boost the immune system's response in individuals with weakened or compromised immune systems. IVIG can be used for various medical conditions such as primary immunodeficiency disorders, secondary immunodeficiencies, autoimmune diseases, and some infectious diseases. The administration of IVIG can help prevent infections, reduce the severity and frequency of infections, and manage the symptoms of certain autoimmune disorders. It is important to note that while IVIG provides temporary immunity, it does not replace a person's own immune system.
Immunoglobulin heavy chains are proteins that make up the framework of antibodies, which are Y-shaped immune proteins. These heavy chains, along with light chains, form the antigen-binding sites of an antibody, which recognize and bind to specific foreign substances (antigens) in order to neutralize or remove them from the body.
The heavy chain is composed of a variable region, which contains the antigen-binding site, and constant regions that determine the class and function of the antibody. There are five classes of immunoglobulins (IgA, IgD, IgE, IgG, and IgM) that differ in their heavy chain constant regions and therefore have different functions in the immune response.
Immunoglobulin heavy chains are synthesized by B cells, a type of white blood cell involved in the adaptive immune response. The genetic rearrangement of immunoglobulin heavy chain genes during B cell development results in the production of a vast array of different antibodies with unique antigen-binding sites, allowing for the recognition and elimination of a wide variety of pathogens.
Staphylococcal Protein A (SpA) is a cell wall-associated protein found on many strains of the bacterium Staphylococcus aureus. It plays an important role in the pathogenesis of staphylococcal infections. SpA has several domains that allow it to bind to various host proteins, including immunoglobulins (Igs), complement components, and fibrinogen.
The protein A's ability to bind to the Fc region of Igs, particularly IgG, enables it to inhibit phagocytosis by masking the antibodies' binding sites, thus helping the bacterium evade the host immune system. Additionally, SpA can activate complement component C1 and initiate the classical complement pathway, leading to the release of anaphylatoxins and the formation of the membrane attack complex, which can cause tissue damage.
Furthermore, SpA's binding to fibrinogen promotes bacterial adherence and colonization of host tissues, contributing to the establishment of infection. Overall, Staphylococcal Protein A is a crucial virulence factor in S. aureus infections, making it an important target for the development of novel therapeutic strategies.
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.
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.
Immunoglobulins (Igs), also known as antibodies, are proteins produced by the immune system to recognize and neutralize foreign substances such as pathogens or toxins. They are composed of four polypeptide chains: two heavy chains and two light chains, which are held together by disulfide bonds. The variable regions of the heavy and light chains contain loops that form the antigen-binding site, allowing each Ig molecule to recognize a specific epitope (antigenic determinant) on an antigen.
Genes encoding immunoglobulins are located on chromosome 14 (light chain genes) and chromosomes 22 and 2 (heavy chain genes). The diversity of the immune system is generated through a process called V(D)J recombination, where variable (V), diversity (D), and joining (J) gene segments are randomly selected and assembled to form the variable regions of the heavy and light chains. This results in an enormous number of possible combinations, allowing the immune system to recognize and respond to a vast array of potential threats.
There are five classes of immunoglobulins: IgA, IgD, IgE, IgG, and IgM, each with distinct functions and structures. For example, IgG is the most abundant class in serum and provides long-term protection against pathogens, while IgA is found on mucosal surfaces and helps prevent the entry of pathogens into the body.
Myeloma proteins, also known as monoclonal immunoglobulins or M-proteins, are entire or abnormal immunoglobulin (antibody) molecules produced by a single clone of plasma cells, which are malignant in the case of multiple myeloma and some related disorders. These proteins accumulate in the blood and/or urine and can cause damage to various organs and tissues.
In multiple myeloma, the excessive proliferation of these plasma cells leads to the overproduction of a single type of immunoglobulin or its fragments, which can be detected and quantified in serum and/or urine electrophoresis. The most common types of myeloma proteins are IgG and IgA, followed by light chains (Bence Jones proteins) and, less frequently, IgD and IgM.
The presence and levels of myeloma proteins are important diagnostic markers for multiple myeloma and related disorders, such as monoclonal gammopathy of undetermined significance (MGUS) and Waldenström macroglobulinemia. Regular monitoring of these proteins helps assess the disease's activity, response to treatment, and potential complications like kidney dysfunction or amyloidosis.
Gamma-globulins are a type of protein found in the blood serum, specifically a class of immunoglobulins (antibodies) known as IgG. They are the most abundant type of antibody and provide long-term defense against bacterial and viral infections. Gamma-globulins can also be referred to as "gamma globulin" or "gamma immune globulins."
These proteins are produced by B cells, a type of white blood cell, in response to an antigen (a foreign substance that triggers an immune response). IgG gamma-globulins have the ability to cross the placenta and provide passive immunity to the fetus. They can be measured through various medical tests such as serum protein electrophoresis (SPEP) or immunoelectrophoresis, which are used to diagnose and monitor conditions related to immune system disorders, such as multiple myeloma or primary immunodeficiency diseases.
In addition, gamma-globulins can be administered therapeutically in the form of intravenous immunoglobulin (IVIG) to provide passive immunity for patients with immunodeficiencies, autoimmune disorders, or infectious diseases.
Immunoglobulin light chains are the smaller protein subunits of an immunoglobulin, also known as an antibody. They are composed of two polypeptide chains, called kappa (κ) and lambda (λ), which are produced by B cells during the immune response. Each immunoglobulin molecule contains either two kappa or two lambda light chains, in association with two heavy chains.
Light chains play a crucial role in the antigen-binding site of an antibody, where they contribute to the specificity and affinity of the interaction between the antibody and its target antigen. In addition to their role in immune function, abnormal production or accumulation of light chains can lead to various diseases, such as multiple myeloma and amyloidosis.
Papain is defined as a proteolytic enzyme that is derived from the latex of the papaya tree (Carica papaya). It has the ability to break down other proteins into smaller peptides or individual amino acids. Papain is widely used in various industries, including the food industry for tenderizing meat and brewing beer, as well as in the medical field for its digestive and anti-inflammatory properties.
In medicine, papain is sometimes used topically to help heal burns, wounds, and skin ulcers. It can also be taken orally to treat indigestion, parasitic infections, and other gastrointestinal disorders. However, its use as a medical treatment is not widely accepted and more research is needed to establish its safety and efficacy.
IgG receptors, also known as Fcγ receptors (Fc gamma receptors), are specialized protein molecules found on the surface of various immune cells, such as neutrophils, monocytes, macrophages, and some lymphocytes. These receptors recognize and bind to the Fc region of IgG antibodies, one of the five classes of immunoglobulins in the human body.
IgG receptors play a crucial role in immune responses by mediating different effector functions, including:
1. Antibody-dependent cellular cytotoxicity (ADCC): IgG receptors on natural killer (NK) cells and other immune cells bind to IgG antibodies coated on the surface of virus-infected or cancer cells, leading to their destruction.
2. Phagocytosis: When IgG antibodies tag pathogens or foreign particles, phagocytes like neutrophils and macrophages recognize and bind to these immune complexes via IgG receptors, facilitating the engulfment and removal of the targeted particles.
3. Antigen presentation: IgG receptors on antigen-presenting cells (APCs) can internalize immune complexes, process the antigens, and present them to T cells, thereby initiating adaptive immune responses.
4. Inflammatory response regulation: IgG receptors can modulate inflammation by activating or inhibiting downstream signaling pathways in immune cells, depending on the specific type of Fcγ receptor and its activation state.
There are several types of IgG receptors (FcγRI, FcγRII, FcγRIII, and FcγRIV) with varying affinities for different subclasses of IgG antibodies (IgG1, IgG2, IgG3, and IgG4). The distinct functions and expression patterns of these receptors contribute to the complexity and fine-tuning of immune responses in the human body.
Immunoelectrophoresis (IEP) is a laboratory technique used in the field of clinical pathology and immunology. It is a method for separating and identifying proteins, particularly immunoglobulins or antibodies, in a sample. This technique combines the principles of electrophoresis, which separates proteins based on their electric charge and size, with immunological reactions, which detect specific proteins using antigen-antibody interactions.
In IEP, a protein sample is first separated by electrophoresis in an agarose or agar gel matrix on a glass slide or in a test tube. After separation, an antibody specific to the protein of interest is layered on top of the gel and allowed to diffuse towards the separated proteins. This creates a reaction between the antigen (protein) and the antibody, forming a visible precipitate at the point where they meet. The precipitate line's position and intensity can then be analyzed to identify and quantify the protein of interest.
Immunoelectrophoresis is particularly useful in diagnosing various medical conditions, such as immunodeficiency disorders, monoclonal gammopathies (like multiple myeloma), and other plasma cell dyscrasias. It can help detect abnormal protein patterns, quantify specific immunoglobulins, and identify the presence of M-proteins or Bence Jones proteins, which are indicative of monoclonal gammopathies.
IGHG3
Nociceptin receptor
Fragment antigen-binding
Fragment crystallizable region
Fcab
F-star
Bispecific monoclonal antibody
List of MeSH codes (D12.776.124)
Subcommissural organ
Belatacept
IGLL1
Immunoglobulin heavy constant alpha 1
Macrophage
Efgartigimod alfa
Pneumococcal pneumonia
Antibody
Small modular immunopharmaceutical
Nomenclature of monoclonal antibodies
FCGR2B
Telitacicept
FCMR
SpAB protein domain
Protein A
Recombinant antibodies
FCAR
Primary and secondary antibodies
FCGR2C
TREM2
CD4 immunoadhesin
Snake antivenom
Immunoglobulin F(ab) and F(ab')2 fragments | Abcam
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Antibodies22
- Use of immunoglobulin fragments eliminates non-specific binding between the Fc portions of antibodies and the Fc receptor on cells. (abcam.com)
- In contrast, F(ab') 2 fragment antibodies are generated by pepsin digestion of whole IgG antibodies (See below IgG structure) to remove most of the Fc region while leaving intact some of the hinge region. (abcam.com)
- Eliminate non-specific binding between Fc portions of antibodies and Fc receptors on cells (such as macrophages, dendritic cells, neutrophils, NK cells and B cells). (abcam.com)
- As fragment antibodies do not have Fc portions, they do not interfere with anti-Fc mediated antibody detection. (abcam.com)
- F(ab) fragments are used to block endogenous immunoglobulins on cells, tissues and exposed immunoglobulins in multiple labeling experiments using primary antibodies from the same species. (abcam.com)
- These antibodies are not recommended for blocking immunoglobulins in WB and ELISA. (abcam.com)
- We recommend using normal serum with these antibodies to prevent the binding to Fc receptors. (abcam.com)
- The effector functions elicited by the fragment crystallizable (Fc) region of immunoglobulin G (IgG) antibodies are subject to variation by the presence of terminal sialic acid (Sia) residues at asparagine-297 (Asn-297). (scirp.org)
- Immunoglobulins (antibodies) are the glycoproteins involved in the immune response. (visualscience.ru)
- The monospecific and bivalent characteristics of naturally occurring immunoglobulin G (IgG) antibodies depend on homodimerization of the fragment crystallizable (Fc) regions of two identical heavy chains (HCs) and the subsequent assembly of two identical light chains (LCs) via disulfide linkages between each HC and LC. (nih.gov)
- Based on their ability to enforce heterodimerization between the two different HCs, the established Fc heterodimers have been extensively exploited as a scaffold to generate bispecific antibodies (bsAbs) in full-length IgG and IgG-like formats. (nih.gov)
- Antibodies directed against the Fc fragment of immunoglobulin G (IgG) are called rheumatoid factors (RFs). (medscape.com)
- Antibodies are glycoproteins belonging to the immunoglobulin superfamily . (wikipedia.org)
- Some authors propose a role for an antibody-mediated pathogenesis supported by: (1) reports that up to 30% of patients have antibodies against myelin proteins, (2) reports that there is deposition of immunoglobulin and complement in sural nerve biopsies, and (3) therapeutic response to intravenous immunoglobulins and plasma exchange. (medlink.com)
- 10 However, many bDMARDs such as TNFis contain an Fc region that RF antibodies bind to, which can result in a lower clinical efficacy and the need for additional interventions. (cybertrontv.com)
- Antibodies (immunoglobulin (Ig) A, IgD, IgE, IgG, IgM) are secreted by B-cells that are activated to plasma cells after antigen presentation in regional lymph nodes or secondary lymphoid organs ( Figure 1 ) [ 9 ] . (encyclopedia.pub)
- However, to date, the role and biomarker potential of IgG Fc region N-glycosylation, which affects the function of antibodies, have not been examined in BC. (elsevierpure.com)
- Most of these immunomodulatory antibodies are of IgG isotypes that have low, or no, binding to the Fc gamma receptors (FcγRs) that trigger cell-mediated cytotoxic effector functions such as antibody dependent cellular cytotoxicity (ADCC) and phagocytosis (ADCP). (bmj.com)
- However, recent preclinical data highlight a potential role for FcγR engagement in the activity of such antibodies. (bmj.com)
- Here we review the biology of the FcγRs and IgG isotypes in both humans and mice, detail the potential roles that FcγR interactions can play in the activity of monoclonal antibodies in general, and of immunomodulatory antibodies in particular, and discuss how preclinical studies on these interactions might be best interpreted and translated to a human setting. (bmj.com)
- Antibodies of the IgG sub-class are bi-functional molecules, possessing a F(ab) domain, variable in sequence and responsible for the binding of antigen, and an Fc domain, constant in sequence and responsible for mediating a range of antibody effector functions [ 1 ]. (bmj.com)
- The important bacterial pathogen Streptococcus pyogenes secretes IdeS (immunoglobulin G-degrading enzyme of S. pyogenes), a proteinase that cleaves human immunoglobulin G (IgG) antibodies in the hinge region resulting in Fc (fragment crystallizable) and F(ab') 2 (fragment antigen-binding) fragments and protects the bacteria against phagocytic killing. (lu.se)
Receptor11
- The use of F(ab') 2 fragments also avoids unspecific binding to Fc receptor on live cells or to Protein A/G. (abcam.com)
- Cells infected with herpes simplex virus type 1 (HSV-1) express a cell surface receptor able to bind to the Fc region of immunoglobulin G (IgG). (lu.se)
- Unlabelled IgG and IgG Fc fragments inhibited the interaction between 125I-labelled rabbit IgG Fc and the HSV Fc receptor, whereas F(ab')2, Facb and pFc' fragments failed to inhibit this interaction. (lu.se)
- These data indicate that the HSV Fc receptor requires both the C gamma 2 and C gamma 3 domains for interaction with the IgG molecule analogous to the known interaction of protein A of Staphylococcus aureus, the Fc binding proteins of Group A, C and G streptococci, and certain human rheumatoid factors. (lu.se)
- In both cases, the long half-life is due to their molecular size above the renal clearance threshold and their interaction with a membrane-bound receptor named the neonatal Fc receptor (FcRn). (nature.com)
- The Fc glycan modulates biological effector functions, including antibody-dependent cellular cytotoxicity (ADCC) which is mediated in part through the activatory Fc receptor, FcγRIIIA. (ox.ac.uk)
- The high-affinity receptor for immunoglobulin E (IgE), FcepsilonRI, is an alphabetagamma2 tetramer found on mast cells, basophils, and several other types of immune effector cells. (ox.ac.uk)
- Receptors bind the Fc portion of human IgG and often this fragment is removed from immunoglobulins to minimize receptor binding and lower background reactivity. (rockland.com)
- Receptor for the Fc region of complexed immunoglobulins gamma. (cusabio.com)
- Receptor for the Fc region of IgG. (lu.se)
- Exists as a hetero-oligomeric receptor complex with Fc epsilon receptor I gamma subunit and / or the CD3 zeta subunit. (lu.se)
Receptors4
- The terms antibody and immunoglobulin are often used interchangeably, [1] though the term 'antibody' is sometimes reserved for the secreted, soluble form, i.e. excluding B-cell receptors. (wikipedia.org)
- Siglecs are a family of sialic acid-binding immunoglobulin-like receptors predominantly expressed on cells of immune system to regulate their functions through recognizing their glycan ligands [ 5 ]. (biomedcentral.com)
- This effect was broadly recapitulated for other Fc receptors (FcγRI, FcγRIIA, FcγRIIB, and FcγRIIIB). (ox.ac.uk)
- Engineering of the protein-carbohydrate interface thus provides an independent parameter in the engineering of Fc effector functions and a route to the synthesis of new classes of Fc domain with novel combinations of affinities for activatory and inhibitory Fc receptors. (ox.ac.uk)
Crystallizable fragment2
- The third component of the molecule is called the Fc-fragment (crystallizable fragment) and is comprised of the invariable CH2 and CH3 domains of the heavy chains. (visualscience.ru)
- Herein, we report that breast cancer (BC) patients can be distinguished from cancer-free (NC) controls by serum immunoglobulin G (IgG) crystallizable fragment (Fc) region N-glycosylation profiling using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). Recently, there has been much progress in the field of tumor immunology. (elsevierpure.com)
Affinity8
- Wozniak-Knopp G, Stadlmayr G, Perthold JW, Stadlbauer K, Woisetschläger M, Sun H, Rüker F. Designing Fcabs: well-expressed and stable high affinity antigen-binding Fc fragments. (boku.ac.at)
- Two complementary, multiplexed detection assays for ActRIIB-Fc were developed by using affinity purification in combination with either proteolytic digestion and LC-HRMS, or Western blotting. (wada-ama.org)
- in case of the model compound GDF-15/Fc, the available reference materials were found to be of substandard quality and w provided as multimer, which significantly interfered with affinity purification process due to the elimination of its binding capability. (wada-ama.org)
- Members of the IgG class of immunoglobulins can be subdivided according to their biochemical features, which include their affinity for complement system proteins and their concentration in the plasma [4]. (visualscience.ru)
- Consistent with previous reports, we found that site-directed mutations disrupting the protein-carbohydrate interface (F241A, F243A, V262E, and V264E) increased galactosylation and sialylation of the Fc and, concomitantly, reduced the affinity for FcγRIIIA. (ox.ac.uk)
- However, a glycan-engineered IgG1 with hypergalactosylated and hypersialylated glycans exhibited unchanged binding affinity to FcγRIIIA. (ox.ac.uk)
- Moreover, when we expressed these mutants as a chemically uniform (Man5GlcNAc2) glycoform, the individual effect of each mutation on FcγRIIIA affinity was preserved. (ox.ac.uk)
- The mixed SAMs were characterized, and hexameric peptide ligand His-Trp-Arg-Gly-Trp-Val (HWRGWV), which shows affinity binding toward the Fc (constant fragment) of human immunoglobulin (IgG), was grafted onto different dilutions of EG6NH2–EG3OH mixed SAMs for preparation of IgG detection surfaces. (ncsu.edu)
IgG17
- Wozniak-Knopp G, Stadlmann J, Rüker F. Stabilisation of the Fc fragment of human IgG1 by engineered intradomain disulfide bonds. (boku.ac.at)
- Biologically active conformations of the IgG1 Fc homodimer are maintained by multiple hydrophobic interactions between the protein surface and the N-glycan. (ox.ac.uk)
- We rationalized this effect by crystallographic analysis of the IgG1 Fc F241A mutant, determined here to a resolution of 1.9 Å, which revealed localized destabilization of this glycan-protein interface. (ox.ac.uk)
- We fused a 5′ terminal cDNA fragments for the Fab region of 2H8 mAb with 3′ terminal cDNA fragments for Fc region of human IgG1. (morulaivf.com)
- We report the in vivo pharmacokinetics of a broad-spectrum vaccinia virus CC chemokine binding protein (35 K) fused to human IgG1 Fc. (ox.ac.uk)
- Among anti-S memory B lymphocytes, the frequency of immunoglobulin G4 subclass-switched B lymphocytes (from IgG1 and IgG3 to IgG4) was 14.0% (median) compared to the repertoire of memory B lymphocytes (median of 1.0%) post-booster doses. (news-medical.net)
- Initially announced in January 2018, this acquisition strengthens Sanofi's position in hematology and specialty medicines by adding Bioverativ's Eloctate (recombinant fusion protein composed of human immunoglobulin[IG] G1-Fc linked cleavage factor VIII) and Alprolix (recombinant fusion protein composed of IX coagulation factor IX Fc fragment of IgG1) for the treatment of hemophilia A and hemophilia B, respectively, to Sanofi's hemophilia portfolio. (biopharminternational.com)
Proteins10
- While EPO-Fc can be simultaneously detected with other recombinant erythropoietins by routine doping control assays, there are currently no tests for other doping-relevant Fc-fusion proteins such as the myostatin inhibitor ActRIIB-Fc (ACE031) or the cytokine GDF15/Fc, which is a member of the transforming growth factor beta (TGFβ) superfamily. (wada-ama.org)
- Within this study, a proteomics-based detection assay for emerging Fc-fusion proteins relevant as performance-enhancing agents in sports will be developed. (wada-ama.org)
- The proactive development detection assays for therapeutic Fc-fusion proteins, TGFβ cytokines and TGFβ inhibitors is of great interest as several drugs of these categories are already available on the black market as well as for research purposes. (wada-ama.org)
- The aim of this research project was to develop detection assays for two emerging Fc-fusion proteins potentially relevant as performance-enhancing agents in sports: The TGF-β cytokine GDF-15/Fc and an ActRIIB-Fc fusion protein related to the TGF-β/myostatin inhibitor ACE-031. (wada-ama.org)
- Both approaches can readily be modified to include other ActRII-Fc fusion proteins such as Luspatercept (modified ActRIIB-Fc). (wada-ama.org)
- In addition to bsAbs, heterodimeric Fc technology is very promising for the generation of Fc-fused proteins and peptides, as well as cytokines (immunocytokines), which can present the fusion partners in the natural monomeric or heterodimeric form rather than the artificial homodimeric form with wild-type Fc. (nih.gov)
- Here, we present relevant concepts and strategies for the generation of heterodimeric Fc proteins, and their application in the development of bsAbs in diverse formats for optimal biological activity. (nih.gov)
- In addition, we describe wild-type Fc-fused monomeric and heterodimeric proteins, along with the difficulties associated with their preparations, and discuss the use of heterodimeric Fc as an alternative scaffold of wild-type Fc for naturally monomeric or heterodimeric proteins, to create Fc-fusion proteins with novel therapeutic modality. (nih.gov)
- The direct comparison with other rhEpo-Fc fusion proteins failed, because no appropriate data were found in the literature. (boku.ac.at)
- Hydrodynamic Gene Delivery of CC Chemokine Binding Fc Fusion Proteins to Target Acute Vascular Inflammation In Vivo. (ox.ac.uk)
Antigens3
- The F(ab) fragment is an antibody structure that still binds to antigens but is monovalent with no Fc portion. (abcam.com)
- However, as opposed to F(ab) fragments, F(ab') 2 fragments can both bind and precipitate antigens thanks to their two binding sites. (abcam.com)
- Immunoglobulins recognize and bind antigens and can be found in the plasma linked to lymphocyte cellular membranes. (visualscience.ru)
Antigen6
- F(ab') 2 fragments have two antigen-binding F(ab) portions linked together by disulfide bonds, and therefore are divalent with a molecular weight of about 110 kDa. (abcam.com)
- Divalent antibody fragments (F(ab') 2 fragments) are smaller than whole IgG molecules and enable a better penetration into tissue thus faciliting better antigen recognition in IHC. (abcam.com)
- Sádio F, Stadlmayr G, Stadlbauer K, Rüker F, Wozniak-Knopp G. Yeast Surface Display and Cell Sorting of Antigen-Binding Fc Fragments. (boku.ac.at)
- Together with the two other constant regions of the heavy and light chains, CH1 and CL, respectively, these regions form one of two Fab fragments (antigen binding fragment). (visualscience.ru)
- IgGs, the most common human immunoglobulins, represent 75% of all plasma immunoglobulins and have several functions including triggering the complement system (the proteolytic plasma enzyme cascade involved in antigen degradation in the blood). (visualscience.ru)
- Structurally an antibody is also partitioned into two antigen-binding fragments (Fab), containing one V L , V H , C L , and C H 1 domain each, as well as the crystallisable fragment (Fc), forming the trunk of the Y shape. (wikipedia.org)
Protein11
- Fc-fusion based drugs are an emerging class of pharmaceuticals which already found their way into competitive sports: EPO-Fc is an erythropoiesis-stimulating agent where the attachment of two immunoglobulin Fc domains to the protein results in a prolonged therapeutic activity due to an increased plasma half-life and enables administration via inhalation. (wada-ama.org)
- 2006): Biochemical characterization of rhEpo-Fc fusion protein expressed in CHO cells. (boku.ac.at)
- In this context, we have expressed a homodimer fusion protein in CHO cells which consists of two identical polypeptide chains, in which our target protein, recombinant human erythropoietin (rhEpo), is N-terminally linked with the Fc part of a human IgG(1) molecule. (boku.ac.at)
- An antibody ( Ab ), also known as an immunoglobulin ( Ig ), [1] is a large, Y-shaped protein used by the immune system to identify and neutralize foreign objects such as pathogenic bacteria and viruses . (wikipedia.org)
- These data indicate that destabilization of the glycan-protein interactions, rather than increased galactosylation and sialylation, modifies the Fc conformation(s) relevant for FcγR binding. (ox.ac.uk)
- High plasma levels of the 35 K-Fc protein are maintained for at least 14 days post gene transfer, with the protein still detectable at 5 weeks. (ox.ac.uk)
- Following papain digestion the Fab fragments are separated from undigested IgG and the Fc region with the supplied Protein A Spin Column. (gbiosciences.com)
- The Protein A Resin binds the IgG and Fc molecules and the Fab are rapidly collected due to the spin-format design. (gbiosciences.com)
- This method has promise as an alternative to conventional Protein A/G chromatography for direct capture of immunoglobulins from streams containing relatively high immunoglobulin concentrations such as colostrum, transgenic or hyper-immune milk. (ncsu.edu)
- The Staphylococcal protein- A (encoded by the spa-gene) is an extracellular protein that binds to the fragment crystallizable (Fc) region of Immunoglobulin G (IgG) inhibiting the host immune response by disrupting cell opsonization and phagocytosis [ 7 ]. (walshmedicalmedia.com)
- The results of laboratory studies, including serum protein electrophoresis (with immunoglobulin [Ig] G, IgA, IgM) C3, C4, erythrocyte sedimentation rate, a complete blood count, CD4 cell count, and CD8 cell count were all within normal limits. (cdc.gov)
Molecule2
- This molecule is created as a fusion of insulin with the Fc fragment of immunoglobulin, which is taken up intracellularly and recycled for a one-week period. (vin.com)
- By using these techniques for the characterization of the recombinant human Epo-Fc (rhEpo-Fc) molecule itself and furthermore, for the separate characterization of both subunits, we could clearly show that no significant differences in the core glycan structures compared to rhEpo and human antibody N-glycans were found. (boku.ac.at)
Region3
- Glycans in the Fc region are shown in black. (wikipedia.org)
- In the present study, we profiled serum IgG Fc region N-glycans in BC patients (N = 90) and NC controls (N = 54) using MALDI-MS. An IgG Fc region N-glycan-based multiple logistic regression model was produced which could distinguish BC patients from NC controls (area under the receiver operative characteristic curve = 0.874). (elsevierpure.com)
- These results suggest that an unknown humoral factor or soluble mediator affects IgGs from the earliest stage of breast cancer, and also suggests that IgG Fc region N-glycosylation may play a role in tumor biology. (elsevierpure.com)
Human3
- The ability of HSV-1-infected cells to bind 125I-labelled human and rabbit IgG and IgG fragments was studied to localize the site of interaction to the C gamma 2 or C gamma 3 domains of IgG. (lu.se)
- by generating a chimeric 2H8 Ab with Fc fragments derived from human immunoglobulin. (morulaivf.com)
- Effects of Composition of Oligo(ethylene glycol)-Based Mixed Monolayers on Peptide Grafting and Human Immunoglobulin Detection. (ncsu.edu)
Gamma2
- 125I-labelled IgG and IgG Fc fragments consisting of C gamma 2 and C gamma 3 domains bound strongly to HSV-infected cells and did not bind to uninfected cells. (lu.se)
- In contrast, 125I-labelled F(ab')2, Facb [consisting of F(ab')2 and C gamma 2 domains] and pFc' (consisting of C gamma 3 domains) fragments did not bind to any of these cells. (lu.se)
Immunology1
- In a recent study published in Science Immunology , researchers evaluated immunoglobulin G (IgG) responses to coronavirus disease 2019 (COVID-19) messenger ribonucleic acid (mRNA) vaccinations. (news-medical.net)
Antibody fragments1
- Monovalent antibody fragments (F(ab) fragments) are powerful tools to block background from primary antibody binding and in double staining experiments. (abcam.com)
Bind1
- 11,12,13 The distinctive, FC-free structure of CIMZIA means RF may not bind to the drug, allowing its concentration to remain stable over time. (cybertrontv.com)
Domains2
- two Fab domains and a Fc domain. (gbiosciences.com)
- Contains 2 immunoglobulin-like C2-type domains. (lu.se)
Serum1
- After the blocking step with normal serum, we recommend incubating F(ab) fragments in excess to block endogenous immunoglobulins in IHC. (abcam.com)
ADCC1
- Given that sialylation of Fc glycans decreases ADCC, one explanation for the effect of these mutants on FcγRIIIA binding is their increased sialylation. (ox.ac.uk)
Autoantibodies2
- Immunoglobulin M (IgM) autoantibodies against the Fc fragment of immunoglobulin G (IgG) are called rheumatoid factors (RFs). (medscape.com)
- 7 One reason for this is the high levels of RF autoantibodies binding with the Fc parts of TNFis to form large immune complexes that are then degraded by macrophages, resulting in lower bioavailability of biologic drugs. (cybertrontv.com)
Specificity2
- Within the V regions, hypervariable regions determine the specificity of the immunoglobulin (Ig). (msdmanuals.com)
- When choosing a secondary antibody product, consideration must be given to species and immunoglobulin specificity, conjugate type, fragment and chain specificity, level of cross-reactivity, and host-species source and fragment composition. (rockland.com)
Enzyme papain2
- An antibody digested by the enzyme papain yields two F(ab) fragments of about 50 kDa each and an Fc fragment. (abcam.com)
- A proteolytic fragment of immunoglobulin G (IgG) obtained by limited digestion with the enzyme papain under controlled conditions of temperature, time and pH. (rockland.com)
Efficacy1
- Anti-CTLA-4 therapy requires an Fc domain for efficacy. (rush.edu)
Glycans1
- N-glycans attached to immunoglobulin G-Fab/Fc fragments are features that influence their mechanism of action. (bvsalud.org)
Vitro1
- In vivo and in vitro activity of an immunoglobulin Fc fragment (Fcab) with engineered Her-2/neu binding sites. (boku.ac.at)
Domain2
- Immunoglobulin Fc heterodimers have been engineered through modifications to the CH3 domain interface, with different mutations on each domain such that the engineered Fc fragments, carrying the CH3 variant pair, preferentially form heterodimers rather than homodimers. (nih.gov)
- The effects of four mutations in the second immunoglobulin-like domain of sFcepsilonRIalpha upon the kinetics of binding to IgE and fragments of IgE have been analyzed using surface plasmon resonance. (ox.ac.uk)
Vivo1
- These results demonstrate that B7-mediated signaling plays a critical role in germinal center formation and immunoglobulin class switching in vivo. (nih.gov)
Disulfide1
- Wozniak-Knopp G, Rüker F. A C-terminal interdomain disulfide bond significantly stabilizes the Fc fragment of IgG. (boku.ac.at)
Constructs2
- To confirm the role of tmr in triphenylmethane dye detoxification, we introduced various tmr-harboring fragments of pLM80 in a pLM80-cured derivative of strain H7550, from the same outbreak as H7858, and assessed the resistance of the constructs to the triphenylmethane dyes crystal violet (CV) and malachite green. (ncsu.edu)
- Constructs harboring fragments spanning bcrABC and tmr were CV resistant, and in such constructs tmr transcription was induced by sublethal levels of either BC or CV. (ncsu.edu)
Digestion1
- Immobilized Papain offers the advantage of generating Fab and Fc fragments without the need to remove the papain enzyme after digestion. (gbiosciences.com)
Isolation1
- The Fab Fragmentation kits are designed for the generation and isolation of Fab fragments from IgG molecules. (gbiosciences.com)
Purity1
- Bound immunoglobulins were recovered in elution buffer (0.2 M sodium acetate buffer, pH 4.0) fractions with a purity of >85% in a single step. (ncsu.edu)
Preparations1
- METHODS: nAbs-Aß42 were isolated from AD patients and age-/sex-matched controls (n = 40) and immunoglobulin preparations. (bvsalud.org)
Significantly1
- Peak monocyte recruitment to the aorta occurs within 3 days and this process is CC chemokine dependent, being significantly reduced by hydrodynamic delivery of 35 K-Fc. (ox.ac.uk)
Immune1
- Subcutaneous immunoglobulin is a potential alternative to intravenous immunoglobulin that may be of similar benefit in some immune-mediated neuromuscular disorders. (medlink.com)
Purification1
- These results suggest that the hexamer peptide chromatography could potentially be used for the selective purification of bovine immunoglobulins from dairy streams. (ncsu.edu)
Type1
- Many research groups have adopted different strategies to generate Fc heterodimers, with the goal of high heterodimerization yield, while retaining biophysical and biological properties of the wild-type Fc. (nih.gov)
Site-directed1
- Our results, together with those from site-directed mutagenesis on fragments of IgE presented in the accompanying paper, define the contact surfaces in the IgE:sFcepsilonRIalpha complex. (ox.ac.uk)
Primarily2
- After 5.0 months to 7.0 months of the second mRNA vaccination, anti-SARS-CoV-2 IgG responses primarily comprised the non-inflammatory immunoglobulin G4 subclass and were enhanced by the booster dose or breakthrough infection. (news-medical.net)
- These functions are primarily triggered through interaction with the complement component C1q or with a family of FcγRs expressed, primarily, on the surface of leukocytes. (bmj.com)