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Immunoglobulin Fc Fragments
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D007141 |
[Crystallizable fragments composed of the carboxy-terminal halves of both IMMUNOGLOBULIN HEAVY CHAINS linked to each other by disulfide bonds. Fc fragments contain the carboxy-terminal parts of the heavy chain constant regions that are responsible for the effector functions of an immunoglobulin (COMPLEMENT fixation, binding to the cell membrane via FC RECEPTORS, and placental transport). This fragment can be obtained by digestion of immunoglobulins with the proteolytic enzyme PAPAIN.
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Immunoglobulin Fragments
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D007128 |
[Partial immunoglobulin molecules resulting from selective cleavage by proteolytic enzymes or generated through PROTEIN ENGINEERING techniques.
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Immunoglobulin G
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D007074 |
[The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B.
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Immunoglobulin G4-Related Disease
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D000077733 |
[A spectrum of systemic autoimmune diseases in which IMMUNOGLOBULIN G4 plays a pathophysiologic role. It can affect multiple organs in highly variable presentations, characterized by inflammatory lesions composed of IgG4-positive PLASMA CELLS, further infiltrated by T helper cells (T-LYMPHOCYTES, HELPER-INDUCER) when linked to progressive FIBROSIS and eventual organ damage.
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Immunoglobulin Gm Allotypes
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D007129 |
[Allelic variants of the gamma-immunoglobulin heavy chain (IMMUNOGLOBULIN GAMMA-CHAINS) encoded by ALLELES of IMMUNOGLOBULIN HEAVY CHAIN GENES.
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Immunoglobulin Heavy Chains
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D007143 |
[The largest of polypeptide chains comprising immunoglobulins. They contain 450 to 600 amino acid residues per chain, and have molecular weights of 51-72 kDa.
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Immunoglobulin Idiotypes
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D007130 |
[Unique genetically-controlled determinants present on ANTIBODIES whose specificity is limited to a single group of proteins (e.g., another antibody molecule or an individual myeloma protein). The idiotype appears to represent the antigenicity of the antigen-binding site of the antibody and to be genetically codetermined with it. The idiotypic determinants have been precisely located to the IMMUNOGLOBULIN VARIABLE REGION of both immunoglobin polypeptide chains.
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Immunoglobulin Isotypes
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D007132 |
[The classes of immunoglobulins found in any species of animal. In man there are nine classes that migrate in five different groups in electrophoresis; they each consist of two light and two heavy protein chains, and each group has distinguishing structural and functional properties.
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Immunoglobulin J Recombination Signal Sequence-Binding Protein
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D051819 |
[A ubiquitously expressed sequence-specific transcriptional repressor that is normally the target of signaling by NOTCH PROTEINS.
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Immunoglobulin J-Chains
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D007144 |
[A 15 kDa "joining" peptide that forms one of the linkages between monomers of IMMUNOGLOBULIN A or IMMUNOGLOBULIN M in the formation of polymeric immunoglobulins. There is one J chain per one IgA dimer or one IgM pentamer. It is also involved in binding the polymeric immunoglobulins to POLYMERIC IMMUNOGLOBULIN RECEPTOR which is necessary for their transcytosis to the lumen. It is distinguished from the IMMUNOGLOBULIN JOINING REGION which is part of the IMMUNOGLOBULIN VARIABLE REGION of the immunoglobulin light and heavy chains.
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Immunoglobulin Joining Region
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D007133 |
[A segment of the immunoglobulin heavy chains, encoded by the IMMUNOGLOBULIN HEAVY CHAIN GENES in the J segment where, during the maturation of B-LYMPHOCYTES; the gene segment for the variable region upstream is joined to a constant region gene segment downstream. The exact position of joining of the two gene segments is variable and contributes to ANTIBODY DIVERSITY. It is distinguished from the IMMUNOGLOBULIN J CHAINS; a separate polypeptide that serves as a linkage piece in polymeric IGA or IGM.
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Immunoglobulin Km Allotypes
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D007131 |
[Allelic variants of the kappa light chains (IMMUNOGLOBULIN KAPPA-CHAINS) encoded by ALLELES of IMMUNOGLOBULIN LIGHT CHAIN GENES.
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Immunoglobulin Light Chains
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D007147 |
[Polypeptide chains, consisting of 211 to 217 amino acid residues and having a molecular weight of approximately 22 kDa. There are two major types of light chains, kappa and lambda. Two Ig light chains and two Ig heavy chains (IMMUNOGLOBULIN HEAVY CHAINS) make one immunoglobulin molecule.
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Immunoglobulin Light Chains, Surrogate
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D054444 |
[An immunolglobulin light chain-like protein composed of an IMMUNOGLOBULIN VARIABLE REGION-like peptide (such as light chain like lambda5 peptide) and an IMMUNOGLOBULIN CONSTANT REGION-like peptide (such as Vpreb1 peptide). Surrogate light chains associate with MU IMMUNOGLOBULIN HEAVY CHAINS in place of a conventional immunoglobulin light chains to form pre-B cell receptors.
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Immunoglobulin Light-chain Amyloidosis
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D000075363 |
[A nonproliferative disorder of the PLASMA CELL characterized by excessive production and misfolding of IMMUNOGLOBULIN LIGHT CHAINS that form insoluble amyloid fibrils (see AMYLOID DEPOSITS) in various tissues. Clinical features include LIVER FAILURE; MULTIPLE MYELOMA; NEPHROTIC SYNDROME; RESTRICTIVE CARDIOMYOPATHY, and neuropathies.
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Immunoglobulin M
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D007075 |
[A class of immunoglobulin bearing mu chains (IMMUNOGLOBULIN MU-CHAINS). IgM can fix COMPLEMENT. The name comes from its high molecular weight and originally being called a macroglobulin.
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Immunoglobulin Subunits
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D050440 |
[The PROTEIN SUBUNITS of the multimeric IMMUNOGLOBULIN proteins, such as IGA; IGD; IGE; IGG; and IGM. Included are the heavy and light chains which contain the specific ANTIGEN binding domains, as well as the accessory proteins that are part of the the secreted forms of IGM and IGA; (SECRETORY IGA).
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Immunoglobulin Switch Region
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D007134 |
[A site located in the INTRONS at the 5' end of each constant region segment of a immunoglobulin heavy-chain gene where recombination (or rearrangement) occur during IMMUNOGLOBULIN CLASS SWITCHING. Ig switch regions are found on genes encoding all five classes (IMMUNOGLOBULIN ISOTYPES) of IMMUNOGLOBULIN HEAVY CHAINS.
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Immunoglobulin Variable Region
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D007135 |
[The paired immunoglobulin fragments composed of the variable domains of the heavy and light chains.
, That region of the immunoglobulin molecule that varies in its amino acid sequence and composition, and comprises the binding site for a specific antigen. It is located at the N-terminus of the Fab fragment of the immunoglobulin. It includes hypervariable regions (COMPLEMENTARITY DETERMINING REGIONS) and framework regions.
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Immunoglobulin alpha-Chains
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D007137 |
[The class of heavy chains found in IMMUNOGLOBULIN A. They have a molecular weight of approximately 58 kDa and contain about 470 amino acid residues arranged in four domains and an oligosaccharide component bound covalently to their Fc fragment constant region.
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