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| Aliases | IGHG4 , immunoglobulin heavy constant gamma 4 (G4m marker) | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 147130; GeneCards: IGHG4; OMA:IGHG4 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Ig gamma-4 chain C region is a protein that in humans is encoded by the IGHG4 gene. [3]
| IGHG4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | IGHG4 , immunoglobulin heavy constant gamma 4 (G4m marker) | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 147130; GeneCards: IGHG4; OMA:IGHG4 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Ig gamma-4 chain C region is a protein that in humans is encoded by the IGHG4 gene. [3]
The complement component 1q is a protein complex involved in the complement system, which is part of the innate immune system. C1q together with C1r and C1s form the C1 complex.
The word allotype comes from two Greek roots, allo meaning 'other or differing from the norm' and typos meaning 'mark'. In immunology, allotype is an immunoglobulin variation that can be found among antibody classes and is manifested by heterogeneity of immunoglobulins present in a single vertebrate species. The structure of immunoglobulin polypeptide chain is dictated and controlled by number of genes encoded in the germ line. However, these genes, as it was discovered by serologic and chemical methods, could be highly polymorphic. This polymorphism is subsequently projected to the overall amino acid structure of antibody chains. Polymorphic epitopes can be present on immunoglobulin constant regions on both heavy and light chains, differing between individuals or ethnic groups and in some cases may pose as immunogenic determinants. Exposure of individuals to a non-self allotype might elicit an anti- allotype response and became cause of problems for example in a patient after transfusion of blood or in a pregnant woman. However, it is important to mention that not all variations in immunoglobulin amino acid sequence pose as a determinant responsible for immune response. Some of these allotypic determinants may be present at places that are not well exposed and therefore can be hardly serologically discriminated. In other cases, variation in one isotype can be compensated by the presence of this determinant on another antibody isotype in one individual. This means that divergent allotype of heavy chain of IgG antibody may be balanced by presence of this allotype on heavy chain of for example IgA antibody and therefore is called isoallotypic variant. Especially large number of polymorphisms were discovered in IgG antibody subclasses. Which were practically used in forensic medicine and in paternity testing, before replaced by modern day DNA fingerprinting.
In immunology, antibodies are classified into several types called isotypes or classes. The variable (V) regions near the tip of the antibody can differ from molecule to molecule in countless ways, allowing it to specifically target an antigen . In contrast, the constant (C) regions only occur in a few variants, which define the antibody's class. Antibodies of different classes activate distinct effector mechanisms in response to an antigen . They appear at different stages of an immune response, differ in structural features, and in their location around the body.
Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide, also known as FCER1A, is a protein which in humans is encoded by the FCER1A gene.
Immunoglobulin lambda-like polypeptide 1 is a protein that in humans is encoded by the IGLL1 gene. IGLL1 has also recently been designated CD179B.
Ig mu chain C region is a protein that in humans is encoded by the IGHM gene.
Ig gamma-1 chain C region is a protein that in humans is encoded by the IGHG1 gene.
Immunoglobulin heavy constant alpha 1 is a immunoglobulin gene with symbol IGHA1. It encodes a constant (C) segment of Immunoglobulin A heavy chain. Immunoglobulin A is an antibody that plays a critical role in immune function in the mucous membranes. IgA shows the same typical structure of other antibody classes, with two heavy chains and two light chains, and four distinct domains: one variable region, and three variable regions. As a major class of immunoglobulin in body secretions, IgA plays a role in defending against infection, as well as preventing the access of foreign antigens to the immunologic system.
Immunoglobulin heavy locus, also known as IGH, is a region on human chromosome 14 that contains a gene for the heavy chains of human antibodies.
Ig delta chain C region is a protein that in humans is encoded by the IGHD gene.
Ig epsilon chain C region is a protein that in humans is encoded by the IGHE gene.
Ig gamma-2 chain C region is a protein that in humans is encoded by the IGHG2 gene.
Ig alpha-2 chain C region is a protein that in humans is encoded by the IGHA2 gene.
Immunoglobulin lambda locus, also known as IGL@, is a region on the q arm of human chromosome 22, region 11.22 (22q11.22) that contains genes for the lambda light chains of antibodies.
Protocadherin gamma-C3 is a protein that in humans is encoded by the PCDHGC3 gene.
Ig gamma-3 chain C region is a protein that in humans is encoded by the IGHG3 gene.
High affinity immunoglobulin gamma Fc receptor I is a protein that in humans is encoded by the FCGR1A gene.
Fc fragment of IgA receptor (FCAR) is a human gene that codes for the transmembrane receptor FcαRI, also known as CD89. FcαRI binds the heavy-chain constant region of Immunoglobulin A (IgA) antibodies. FcαRI is present on the cell surface of myeloid lineage cells, including neutrophils, monocytes, macrophages, and eosinophils, though it is notably absent from intestinal macrophages and does not appear on mast cells. FcαRI plays a role in both pro- and anti-inflammatory responses depending on the state of IgA bound. Inside-out signaling primes FcαRI in order for it to bind its ligand, while outside-in signaling caused by ligand binding depends on FcαRI association with the Fc receptor gamma chain.
High affinity immunoglobulin epsilon receptor subunit beta is a protein that in humans is encoded by the MS4A2 gene.
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulphide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha, delta, epsilon, gamma and mu, all consisting of a variable domain (VH) and three or four constant domains. Ig molecules are highly modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set, C1-set, C2-set and I-set. Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure, with the types differing in the number of strands in the beta-sheets as well as in their sequence patterns.
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