IgA Mouse Monoclonal Antibody [3-B6]

Function

Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens . The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen . Ig alpha is the major immunoglobulin class in body secretions.

Background References

1. Kerr M.A.The structure and function of human IgA.Biochem. J. 271:285-296(1990) .

Post-translational Modification

3-Hydroxykynurenine, an oxidized tryptophan metabolite that is common in biological fluids, reacts with alpha-1-microglobulin to form heterogeneous polycyclic chromophores including hydroxanthommatin. The chromophore reacts with accessible cysteines forming non-reducible thioether cross-links with Ig alpha-1 chain C region Cys-352.; N- and O-glycosylated. N-glycan at Asn-144: Hex5HexNAc4.

Subcellular Location

Cell membrane, Immunoglobulin, Membrane, Secreted

UNIPROT

SwissProt: P01876 Human

SwissProt: P01877 Human

Synonyms