| 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. |
| Protein Name | Immunoglobulin Heavy Constant Alpha 1Ig Alpha-1 Chain C RegionIg Alpha-1 Chain C Region BurIg Alpha-1 Chain C Region Tro |
| Cellular Localisation | Isoform 1: SecretedIsoform 2: Cell MembraneSingle-Pass Type I Membrane Protein |
| Alternative Protein Names | Immunoglobulin Heavy Constant Alpha 1 proteinIg Alpha-1 Chain C Region proteinIg Alpha-1 Chain C Region Bur proteinIg Alpha-1 Chain C Region Tro proteinIGHA1 protein |
Information sourced from Uniprot.org
