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Immunoglobulin lambda constant 1

Function

Constant region of immunoglobulin light 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 (PubMed:20176268, PubMed:22158414). 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 (PubMed:17576170, PubMed:20176268).

Cellular localization

Alternative names

Immunoglobulin lambda constant 1, Ig lambda chain C region MGC, Ig lambda-1 chain C region, IGLC1

swissprot:P0CG04 entrezGene:3546 entrezGene:8217 entrezGene:3538 entrezGene:3537 entrezGene:3535 swissprot:P01842 swissprot:P01701 omim:147220