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Immunoglobulin kappa constant

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:22158414, PubMed:20176268). 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).

Involvement in disease

Immunoglobulin kappa light chain deficiency

IGKCD

A disease characterized by the complete absence of immunoglobulin kappa chains.

None

The disease is caused by variants affecting the gene represented in this entry.

Cellular localization

  • Secreted
  • Cell membrane

Alternative names

  • Immunoglobulin kappa constant
  • Ig kappa chain C region
  • Ig kappa chain C region AG
  • Ig kappa chain C region CUM
  • Ig kappa chain C region EU
  • Ig kappa chain C region OU
  • Ig kappa chain C region ROY
  • Ig kappa chain C region TI
  • IGKC

Target type

Antibodies

Molecular weight

11765Da