| 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. 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. |
| Protein Name | Immunoglobulin Kappa ConstantIg Kappa Chain C RegionIg Kappa Chain C Region AgIg Kappa Chain C Region CumIg Kappa Chain C Region EuIg Kappa Chain C Region OuIg Kappa Chain C Region RoyIg Kappa Chain C Region Ti |
| Cellular Localisation | SecretedCell Membrane |
| Alternative Antibody Names | Anti-Immunoglobulin Kappa Constant antibodyAnti-Ig Kappa Chain C Region antibodyAnti-Ig Kappa Chain C Region Ag antibodyAnti-Ig Kappa Chain C Region Cum antibodyAnti-Ig Kappa Chain C Region Eu antibodyAnti-Ig Kappa Chain C Region Ou antibodyAnti-Ig Kappa Chain C Region Roy antibodyAnti-Ig Kappa Chain C Region Ti antibodyAnti-IGKC antibody |
Information sourced from Uniprot.org
