| Function | V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. 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 Lambda Variable 1-51Ig Lambda Chain V-I Region Bl2Ig Lambda Chain V-I Region EpsIg Lambda Chain V-I Region NewIg Lambda Chain V-I Region Nig-64 |
| Cellular Localisation | SecretedCell Membrane |
| Alternative Antibody Names | Anti-Immunoglobulin Lambda Variable 1-51 antibodyAnti-Ig Lambda Chain V-I Region Bl2 antibodyAnti-Ig Lambda Chain V-I Region Eps antibodyAnti-Ig Lambda Chain V-I Region New antibodyAnti-Ig Lambda Chain V-I Region Nig-64 antibodyAnti-IGLV1-51 antibody |
Information sourced from Uniprot.org
