IGLC2 Mouse Monoclonal Antibody [E12-B9]

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 .

Background References

1. Phipps JE et al. Inhibition of pathologic immunoglobulin-free light chain production by small interfering RNA molecules. Exp Hematol 38(11):1006-13 (2010).

2. van der Burg M et al. Unraveling of the polymorphic C lambda 2-C lambda 3 amplification and the Ke+Oz- polymorphism in the human Ig lambda locus. J Immunol 169(1):271-6 (2010).

Subcellular Location

Secreted, Cell membrane.

UNIPROT

SwissProt: P0DOY2 Human

Synonyms

Ig lambda chain C regions antibody

IGLC antibody

immunoglobulin lambda constant region 2 (Kern- Oz- marker) antibody

MGC20392 antibody

MGC45681 antibody

partial Ke Oz polypeptide antibody