Anti-Kappa Light Chains, clone L1C1 (Monoclonal) [Mouse]

MON 3295 detects surface immunoglobulin on normal and neoplastic B-cells. In paraffin-embedded tissue, anti-kappa exhibits strong staining of kappa-positive plasma cells and cells that have absorbed exogenous immunoglobuli ns. When dealing with B-cell neoplasms, the determination of light chain ratios remains the centerpiece. Most B-cell lymphomas express either kappa or lambda light chains, whereas reactive proliferations display a mixture of kappa and lambda positive cells . If only a single light chain type is detected, a lymphoproliferative disorder exists. Monoclonality is determined by a kappa-lambda ratio of greater than or equal to 3:1 or a lambda-kappa ratio greater than 2:1 . Protein function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). 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:20176268, PubMed:17576170). [The UniProt Consortium]