The IGKV1-5 Monoclonal Antibody (PACO09898) is a powerful tool for research involving the IGKV1-5 gene, a key player in immune function and antibody production. This antibody, produced through advanced monoclonal technology, specifically targets the IGKV1-5 protein, allowing for precise detection and analysis in a variety of experimental settings. IGKV1-5 is a crucial component of the immune system, playing a vital role in the generation of antibodies that target specific pathogens and foreign substances. By studying the function and expression of IGKV1-5, researchers can gain valuable insights into the mechanisms of immune response and potentially develop novel therapeutic strategies for a wide range of diseases and conditions.
With its high specificity and sensitivity, the IGKV1-5 Monoclonal Antibody (PACO09898) is an essential tool for advancing research in immunology, infectious diseases, and antibody engineering. Whether used in Western blotting, immunofluorescence, or flow cytometry, this antibody provides reliable and accurate results to support your scientific investigations. Unlock the potential of IGKV1-5 research with this cutting-edge antibody reagent.
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).
