The IGLV1-51 Antibody (PAC018709) is a valuable tool for researchers studying immunology and cancer research. This monoclonal antibody specifically targets the IGLV1-51 protein, which is implicated in immune responses and antibody production. Raised in rabbits, this antibody is highly reactive with human samples and is validated for use in various applications, including Western blotting.IGLV1-51 is a key player in the immune system, particularly in the production of antibodies that target specific antigens. By targeting this protein, researchers can gain valuable insights into how the immune system responds to different stimuli and how it can be manipulated for therapeutic purposes.
This antibody is essential for studies focusing on antibody diversity, B-cell development, and immune response mechanisms.Overall, the IGLV1-51 Antibody (PAC018709) is a reliable tool for investigating the role of IGLV1-51 in immune regulation and antibody production, making it a valuable asset for any research laboratory studying immunology and cancer.
The image on the left is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using PACO18709(Lambda Light chain Antibody) at dilution 1/20, on the right is treated with synthetic peptide. (Original magnification: x200).
Gel: 12%SDS-PAGE, Lysate: 40 μg, Lane: Human plasma solution, Primary antibody: PACO18709(Lambda Light chain Antibody) at dilution 1/200 dilution, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 10 seconds.
The image on the left is immunohistochemistry of paraffin-embedded Human esophagus cancer tissue using PACO18709(Lambda Light chain Antibody) at dilution 1/20, on the right is treated with synthetic peptide. (Original magnification: x200).
Background:
Antibody producing cells of the immune system require multiple rearrangements of immunoglobulin (antibody, Ig) genes. Immunoglobulins are four-chain, Y-shaped, monomeric structures of two identical heavy chains and two identical light chains held together through interchain disulfide bonds. Immunoglobulins in vertebrates help to remove non-self molecules or cells (antigens) by recognizing and binding to the antigen and carrying out effector functions that activate the immune system. Variable genetic combinations of the five heavy chain classes (M, D, G, E and A) and the two light chain isotypes, κ and Lambda, confer the role of an antibody. The variable region genes encoding immunoglobulin κ and Lambda chains are assembled from three DNA segments, the V, C and J genes. κ and Lambda consist of a variable region and a constant region and can easily be differentiated by the antigenic properties of the constant region. The ratio of κ to Lambda is 70:30 , the vast majority of which is bound to heavy-chain in immunoglobulin.
Synonyms:
Ig lambda chain V-I region NEW
UniProt Protein Function:
IGLV1-51: V segment of the variable region of immunoglobulins light chain that participates to the antigen recognition. Immunoglobulins (Igs), also known as antibodies, are membrane- bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound Igs serve as receptors which, upon binding of a specific antigen (Ag), trigger the clonal expansion and differentiation of B lymphocytes into Ig-secreting plasma cells. Secreted Igs 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 region of one heavy chain, together with that of its associated light chain. Thus, each Ig has two antigen binding sites with remarkable affinity for a particular antigen. The variable regions are assembled by a process called V(D)J recombination and can then be subjected to somatic hypermutation after exposure to antigen to allow affinity maturation for a particular Ag (PubMed:20176268, PubMed:17576170). {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Immunoglobulins are composed of two identical heavy chains and two identical light chains, linked by disulfide bonds. {ECO:0000303|PubMed:20176268}
