The IGLV1-51 Monoclonal Antibody (PAC018710) is a powerful tool for researchers studying immunoglobulin genes and antibody production. This antibody, generated using hybridoma technology, specifically targets the IGLV1-51 protein and is optimized for use in applications such as ELISA and flow cytometry. With high specificity and sensitivity for human samples, this antibody enables precise detection and quantification of IGLV1-51, facilitating insights into antibody diversity and immune responses.IGLV1-51 is a key component of immunoglobulins, playing a crucial role in antibody diversity and antigen recognition.
By targeting this specific protein, researchers can gain a deeper understanding of the immune system's ability to respond to pathogens and foreign substances. The IGLV1-51 Monoclonal Antibody is an essential tool for investigating B cell development, antibody production, and immune system function in both health and disease contexts. Its versatility and reliability make it a valuable asset for studies in immunology, infectious diseases, and antibody engineering.
The image on the left is immunohistochemistry of paraffin-embedded Human esophagus cancer tissue using PACO18710(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: PACO18710(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 brain tissue using PACO18710(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}
