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Overview
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Background
HLA-G Antibody (4H84) is an IgG1 κ mouse monoclonal HLA-G antibody (also designated HLA major histocompatibility complex, class I, G antibody, human leukocyte antigen (HLA) G antibody, 45 kDa transmembrane class I human leukocyte antigen G antibody, chromosome 6p22 gene complex class 1G antibody, placenta trophoblast marker antibody, or fetal derived placental cell marker antibody) that detects the HLA-G protein of mouse, rat and human origin by WB, IP, IF and IHC(P). HLA-G Antibody (4H84) is available as both the non-conjugated anti-HLA-G antibody form, as well as multiple conjugated forms of anti-HLA-G antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor conjugates. Major histocompatibility complex (MHC), human leukocyte antigen (HLA) molecules are cell-surface receptors that bind foreign peptides and present them to T lymphocytes. MHC class I molecules consist of two polypeptide chains, an α or heavy chain, and a non-covalently associated protein, β-2-microglobulin. Cytotoxic T lymphocytes bind antigenic peptides presented by MHC class I molecules. Antigens that bind to MHC class I molecules are typically 8-10 residues in length and are stabilized in a peptide binding groove. MHC class II molecules are encoded by polymorphic MHC genes and consist of a non-covalent complex of an a and b chain. Helper T lymphocytes bind antigenic peptides presented by MHC class II molecules. MHC class II molecules bind 13-18 amino acid antigenic peptides. Accumulating in endosomal/lysosomal compartments and on the surface of B cells, HLA-DM and -DO molecules regulate binding of exogenous peptides to class II molecules (HLA-DR) by sustaining a conformation that favors peptide exchange. The differential structural properties of MHC class I and class II molecules account for their respective roles in activating different populations of T lymphocytes.
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