Purified Anti-Human HLA-G Antibody[MEM-G/11]

HLA-G Antibody (4H84) is an IgG1 kappa 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(R) 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 alpha or heavy chain, and a non-covalently associated protein, beta-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. Protein function: [Isoform 1]: Non-classical major histocompatibility class Ib molecule involved in immune regulatory processes at the maternal-fetal interface (PubMed:19304799, PubMed:23184984, PubMed:29262349). In complex with B2M/beta-2 microglobulin binds a limited repertoire of nonamer self-peptides derived from intracellular proteins including histones and ribosomal proteins (PubMed:7584149, PubMed:8805247). Peptide-bound HLA-G-B2M complex acts as a ligand for inhibitory/activating KIR2DL4, LILRB1 and LILRB2 receptors on uterine immune cells to promote fetal development while maintaining maternal- fetal tolerance (PubMed:16366734, PubMed:19304799, PubMed:20448110, PubMed:23184984, PubMed:27859042, PubMed:29262349). Upon interaction with KIR2DL4 and LILRB1 receptors on decidual NK cells, it triggers NK cell senescence-associated secretory phenotype as a molecular switch to promote vascular remodeling and fetal growth in early pregnancy (PubMed:16366734, PubMed:19304799, PubMed:23184984, PubMed:29262349). Through interaction with KIR2DL4 receptor on decidual macrophages induces pro-inflammatory cytokine production mainly associated with tissue remodeling (PubMed:19304799). Through interaction with LILRB2 receptor triggers differentiation of type 1 regulatory T cells and myeloid-derived suppressor cells, both of which actively maintain maternal-fetal tolerance (PubMed:20448110, PubMed:27859042). May play a role in balancing tolerance and antiviral-immunity at maternal-fetal interface by keeping in check the effector functions of NK, CD8+ T cells and B cells (PubMed:10190900, PubMed:11290782, PubMed:24453251). Reprograms B cells toward an immune suppressive phenotype via LILRB1 (PubMed:24453251). May induce immune activation/suppression via intercellular membrane transfer (trogocytosis), likely enabling interaction with KIR2DL4, which resides mostly in endosomes (PubMed:20179272, PubMed:26460007). Through interaction with the inhibitory receptor CD160 on endothelial cells may control angiogenesis in immune privileged sites (PubMed:16809620). [The UniProt Consortium]