- Tel: 858.663.9055
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- Tel: 858.663.9055
- Email: info@nsjbio.com
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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 a or heavy chain, and a non-covalently associated protein, beta2-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 noncovalent 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.
Optimal dilution of the HLA-G antibody should be determined by the researcher.
A recombinant partial protein sequence (within amino acids 1-200) from the human protein was used as the immunogen for the HLA-G antibody.
Aliquot the HLA-G antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
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