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HLA-G pAb

HLA-G pAb

Cat no: BS60401


Supplier: Bioworld Technology, Inc.
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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, b-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.
Catalogue number: BS60401
Reactivities: Human, Mouse, Rat
Hosts: Rabbit
Applications: Western Blot
Size: 100ug/100ul
Swiss prot: P17693
Dilutions: WB: 1:500~1:1000
Form: liquid
Storage buffer: 1 mg/ml in Phosphate buffered saline (PBS) with 0.05% sodium azide, approx. pH 7.2.
Concentration: 1ug/ul
Antigen: A synthetic peptide corresponding to residues in Human HLA-G.
Species: HLA-G pAb detects endogenous levels of HLA-G protein.
Molecular weight: ~ 42 kDa
Purity: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Storage temp: Store at 4 degrees C short term. Aliquot and store at -20 degrees C long term. Avoid freeze-thaw cycles.
Alternative names: HLA class I histocompatibility antigen, alpha chain G; HLA G antigen; MHC class I antigen G; HLA-G; HLA-6.0; HLAG
Additional info: For research use only, not for use in diagnostic procedure.

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