The major histocompatibility complex (MHC) gene locus encodes a group of highly polymorphic, cell surface proteins that play a broad role in the immune response to protein antigens. MHC molecules function by binding and presenting small antigenic protein fragments to antigen-specific receptors expressed by T cells (TCR). Class I MHC molecules consist of two separate polypeptide chains. The class I α chain is an MHC encoded, transmembrane polypeptide containing three extracellular domains: α1, α2 and α3. The second chain consists of a non-MHC encoded, 12 kD polypeptide called β2 microglobulin (β2M). Since β2M does not contain a transmembrane domain, it associates with the a chain through non-covalent interaction. This association is important for the stability of the MHC class I structure, its peptide-loading and its ability to present peptide antigen to CD8+ T cells. β2M is relatively invariant within each species. For example, human β2M is reported to have high affinity for human and mouse MHC class I heavy chains. Human β2 Microglobulin recombinant protein was expressed in insect cells. The expressed protein was purified by a combination of ion-exchange and gel-filtration methods.

(RUO)

0.5 mg/ml

recombinant β2 microglobulin

Aqueous buffered solution containing ≤0.09% sodium azide.

Development References(3) 1. Parker KC, DiBrino M, Hull L, Coligan JE. The beta 2-microglobulin dissociation rate is an accurate measure of the stability of MHC class I heterotrimers and depends on which peptide is bound. J Immunol. 1992; 149(6):1896-1904. (Biology). 2. Shields MJ, Moffat LE, Ribaudo RK. Functional comparison of bovine, murine, and human beta2-microglobulin: interactions with murine MHC I molecules. Mol Immunol. 1998; 35(14-15):919-928. (Biology). 3. Silver ML, Parker KC, Wiley DC. Reconstitution by MHC-restricted peptides of HLA-A2 heavy chain with beta 2-microglobulin, in vitro. Nature. 1991; 350(6319):619-622. (Biology: Activation).