B2M Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (21-119 a.a.) and having a molecular mass of 14 kDa. The B2M is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
B2M is a single-chain polypeptide consisting of 119 amino acids. It is non-covalently associated with the alpha chains of MHC class I molecules. The primary function of B2M is to stabilize the MHC class I molecules and facilitate their transport to the cell surface. Once on the cell surface, these molecules present endogenous peptides to cytotoxic T lymphocytes, which are critical for immune surveillance and the destruction of infected or malignant cells .
Recombinant human B2M is produced using various expression systems, including E. coli and HEK293 cells. The recombinant protein is often tagged with a polyhistidine (His) tag at the N-terminus or C-terminus to facilitate purification and detection. The His tag allows for easy purification using nickel affinity chromatography, which is a common method for isolating His-tagged proteins .
Recombinant human B2M is used in various research applications, including:
The production of recombinant human B2M involves cloning the B2M gene into an expression vector, which is then introduced into a host cell line such as E. coli or HEK293 cells. The host cells express the recombinant protein, which is subsequently purified using affinity chromatography. The His tag facilitates the purification process by binding to nickel ions on the chromatography resin, allowing for the selective isolation of the His-tagged protein .