Recombinant Cynomolgus / Rhesus macaque beta 2-Microglobulin / B2M Protein, 100 µg

Background
β2 microglobulin is also known as Beta-2-microglobulin (B2M), is a component of MHC class I molecules which belongs to the beta-2-microglobulin family. B2M is present on all nucleated cells (excludes red blood cells). B2M associates not only with the alpha chain of MHC class I molecules, but also with class I-like molecules such as CD1 and Qa. An additional function of B2M is association with the HFE protein, together regulating the expression of hepcidin in the liver which targets the iron transporter ferroportin on the cytoplasmic membrane of enterocytes and macrophages for degradation resulting in decreased iron uptake from food and iron release from recycled red blood cells respectively. Loss of this function causes iron excess and hemochromatosis. Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP).

Source
Cynomolgus / Rhesus macaque B2M, His Tag (B2M-C5226) is expressed from human 293 cells (HEK293). It contains AA Ile 21 - Met 119 (Accession # Q8SPW0). In the region Ile 21 - Met 119, the AA sequence of Cynomolgus and Rhesus macaque beta 2-Microglobulin are homologus.
Predicted N-terminus: Ile 21

Molecular Characterization
Cynomolgus B2M is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 12.6 kDa. The predicted N-terminus is Ile 21. DTT-reduced Protein migrates as 14 kDa in SDS-PAGE .

Endotoxin
Less than 1.0 EU per μg of the Cynomolgus B2M by the LAL method.

Purity
>95% as determined by SDS-PAGE.

Formulation
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally Mannitol or Trehalose are added as protectants before lyophilization.

Reconstitution
See Certificate of Analysis for reconstitution instructions and specific concentrations.

Storage
Avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C); After reconstitution under sterile conditions for 3 months (-70°C).

References

(1) Güssow D., et al., 1987, J. Immunol. 139 (9): 3132–8.
(2) Gorevic P.D., et al., 1986, Proc. Natl. Acad. Sci. U.S.A. 83:7908-7912.
(3) Argiles A., et al., 1992, Nephrol. Dial. Transplant. 7:1106-1110.
(4) Momoi T., et al., 1995, Clin. Chim. Acta 236:135-144.
(5) Collins E.J., et al., 1995, Proc. Natl. Acad. Sci. U.S.A. 92:1218-1221.