MIF
Origine: Humain
Hôte: HEK-293 Cells
Recombinant
The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
Lyophilized recombinant human Macrophage Migration Inhibitory Factor (rhMIF) remains stable up to 6 months at -80 °C from date of receipt. Upon reconstitution, rhMIF remains stable up to 2 weeks at 4 °C or up to 3 months at -20 °C.
Macrophage Migration Inhibitory Factor (MIF) is a pleiotropic cytokine, existing as a homotrimer in vivo. MIF was originally identified as a T cell derived factor responsible for the inhibition of macrophage migration. However, recently MIF has received much more attention because of its possible roles in angiogenesis and cancer development. MIF is over-expressed in various cancers, including pancreatic, breast, colon, brain, prostate, skin, and lung. The intratumoral expression of MIF is strongly correlated with angiogenic growth factor expression, such as the expression of Interleukin 8 (IL-8) and Vascular Endothelial Growth Factor (VEGF), and with risk of recurrence after resection. Recombinant human Macrophage Migration Inhibitory Factor (rhMIF) produced in E. coli is a single non-glycosylated polypeptide chain containing 115 amino acids. rhMIF has a molecular mass of 12.5 kDa analyzed by reducing SDS-PAGE. Synonyms: Macrophage Migration, Inhibitory Factor, GLIF, MMIF, GIF, Glycosylation-inhibiting factor