MIF Anti-Human 100 µg

MIF (or macrophage migration inhibitory factor) was the first lymphokine/cytokine to be recognized in the pregenomics era. Regardless, it is one of the least understood of all inflammatory mediators. Human MIF is a 12.5 kDa, 115 amino acid (aa) nonglycosylated polypeptide that is synthesized without a signal sequence. Secretion occurs nonclassically via an ABCA1 transporter. The initiating Met is removed, leaving Pro as the first amino acid. The molecule consists of two αhelices and six βstrands, four of which form a βsheet. The two remaining βstrands interact with other MIF molecules, creating a trimer. Structure-function studies suggest MIF is bifunctional with segregated topology. The N-and C-termini mediate enzyme activity (in theory). Phenylpyruvate tautomerase activity (enol to keto) has been demonstrated and is dependent upon Pro at position #1. Amino acids 50-65 have also been suggested to contain thiol protein oxidoreductase activity. MIF has proinflammatory cytokine activity centered around aa’s 49-65. On fibroblasts, MIF induces, IL1, IL8, and MMP expression; on macrophages, MIF stimulates NO production and TNF-α release following IFNγ activation. MIF apparently acts through CD74 and CD44, likely in some form of trimeric interaction. Human MIF is active on mouse cells. Human MIF is 90%, 94%, 95%, and 90% aa identical to mouse, bovine, porcine, and rat MIF, respectively.