Recombinant Human MIF protein (His Tag)

Background

Migration Inhibitory Factor (MIF) is a secreted protein without a cleavable signal sequence and is secreted via a specialized, non-classical pathway. It is secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens. MIF consists of two α-helices and six β-strands, four of which form a β-sheet. The two remaining β-strands 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(a.a.) have also been suggested to contain thiol-protein oxidoreductase activity. MIF has proinflammatory cytokine activity centered around 49 - 65(a.a.). On fibroblasts, MIF induces, IL-1, IL-8 and MMP expression; on macrophages, MIF stimulates NO production and TNF-α release folllowing IFN-γ 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 % a.a. identical to mouse, bovine, porcine and rat MIF, respectively.

Expression system

Escherichia coli.

Purity

> 95 % by SDS-PAGE and HPLC analyses.

Molecular weight

Approximately 13.5 kDa, a single non-glycosylated polypeptide chain containing 117 amino acids, with 6 × His at the C-terminus.

Endotoxin

Less than 1 EU/μg of rHuMIF, His as determined by LAL method.

Form

Sterile Filtered White lyophilized (freeze-dried) powder. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.

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