• Product NameRecombinant Human Macrophage Migration Inhibitory Factor, His
• Host SpeciesEscherichia coli.
• Purification> 95 % by SDS-PAGE and HPLC analyses.
• Biological ActivityFully biologically active when compared to standard. The specific activity is determined by binding rhCD74 in a functional ELISA.
• EndotoxinLess than 1 EU/ug of rHuMIF, His as determined by LAL method.
• Alternative Names    GLF, L-dopachrome Isomerase, Phenylpyruvate Tautomerase
• Calculated MW Approximately 13.5 kDa, a single non-glycosylated polypeptide chain containing 117 amino acids, with 6 x His at the C-terminus.
• Target Sequence MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFALEHHH HHH
• Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.
• Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 ˚C as supplied.- 1 month, 2 to 8 ˚C under sterile conditions after reconstitution.- 3 months, -20 to -70 ˚C under sterile conditions after reconstitution.

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 (a.a.) 49 - 65. 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% aa identical to mouse, bovine, porcine and rat MIF, respectively.

• Flow Cytometry (FCM) General Protocol
• Immunofluorescence(IC)
• Immunohistochemistry(Polymer)
• Western Blotting