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Recombinant Human Migration Inhibitor Factor produced in E.coli is a single non-glycosylated polypeptide chain containing 123 amino acids and having a molecular mass of approximately 13.5 kDa.
Specificity
Fully biologically active measured by its ability to bind rhCD74 in a functional ELISA.
Endotoxin
Less than 1EU/μg of rHuMIF as determined by LAL method.
Purity
>95% by SDS-PAGE and HPLC analyses.
Storage
This lyophilized preparation is stable for several weeks at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
PDB rendering based on 1ca7.Available structures: 1ca7, 1cgq, 1gcz, 1gd0, 1gif,1ljt, 1mif, 1p1g, 2ooh, 2oow, 2ooz
BACKGROUND
Antigen Description
Human 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 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, 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.
Function
cytokine activity; isomerase activity; phenylpyruvate tautomerase activity; protein binding.