Recombinant Human Migration Inhibitor Factor
|Recombinant Human Migration Inhibitor Factor
- Product Overview
- 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.
- Fully biologically active measured by its ability to bind rhCD74 in a functional ELISA.
- Less than 1EU/μg of rHuMIF as determined by LAL method.
- >95% by SDS-PAGE and HPLC analyses.
- 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.
- 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
- 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.
- cytokine activity; isomerase activity; phenylpyruvate tautomerase activity; protein binding.
- Gene ID
- GIF; GLIF; MMIF; macrophage migration inhibitory factor (glycosylation-inhibiting factor); MIF_HUMAN; EC22.214.171.124; Phenylpyruvate tautomerase.
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