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Migration Inhibitor Factor (MIF), Human


*This product has been discontinued! *


Synonyms Migration Inhibitor Factor (MIF), Human;
Description Human MIF consists of two ª-helices and six ß-strands, four of which form a ß-sheet. The two remaining ß-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-ª 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.
Amino Acid Sequence
MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV
HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL
CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFALEHHH
HHH
Source Escherichia coli
Biological Activity Fully biologically active measured by its ability to bind rhCD74 in a functional ELISA.

Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.
Molecular Weight Approximately 12.5 kDa, a single non-glycosylated polypeptide chain containing 115 amino acids.
Formulation Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
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.
Purity >95% by SDS-PAGE and HPLC analyses.
Endotoxin Level Less than 0.2EU/ug of rHuMIF as determined by LAL method.
Storage This lyophilized preparation is stable 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.



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