Product name
Recombinant Human MIF protein (His Tag)
Code
CD01288
Biological activity
Fully biologically active when compared to standard. The specific activity is determined by binding rhCD74 in a functional ELISA.
Endotoxin
Less than 1 EU/μg of rHuMIF, His as determined by LAL method.
Synonyms
MIF,GIF, GLIF, MMIF,Human
Sequence
MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFALEHHH HHH
Uniprot Accession
Molecular Weight
Approximately 13.5 kDa, a single non-glycosylated polypeptide chain containing 117 amino acids, with 6 × His at the C-terminus.
Formulation
Lyophilized from a 0.2 μm 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.
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.
Storage
-20ºC
Research area
Others
