MIF (or macrophage migration inhibitory factor) was the first lymphokine/cytokine to be recognized in the pregenomics era (1, 2). Regardless, it is one of the least understood of all inflammatory mediators (1, 3). Human MIF is a 12.5 kDa, 115 amino acid (aa) nonglycosylated polypeptide that is synthesized without a signal sequence (4 - 7). Secretion occurs nonclassically via an ABCA1 transporter (8). The initiating Met is removed, leaving Pro as the first amino acid. The molecule consists of two alpha -helices and six beta -strands, four of which form a beta -sheet. The two remaining beta -strands interact with other MIF molecules, creating a trimer (2, 9, 10). 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 (11). Amino acids 50 - 65 have also been suggested to contain thiol-protein oxidoreductase activity (12).
Lyophilized from a 0.22 µm filtered solution of 50mM Tris 150mM NaCl pH8.0.
Target:
MIF
Application Dilute:
Lyophilized from a 0.22 µm filtered solution of 50mM Tris 150mM NaCl pH8.0.
Application Notes:
Cross-Reactivity: Centrifµge the vial before opening. Reconstitute to a concentration of 0.1-0.5 mg/mL in sterile distilled water. Avoid vortex or vigorously pipetting the protein. For long term storage,it is recommended to add a carrier protein or stablizer (e.g. 0.1% BSA,5% HSA,10% FBS or 5% Trehalose),and aliquot the reconstituted protein solution to minimize free-thaw cycles., ResearchArea: Cytokines & Cytokine receptors
Recombinant Mouse Macrophage migration inhibitory factor/MIF Protein was determined by SDS-PAGE under reducing conditions with Coomassie Blue.
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