Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Bioassay data are not available. |
Source | E. coli-derived human MIF protein Pro2-Ala115, with an N-terminal Met |
Accession # | |
N-terminal Sequence | Met1 & Pro2 |
Protein/Peptide Type | Recombinant Proteins |
Purity | >97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 12.4 kDa & 12.3 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Supplied as a 0.2 μm filtered solution in MES and NaCl. |
Purity | >97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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). MIF has proinflammatory cytokine activity centered around amino acids 49 - 65. On fibroblasts, MIF induces, IL-1, IL-8 and MMP expression; on macrophages, MIF stimulates NO production and TNF-alpha release folllowing IFN-gamma activation (13, 14). MIF apparently acts through CD74 and CD44, likely in some form of trimeric interaction (15, 16). Human MIF is active on mouse cells (14). Human MIF is 90%, 94%, 95%, and 90% aa identical to mouse, bovine, porcine and rat MIF, respectively.
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Uniprot |
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