Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Bioassay data are not available. |
Source | E. coli-derived mouse MIF protein Pro2-Ala115 |
Accession # | |
N-terminal Sequence | Pro2 |
Protein/Peptide Type | Recombinant Proteins |
Gene | Mif |
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. 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 | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
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). Mouse 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 (6). 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, 8). Structure-function studies suggests 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 (9). Amino acids 3 - 23 have also been shown to be reminescent of a GST glutathione-binding domain (10). MIF has proinflammatory cytokine activity centered on aa’s 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 (11, 12). Mouse MIF apparently acts through CD74 and CD44, likely in some form of trimeric interaction (13, 14). Mouse MIF is active on human cells, while human MIF is active on mouse cells (12). Mouse MIF is 99%, 84%, 90%, and 90% aa identical to rat, porcine, bovine and human MIF, respectively.
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