Recombinant Human MIF Protein Summary
A biologically active protein to MIF.
Source: E. coli
Amino Acid Sequence: MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA
Novus' biologically active proteins are stringently purified to provide only the safest and most highly effective proteins available. This protein was expressed in E. coli, purified by HPLC, QC tested by SDS-PAGE and Western Blot and validated on appropriate cell lines for bioactivity. All HPLC and bioactivity data is provided for your assurance.
|Details of Functionality
MIF Protein is fully biologically active when compared to standard. The specific activity is determined by binding rhCD74 in a functional ELISA.
| Protein/Peptide Type
Biologically Active Protein
> 97 % pure by SDS-PAGE and HPLC
Less than 1EU/ug of endotoxin as determined by LAL method.
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.
Packaging, Storage & Formulations
Store at -20 to -70C as supplied. After reconstitution, store at 2 to 8C for 1 month and at -20 to -70C for long term storage. Avoid repeated freeze-thaw cycles.
Lyophilized from a 0.2 um filtered concentrated solution in PBS, pH 7.4.
> 97 % pure by SDS-PAGE and HPLC
Reconstitute with sterilized distilled water or 0.1% BSA aqueous buffer to a final concentration of 0.1 - 1.0 mg/ml.
This lyophilized preparation is stable at 2-8 degrees C, but should be kept at -20 degrees C for long term storage, preferably desiccated. Upon reconstitution, the preparation is most stable at -20 to -80 degrees C, and can be stored for one week at 2-8 degrees C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20 degrees C to -80 degrees C. Avoid repeated freeze/thaw cycles.
Alternate Names for Recombinant Human MIF Protein
- EC 22.214.171.124
- EC 126.96.36.199
- GIFmacrophage migration inhibitory factor
- Glycosylation-inhibiting factor
- L-dopachrome isomerase
- L-dopachrome tautomerase
- macrophage migration inhibitory factor (glycosylation-inhibiting factor)
- Phenylpyruvate tautomerase
Migration Inhibitory Factor (MIF) is a secreted protein without a cleavable signal sequence and is secreted via a specialized, nonclassical pathway. It is secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens. MIF 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. 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-alpha release folllowing IFN-gamma 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.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed
for 2 years from date of receipt.
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