Recombinant Human MIF Protein

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Func, PAGE, Bioactivity
Format
Carrier-Free
Concentration
LYOPH

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Recombinant Human MIF Protein Summary

Description
A biologically active protein to MIF.

Source: E. coli

Amino Acid Sequence: MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA
Preparation
Method
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.
Source
E. coli
Protein/Peptide Type
Recombinant Protein
Gene
MIF
Purity
> 97 % pure by SDS-PAGE and HPLC
Endotoxin Note
Less than 1EU/ug of endotoxin as determined by LAL method.

Applications/Dilutions

Theoretical MW
12.5 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.

Packaging, Storage & Formulations

Storage
Store at -20C. Avoid freeze-thaw cycles.
Buffer
Lyophilized from a 0.2 um filtered concentrated solution in PBS, pH 7.4.
Concentration
LYOPH
Purity
> 97 % pure by SDS-PAGE and HPLC
Reconstitution Instructions
Reconstitute with sterilized distilled water or 0.1% BSA aqueous buffer to a final concentration of 0.1 - 1.0 mg/ml.

Notes

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 5.3.2.1
  • EC 5.3.3.12
  • GIFmacrophage migration inhibitory factor
  • GLIF
  • Glycosylation-inhibiting factor
  • L-dopachrome isomerase
  • L-dopachrome tautomerase
  • macrophage migration inhibitory factor (glycosylation-inhibiting factor)
  • MIF
  • MMIF
  • Phenylpyruvate tautomerase

Background

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.

Limitations

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 3 months from date of receipt.

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Bioinformatics

Gene Symbol MIF
Entrez