Recombinant Human MIF Protein

• Reactivity: Hu
• Applications: PAGE, Bioactivity
• Format: Carrier-Free
• Concentration: LYOPH

Recombinant Human MIF Protein Summary

• Description: A single non-glycosylated polypeptide chain containing 115 amino acids corresponding to MIF Source: E. coli

  Amino Acid Sequence: MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA

• 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: >95%, by SDS-PAGE
• Endotoxin Note: Less than 1 EU/ug of MIF as determined by LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
  • SDS-Page
• 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 -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.
• Buffer: Lyophilized from a 0.2 um filtered concentrated solution in PBS, pH 7.4. with 0.02% Tween-80.
• Preservative: 5% Trehalose
• Concentration: LYOPH
• Purity: >95%, by SDS-PAGE
• Reconstitution Instructions: Recommended to centrifuge prior to opening. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL.

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.

Publications for MIF Recombinant Protein (NBP2-34998)(1)

Publication using NBP2-34998

• Jovanovic Krivokuca M, Stefanoska I, Vilotic A et al. Macrophage migration inhibitory factor modulates cytokine expression in the trophoblast cell line HTR-8/SVneo Reproduction, fertility, and development 2020-12-16 [PMID: 33323165]

Bioinformatics

• Gene Symbol: MIF