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Recombinant Human Macrophage Migration Inhibitory Factor, His

Catalog No.
P1607
 
Grouped product items
SizePriceStock Qty
10ug
$99.00
Ship with 5-10 days
100ug
$977.00
Ship with 5-10 days
500ug
$2,190.00
Ship with 5-10 days
For scientific research use only and should not be used for diagnostic or medical purposes.

Tel: +1-832-696-8203

Email: [email protected]

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Background

Migration Inhibitory Factor (MIF) is a secreted protein without a cleavable signal sequence and is secreted via a specialized, non-classical pathway. It is secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens. MIF consists of two α-helices and six β-strands, four of which form a β-sheet. The two remaining β-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 (a.a.) 49 - 65. On fibroblasts, MIF induces, IL-1, IL-8 and MMP expression; on macrophages, MIF stimulates NO production and TNF-α release folllowing IFN-γ 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% aa identical to mouse, bovine, porcine and rat MIF, respectively.

Reference

1. Edwards KM, Tomfohr LM, Mills PJ, et al. 2011. Sleep, 34: 161-3

2. Delaloye J, De Bruin IJ, Darling KE, et al. 2012. Cytokine

3. Leu RW, Woodson PD, Whitley SB. 1977. J Reticuloendothel Soc, 22: 329-40

4. Landolfo S. 1977. G Batteriol Virol Immunol, 70: 137-43

5. Baugh JA, Chitnis S, Donnelly SC, et al. 2002. Genes Immun, 3: 170-6.

Information

Alternate NamesGLF, L-dopachrome Isomerase, Phenylpyruvate Tautomerase
SourceEscherichia coli.
M.WtApproximately 13.5 kDa, a single non-glycosylated polypeptide chain containing 117 amino acids, with 6 × His at the C-terminus.
AA SequenceMPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFALEHHH HHH
AppearanceSterile Filtered White lyophilized (freeze-dried) powder.
Stability & StorageUse a manual defrost freezer and avoid repeated freeze-thaw cycles.
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
FormulationLyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.
ReconstitutionWe recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
Biological ActivityFully biologically active when compared to standard. The specific activity is determined by binding rhCD74 in a functional ELISA.
Shipping ConditionGel pack.
HandlingCentrifuge the vial prior to opening.
UsageFor Research Use Only! Not to be used in humans.

Quality Control

Quality Control & DataSheet

View current batch:
    Purity > 95 % by SDS-PAGE and HPLC analyses.
    Endotoxin: Less than 1 EU/µg of rHuMIF, His as determined by LAL method.
  • Datasheet