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Recombinant Human Macrophage Migration Inhibitory Factor

Catalog No.
P1593
 
Grouped product items
SizePriceStock Qty
10ug
$99.00
Ship with 5-10 days
100ug
$813.00
Ship with 5-10 days
500ug
$1,825.00
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 12.5 kDa, a single non-glycosylated polypeptide chain containing 115 amino acids.
AA SequenceMPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA
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. with 5% trehalose, 0.02% Tween-80.
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.
    Endotoxin: Less than 1 EU/μg of rHuMIF as determined by LAL method.
  • Datasheet