Recombinant Human MIF

Molecule:

MIF

Synonyms:

GIF, GLIF, MMIF, glycosylation-inhibiting factor, phenylpyruvate tautomerase

Species:

Human

Cat. No.:

CSI20147A pdf (datasheet)

Quantity/Size:

10 μg

Price:

$190.00 BUY

Description:

Recombinant Human MIF is a single non-glycosylated polypeptide chain containing 115 amino acids.

Background: Migration Inhibitory Factor (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 (enolto-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-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% aa identical to mouse, bovine, porcine and rat MIF, respectively.

Data PDF:

CSI20147

Source:

E. coli

Molecular Weight:

~12.5 kDa

Formulation:

Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.

Purity:

>97 % by SDS-PAGE and HPLC analyses.

Biological Activity:

Fully biologically active when compared to standard. The specific activity is determined by binding rhCD74 in a functional ELISA.

Endotoxin Level:

Less than 1 EU/μg of recombinant human MIF as determined by LAL method.

Amino Acid Sequence:

MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA

Reconstitution:

Centrifuge vial prior to opening. 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.

Storage/Stability:

This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.