MIF-3

E.coli

MIF, Glutathione-binding 13 kDa Protein, L-dopachrome Isomerase, L-dopachrome Tautomerase, Phenylpyruvate Tautomerase

Macrophage migration inhibitory factor (MIF or MMIF), also named as glycosylation-inhibiting factor (GIF), L-dopachrome isomerase, or phenylpyruvate tautomerase, is a protein encoded by the MIF gene. It is released from white blood cells by bacterial antigen stimulation to trigger an acute immune response, or by glucocorticoids to counter-act the inhibitory effects of glucocorticoids on immune system. MIF is a homotrimer of which each subunit contains 115 amino acids. As mentioned above, MIF is involved in the innate immune response to bacterial pathogens and counter-acts the anti-inflammatory activity of glucocorticoids. Furthermore, it also plays a role as mediator in regulating the function of macrophages in host defense and has phenylpyruvate tautomerase and dopachrome tautomerase activity in vitro. Rat MIF is 99 %, 90 %, 89 %, and 89 % a.a. identical to human, murine, porcine and bovine, respectively.

Approximately 12.5 kDa

MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTSDPCALC SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA

Sterile Filtered White lyophilized (freeze-dried) powder.

> 97 % by SDS-PAGE and HPLC analyses.

< 1.0 EU per 1μg of the protein

Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM Tris, pH 8.0, 150 mM NaCl, 3 % trehalose.