Glycosylation-inhibiting factor, L-dopachrome isomerase, MIF, Macrophage Migration Inhibitory Factor, Macrophage Migration Inhibitory Factor (Glycosylation-Inhibiting Factor), GLIF, MMIF, EC:, GIF, EC, EC, Macrophage Migration-Inhibitory Factors, Epididymis Secretory Sperm Binding Protein, EC:, Phenylpyruvate Tautomerase, L-Dopachrome Tautomerase


MIF is an important regulator of innate immunity.The MIF protein superfamily also includes a second member with functionally related properties, the D-dopachrome tautomerase (D-DT).CD74 is a surface receptor for MIF.Macrophage migration inhibitory factor is a protein that in humans is encoded by the MIF gene.The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity.

KO Status


Drug Information

Launched drug: 1
Drug in clinical trials: 1
Latest Research Phase: Approved

Drug Name





Clinical Trials


AV-411, KC-404, MN-166


Diabetic Neuropathies, Multiple Sclerosis, Chronic Progressive, Multiple Sclerosis, Pneumonia, Viral, Asthma, Neuralgia, Amyotrophic Lateral Sclerosis


BAX-69, BAX-069

Phase 2 Clinical

Cytokine Pharmasciences

Ovarian Neoplasms, Lupus Nephritis, Ascites, Colorectal Neoplasms

Melanoma vaccine (AlphaVax)







Cytokine Pharmasciences

Communicable Diseases



Ferring Bv






Autoimmune Diseases, Breast Neoplasms, Prostatic Neoplasms, Inflammation





Coumarin and chromen-4-one analogues as tautomerase inhibitors of macrophage migration inhibitory factor: discovery and X-ray crystallography

Orita M., Yamamoto S., Katayama N., Aoki M., Takayama K., Yamagiwa Y., Seki N., Suzuki H., Kurihara H., Sakashita H., Takeuchi M., Fujita S., Yamada T., Tanaka A.,

J. Med. Chem. 44:540-547(2001)

Alternative chemical modifications reverse the binding orientation of a pharmacophore scaffold in the active site of macrophage migration inhibitory factor

Crichlow G.V., Cheng K.F., Dabideen D., Ochani M., Aljabari B., Pavlov V.A., Miller E.J., Lolis E., Al-Abed Y.,

J. Biol. Chem. 282:23089-23095(2007)

Structural and kinetic analyses of macrophage migration inhibitory factor active site interactions

Crichlow G.V., Lubetsky J.B., Leng L., Bucala R., Lolis E.J.,

Biochemistry 48:132-139(2009)

MIF intersubunit disulfide mutant antagonist supports activation of CD74 by endogenous MIF trimer at physiologic concentrations

Fan C., Rajasekaran D., Syed M.A., Leng L., Loria J.P., Bhandari V., Bucala R., Lolis E.J.,

Proc. Natl. Acad. Sci. U.S.A. 110:10994-10999(2013)

A genome annotation-driven approach to cloning the human ORFeome

Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.,

Genome Biol. 5:R84.1-R84.11(2004)

Complete sequencing and characterization of 21,243 full-length human cDNAs

Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Sugano S.,

Nat. Genet. 36:40-45(2004)

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)

The MGC Project Team,

Genome Res. 14:2121-2127(2004)

Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides

Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.,

Nat. Biotechnol. 21:566-569(2003)

Human liver protein map: a reference database established by microsequencing and gel comparison

Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.,

Electrophoresis 13:992-1001(1992)

The major binding protein of the interferon antagonist sarcolectin in human placenta is a macrophage migration inhibitory factor

Zeng F.Y., Weiser W.Y., Kratzin H., Stahl B., Karas M., Gabius H.J.,

Arch. Biochem. Biophys. 303:74-80(1993)