Recombinant Mouse MIF protein

Background

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. Mouse MIF is active on human cells, while human MIF is active on mouse cells. Mouse MIF is 99 %, 84 %, 90 %, and 90 % a.a. identical to rat, porcine, bovine and human MIF, respectively.

Expression system

Escherichia coli.

Purity

> 96 % by SDS-PAGE and HPLC analyses.

Molecular weight

Approximately 12.5 kDa, a single non-glycosylated polypeptide chain containing 115 amino acids.

Endotoxin

Less than 1 EU/μg of rMuMIF as determined by LAL method.

Form

Sterile Filtered White lyophilized (freeze-dried) powder. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, 1 mM DTT.

Packaging image shown for reference. Select a size from the available options.