MIF Recombinant Protein

Macrophage migration inhibitory factor (MIF) is a small secreted protein that can act as a pleiotropic pro-inflammatory cytokine, as well as an enzyme. MIF pro-inflammatory activity can be initiated by signaling through CD74 and CD44, resulting in the secretion of TNF-a, IL-1, IL-6, IL-8, and various MMPs. The enzymatic activity of MIF is characterized by its ability to act as a tautomerase, capable of catalyzing the keto-to-enol isomerization of keto-phenylpyruvate and L-dopachrome. It appears as though MIF catalytic activity is dependent upon a trimeric configuration and a free N-terminal proline residue. Insect cell-derived Recombinant Human MIF is a 15 kDa protein containing 124 amino acid residues, including an N-terminal His-tag.

The recombinant protein is stable for at least 2 years from date of receipt at -20˚ C. Reconstituted protein is stable for at least 3 months when stored in working aliquots with a carrier protein at -20˚ C. As with any protein, exposing the recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.