Mouse MIF (His Tag) recombinant protein

Mouse MIF (His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

Macrophage migration inhibitory factor (MIF) is an immunoregulatory cytokine, the effect of which on arresting random immune cell movement was recognized several decades ago. Despite its historic name, MIF also has a direct chemokine-like function and promotes cell recruitment. MIF is an ubiquitously expressed protein that plays a crucial role in many inflammatory and autoimmune disorders. Increasing evidence suggests that MIF also controls metabolic and inflammatory processes underlying the development of metabolic pathologies associated with obesity. Further research has shown that MIF plays a particularly critical part in cell cycle regulation and therefore in tumorigenesis as well. The significance of the role of MIF in a variety of both solid and hematologic tumors has been established. More recently, interest has increased in the role of MIF in the development of central nervous system (CNS) tumors, in which it appears to influence cell cycle control. MIF contributes to malignant disease progression on several different levels. Both circulating and intracellular MIF protein levels are elevated in cancer patients and MIF expression reportedly correlates with stage, metastatic spread and disease-free survival. Blockade of MIF bioactivity successfully inhibited tumor cell growth in vivo and in vitro. MIF plays important roles in the pathogenesis of gastrointestinal, hepatic, and pancreatic disorders.

Macrophage migration inhibitory factor

MGC107654; GIF; MMIF; GLIF; DER6; MIF

P34884

Mif

Human Cells

A DNA sequence encoding the mouse MIF (P34884) precursor (Pro 2-Ala 115) was fused with a polyhistidine tag at the C-terminus and a signal peptide at the N-terminus.

Mouse

The secreted recombinant mouse MIF consists of 125 amino acids and has a calculated molecular mass of 13.8 kDa. As a result of glycosylation, the apparent molecular mass of the recombinant protein is approximately 18 and 22 kDa in SDS-PAGE under reducing conditions due to different glycosylation.

> 85 % as determined by SDS-PAGE