MIF Protein (AA 2-115, N-Term)

Catalog No. ABIN2667555

Product Details

Target: MIF (Macrophage Migration Inhibitory Factor (Glycosylation-Inhibiting Factor) (MIF))

Protein Type: Recombinant

Biological Activity: Active

Protein Characteristics: AA 2-115, N-Term

Origin: Human

Source: Escherichia coli (E. coli)

Application: Flow Cytometry (FACS)

Purity: >95 % , as determined by Coomassie stained SDS-PAGE.

Sterility: 0.22 μm filtered

Endotoxin Level:

Less than 0.1 EU per μg of protein as determine by the LAL method.

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Comment:

Biological activity: Human MIF inhibits the migration of THP-1 cells in the presence of 25 ng/ml of human MCP-1 in a trans-well experimental system. The IC50 is 1.0 - 5.0 μg/mL.

Restrictions: For Research Use only

Handling

Format: Liquid

Reconstitution: For maximum results, quick spin vial prior to opening. Stock solutions should be prepared at no less than 10 μg/mL in sterile buffer (PBS, HPBS, DPBS, and EBSS) containing carrier protein such as 1 % BSA or HSA. After dilution, the cytokine can be stored between 2 °C and 8 °C for one month or from -20 °C to -70 °C for up to 3 months.

Buffer: 0.22 μm filtered protein solution is in PBS.

Handling Advice: Avoid repeated freeze/thaw cycles.

Storage: -20 °C

Storage Comment: Unopened vial can be stored between 2°C and 8°C for three months, at -20°C for six months, or at -70°C for one year.

Target Details

Target: MIF (Macrophage Migration Inhibitory Factor (Glycosylation-Inhibiting Factor) (MIF))

Alternative Name: MIF (MIF Products)

Synonyms: mif Protein, Mif Protein, gif Protein, glif Protein, mmif Protein, LOC100136498 Protein, LOC100284350 Protein, LOC100284546 Protein, GIF Protein, Glif Protein, GLIF Protein, MMIF Protein, macrophage migration inhibitory factor L homeolog Protein, macrophage migration inhibitory factor Protein, macrophage migration inhibitory factor (glycosylation-inhibiting factor) Protein, mif.L Protein, mif Protein, MIF Protein, Mif Protein, PHATRDRAFT_49660 Protein, LOC100136498 Protein, cl405_1 Protein, LOC100284546 Protein

Background: MIF was discovered in the 1960's as a T-lymphocyte product that inhibits the random migration of macrophages during delayed-type hypersensitivity responses. This cytokine is a single, non-glycosylated, 115 amino acids polypeptide that has a β-α-β motif. It is known that MIF induces inflammatory cytokines, nitric oxide and superoxide anions, and regulates macrophage and lymphocyte proliferation. The immunoregulatory activities of MIF are based upon transcriptional regulation of inflammatory gene products, modulation of cell proliferation and cell cycle inhibition of p53-mediated apoptosis, and a number of metabolic effects. MIF also demonstrates broad regulatory properties and is considered as a critical mediator of multiple disorders, including inflammatory and autoimmune diseases such as rheumatoid arthritis, glomerulonephritis, diabetes, atherosclerosis, sepsis, asthma, and acute respiratory distress syndrome. Furthermore, studies have highlighted the role of MIF in tumorigenesis. Human cancer tissues, including skin, brain, breast, colon, prostate, and lung-derived tumors overexpress MIF, MIF levels correlated with tumor aggressiveness and metastatic potential. Therefore, MIF is considered a viable therapeutic target for treating inflammatory diseases and neoplasia. In addition to its physiologic and pathophysiologic activities, MIF is known to act as a tautomerase and has a catalytically active N-terminal proline that is invariant in structurally homologous bacterial isomerases. Although the relationship between the catalytic activity and biological function of MIF is not yet fully understood, targeting MIF tautomerase activity using small-molecule inhibitors has emerged as an attractive strategy for inhibiting MIF proinflammatory activity and attenuating its biological activity in vitro and in vivo. Human and mouse MIF share a 90 % homology.

Molecular Weight: The 115 amino acid recombinant protein has a predicted molecular mass of approximately 12.5 kDa. The protein migrates above 14 kDa by SDS-PAGE in DTT-reducing conditions and above 12.5 kDa in non-reducing conditions. The predicted N-terminal amino acid is

Pathways: Regulation of Systemic Arterial Blood Pressure by Hormones, Positive Regulation of Immune Effector Process, Production of Molecular Mediator of Immune Response, Regulation of Carbohydrate Metabolic Process, Feeding Behaviour, Smooth Muscle Cell Migration, Negative Regulation of intrinsic apoptotic Signaling