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

Produktnummer ABIN2667556

Produktdetails

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

Protein-Typ: Recombinant

Biologische Aktivität: Active

Proteineigenschaft: AA 2-115, N-Term

Spezies: Maus

Quelle: Escherichia coli (E. coli)

Applikation: Flow Cytometry (FACS)

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

Sterilität: 0.22 μm filtered

Endotoxin-Niveau:

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

Anwendungsinformationen

Applikationshinweise: Optimal working dilution should be determined by the investigator.

Kommentare:

Biological activity: Mouse 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 0.4 - 1.5 μg/mL.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Rekonstitution: 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.

Handhabung: Avoid repeated freeze/thaw cycles.

Lagerung: -20 °C

Informationen zur Lagerung: 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.

Antigendetails

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

Andere Bezeichnung: MIF (MIF Produkte)

Synonyme: 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

Hintergrund: 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 acid 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 to be 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.

Molekulargewicht: 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