- Regulatory Status
- Other Names
- Macrophage migration inhibitory factor, GIF, GLIF, MMIF
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- Product Citations
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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.Product Details
- Human MIF, amino acids (Pro2-Ala115) (Accession# NP_002406.1), was expressed in E. coli with an additional N-terminal Met.
- Molecular Mass
- The 115 amino acid recombinant protein has a predicted molecular mass of approximately 12.5 kD. The protein migrates above 14 kD by SDS-PAGE in DTT-reducing conditions and above 12.5 kD in non-reducing conditions. The predicted N-terminal amino acid is Met.
- >95%, as determined by Coomassie stained SDS-PAGE.
- 0.22 µm filtered protein solution is in PBS.
- Endotoxin Level
- Less than 0.1 EU per µg of protein as determine by the LAL method.
- 10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial. To obtain lot-specific concentration and expiration, please enter the lot number in our Certificate of Analysis online tool.
- Storage & Handling
- Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
- Application Notes
We currently check the quality of this recombinant protein by purity, endotoxin level and molecular weight. At this time, we do not have bioassay system established yet for testing this protein. However, we are continuing to seek out options to test its activity.
BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are verified in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at firstname.lastname@example.org.
Macrophages, eosinophils, T cells, pituitary gland.
- MIF stimulates IL-1, IL-8, and MMP expression on fibroblasts. It also stimulates NO and TNF-alpha production on macrophages. MIF regulates the migration of macrophages. The secretion of MIF is regulated by steroids.
- Macrophages, fibroblasts
- Human MIF inhibits the migration of THP-1 cells in the presence of human MCP-1
- Biology Area
- Cell Biology, Cell Motility/Cytoskeleton/Structure, Immunology, Innate Immunity
- Molecular Family
- Antigen References
1. David JR. 1966. Proc. Natl. Acad. Sci. 56:72.
2. Hare AA, et al. 2010. Bioorg. Med. Chem. Lett. 20:5811.
3. Calandra T, et al. 2003. J. Infect. Dis. 187:s385.
4. Senter PD, et al. 2002. Proc. Natl. Acad. Sci. 99:144.
5. Calandra T, et al. 1995. Nature. 377:68.
6. Ouertatani-Sakouhi H, et al. 2010. Biol. Chem. 285:26581.
- Gene ID
- 4282 View all products for this Gene ID
- View information about MIF on UniProt.org
- Why choose BioLegend recombinant proteins?
• Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
• Greater than 95% Purity or higher, tested on every lot of product.
• 100% Satisfaction Guarantee for quality performance, stability, and consistency.
• Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
• Bulk and customization available. Contact us.
• Learn more about our Recombinant Proteins.
- How does the activity of your recombinant proteins compare to competitors?
We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!
- What is the specific activity or ED50 of my recombinant protein?
The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.
- Have your recombinants been tested for stability?
Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.
- Does specific activity of a recombinant protein vary between lots?
Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.
- How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)