- Regulatory Status
- Other Names
- Adipose tissue-specific secretory factor (ADSF), C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, FIZZ3, RETN1, RSTN
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- Product Citations
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Resistin, originally found in the inflammatory zone in humans, is a cysteine-rich secreted peptide hormone. It belongs to a member of the resistin-like molecule family. In rodents, resistin exists in two distinct states in circulating serum, noncovalent coiled-coil trimers and disulfide bond-linked tail-to-tail hexamers. Rodent resistin is mainly secreted by mature adipocytes, and it has been linked to the pathogenesis of obesity-mediated insulin resistance and of type 2 diabetes. Resistin-deficient mice exhibit low glucose levels and reduced hepatic glucose production after fasting, suggesting a role of resistin in the maintenance of blood glucose during fasting. Administration of recombinant resistin to normal mice leads to impairment of glucose tolerance and insulin action. Rodent resistin inhibits adipocyte differentiation, as a feedback regulator of adipogenesis. In addition, resistin stimulates pro-inflammatory cytokines TNF-α and IL-6 via NF-κB activation in rat pancreatic acinar cells. In humans, resistin is primarily expressed and secreted from peripheral blood mononuclear cells, bone marrow cells and macrophages. Resistin serum levels are associated with insulin resistance, disease severity, clinical complications, and prognosis in patients with chronic liver disease. Human resistin directly aggravates atherosclerosis by stimulating monocytes to induce vascular inflammation. Human resistin stimulates the pro-inflammatory cytokines TNF-α/IL-12 in macrophages and TNF-α/IL-6 in adipocytes via an NF-κB-dependent pathway. TNF-α induces upregulation of resistin in human macrophages. Resistin promotes neutrophil pro-inflammatory activation, neutrophil extracellular trap formation, and increases the severity of acute lung injury in humanized resistin mice (hRTN+/−/−) (mice that express human resistin but lack murine resistin). Resistin is increased in the circulation of patients with acute respiratory distress syndromes and sepsis.Product Details
- Mouse Resistin, amino acids (Ser21 - Ser114) (Accession: NP_075360.1), was expressed in .E. coli.
- Molecular Mass
- The 94 amino acid recombinant protein has a predicted molecular mass of approximately 10 kD. The predicted N-terminal amino acid is Ser.
- >95%, as determined by Coomassie stained SDS-PAGE.
- Lyophilized from 0.22 μm filtered protein solution is in PBS pH 7.2.
- Endotoxin Level
- Less than 0.1 EU per μg protein as determined by the LAL method.
- Storage & Handling
- Unopened vial can be stored between 2°C and 8°C for one month, at -20°C for six months, or at -70°C for one year. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C to -70°C. Stock solutions can also be prepared at 50 - 100 µg/mL in sterile buffer (PBS, HPBS, DPBS, or EBSS) containing carrier protein such as 0.2 - 1% BSA or HSA and stored in working aliquots at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
- Mouse Resistin induces the expression of IL-6 in mouse 3T3-L1 cells in a dose-dependent manner. The ED50 for this effect is 0.8 - 4 µg/mL.
- Application Notes
BioLegend carrier-free recombinant proteins provided in lyophilized format are shipped on blue ice. If you have any concerns, contact us at firstname.lastname@example.org.
- Monomer and disulfide bond-linked homodimer
Predominantly expressed in rodent adipocytes, detectable level in stomach, intestines, adrenal gland, and skeletal muscle.
- Rodent resistin antagonizes insulin action, and it has been linked to the pathogenesis of obesity-mediated insulin resistance and of type 2 diabetes. Resistin inhibits adipoctye differentiation.
- Rodent adipocytes, skeletal muscle, cardiomyocytes.
- Rat Resistin induces the expression of IL-6 in mouse 3T3-L1 cells.
- Cell Sources
- E. coli
- Molecular Family
- Enzymes and Regulators
- Antigen References
- Banerjee RR, et al. 2004. Science. 303:1195-8.
- Steppan CM, et al. 2001. Nature. 409:307-12.
- Hsu WY, et al. 2011. J. Cell. Physiol. 10.1002/jcp.22555.
- Mu H, et al. 2006. Cardiovasc. Res. 70:146-57.
- Holcomb IN, et al. 2000. EMBO J. 15:4046-455.
- Patel L, et al. 2003. Biochem. Biophys. Res. Commun. 300:472-6.
- Bokarewa M, et al. 2005. J. Immunol. 174:5789-95.
- Silswal N, et al. 2005. Biochem. Biophys. Res. Commun. 334:1092-101.
- Yagmur E, et al. 2006. Am. J. Gastroenterol. 101:1244-52.
- Cho Y, et al. 2011. J. Am. Coll. Cardiol. 10.1016/j.jacc.2010.07.035.
- Fang JD, Lee SL. 2014. Biochim. Biophys. Acta. 7:1285-94.
- Jiang S, et al. 2014. J. Immunol. 192:4795-803.
- Stojsavljević S, et al. 2014. World J. Gastroenterol 48:18070-91.
- Pravenec M, et al. 2003. J. Biol. Chem. 278:45209-15.
- Nogueiras R, et al. 2003. FEBS Lett. 548:21-27.
- Jiang CY, et al. 2013. J. Endocrinol. Invest. 36:986-92.
- Kusminski CM, et al. J. Clin. Endocrinol. Metab. 92:270-6.
- Kim KH, et al. 2001. J. Biol. Chem. 76:11252-6.
- Patel SD, et al. 2004. Science. 304:1154-58.
- Park HK, Ahima RS. 2013. Diabetes Metab. J. 10.4093/dmj.2013.37.6.404.
- Gene ID
- 57264 View all products for this Gene ID
- View information about Resistin 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) = 10e6/ ED50 (ng/mL)