Recombinant Mouse Resistin Protein, CF Summary
Product Specifications
Ser21-Ser114
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
5335-RN
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 500 μg/mL in sterile PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
Background: Resistin
Resistin (resistance-to-insulin), also known as adipocyte-specific secretory factor (ADSF) and found in inflammatory zone 3 (FIZZ3), is a 10 kDa member of a small family of secreted cysteine-rich peptide hormones. These molecules purportedly play some role in inflammation, glucose metabolism, and angiogenesis (1, 2, 3, 4). Mouse Resistin precursor is 114 amino acids (aa) in length. It contains a 20 aa signal sequence plus a 94 aa mature region. The mature region shows an N-terminal alpha -helical tail (aa 27 - 48) and a C-terminal beta -sheet globular head (aa 51 - 112) (5, 6). The Resistin molecule circulates as either a noncovalent trimer (minor form), or a disulfide-linked homohexamer (major form). Noncovalent trimers are generated when the alpha -helical segments self-associate to form a three-stranded coiled-coil structure. Covalent hexamers subsequently appear when the free Cys at position #26 is engaged by adjacent trimers. It is hypothesized that the hexamer is a less active form of the molecule, and bioactivity is achieved at the target site by disulfide bond reduction (5). Although Resistin family molecules can noncovalently interact to form heterotrimers in vitro, there is no evidence to suggest this occurs in vivo with Resistin (7, 8). Mature mouse Resistin shares 72% and 56% aa identity with rat and human Resistin, respectively. Rat Resistin possesses an alternate start site at Met48; this Met is not found in the mouse molecule, however (9). Rodent Resistin is expressed by white adipocytes, splenocytes, astrocytes, and anterior pituitary epithelium (6, 10, 11). Although the function of Resistin is unclear, it would seem to block insulin-stimulated uptake of glucose by adipocytes, and promote glucose release by hepatocytes (6, 12, 13). As such, it has been proposed to participate in diet-induced insulin-sensitivity. Diets high in fat promote an increase in overall adipocyte size. Hypertrophic adipocytes are known to secrete TNF-alpha, which acts locally to block ACRP30 production. Since ACRP30 is an insulin-sensitizer, a drop in ACRP30 availability leads to insulin-insensitivity, which drives increased insulin production (a compensatory mechanism). High insulin induces Resistin secretion, which now antagonizes insulin action, prompting more insulin production, and more Resistin secretion (14).
- Asano, T. et al. (2006) Curr. Diabetes Rev. 2:449.
- McTernan, P.G. et al. (2006) Curr. Opin. Lipidol. 17:170.
- Pang, S. and Y. Le (2006) Cell. Mol. Immunol. 3:29.
- Robertson, S.A. et al. (2008) Regul. Pept. Aug 5 epub.
- Patel, S.D. et al. (2004) Science 304:1154.
- Steppan, C.M. et al. (2001) Nature 409:307.
- Chen, J. et al. (2002) J. Endocrinol. 175:499.
- Banerjee, R.R. and M.A. Lazar (2001) J. Biol. Chem. 276:25970.
-
Del Arco, A. et al. (2003) FEBS Lett. 555:243.
-
Milan, G. et al. (2002) Obesity Res. 10:1095.
-
Morash, B.A. et al. (2002) FEBS Lett. 526:26.
-
Rajala, M.W. et al. (2003) J. Clin. Invest. 111:225.
-
Banerjee, R.R. et al. (2004) Science 303:1195.
-
Ribot, J. et al. (2008) Obesity 16:723.
FAQs
No product specific FAQs exist for this product, however you may
View all Proteins and Enzyme FAQsReviews for Recombinant Mouse Resistin Protein, CF
There are currently no reviews for this product. Be the first to review Recombinant Mouse Resistin Protein, CF and earn rewards!
Have you used Recombinant Mouse Resistin Protein, CF?
Submit a review and receive an Amazon gift card.
$25/€18/£15/$25CAN/¥75 Yuan/¥2500 Yen for a review with an image
$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image