Recombinant Mouse Resistin Protein, CF

Catalog # Availability Size / Price Qty
5335-RN-050
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Mouse Resistin Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
Measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells. The ED50 for this effect is 0.8-4 μg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse Resistin protein
Ser21-Ser114
Accession #
N-terminal Sequence
Analysis
Ser21
Structure / Form
Homohexamer
Predicted Molecular Mass
10.2 kDa
SDS-PAGE
10 kDa, under reducing conditions

Product Datasheets

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5335-RN

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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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).

References
  1. Asano, T. et al. (2006) Curr. Diabetes Rev. 2:449.
  2. McTernan, P.G. et al. (2006) Curr. Opin. Lipidol. 17:170.
  3. Pang, S. and Y. Le (2006) Cell. Mol. Immunol. 3:29.
  4. Robertson, S.A. et al. (2008) Regul. Pept. Aug 5 epub.
  5. Patel, S.D. et al. (2004) Science 304:1154.
  6. Steppan, C.M. et al. (2001) Nature 409:307.
  7. Chen, J. et al. (2002) J. Endocrinol. 175:499.
  8. Banerjee, R.R. and M.A. Lazar (2001) J. Biol. Chem. 276:25970.
  9. Del Arco, A. et al. (2003) FEBS Lett. 555:243.
  10. Milan, G. et al. (2002) Obesity Res. 10:1095.
  11. Morash, B.A. et al. (2002) FEBS Lett. 526:26.
  12. Rajala, M.W. et al. (2003) J. Clin. Invest. 111:225.
  13. Banerjee, R.R. et al. (2004) Science 303:1195.
  14. Ribot, J. et al. (2008) Obesity 16:723.
Entrez Gene IDs
56729 (Human); 57264 (Mouse)
Alternate Names
Adipose tissue-specific secretory factor; ADSF; ADSFMGC126609; C/EBP-epsilon regulated myeloid-specific secreted cysteine-rich proteinprecursor 1; C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein; Cysteine-rich secreted protein A12-alpha-like 2; Cysteine-rich secreted protein FIZZ3; FIZZ3; FIZZ3MGC126603; found in inflammatory zone 3; HXCP1; Resistin; RETN; RETN1; RSTNXCP1

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