Fibroblast growth factor 21, Recombinant, Human (FGF-21)

Human FGF-21 Fibroblast growth factor 21 (FGF-21) is a member of the FGF gene family, which currently contains 22 human members. Based on its structure, it is further classified as an FGF19 subfamily member. This subfamily includes FGF-19, -21, and -23. Like all other FGF subfamilies, FGF-19 subfamily members contain a 120 amino acid (aa) core FGF domain that exhibits a b-trefoil structure (1, 2). Unlike other FGF subfamilies, FGF-19 subfamily members apparently exhibit poor binding to ECM, resulting in highly diffusible molecules (3). The c-DNA for FGF-21 predicts a 209 aa polypeptide that contains a 28 aa signal sequence and a 181 aa mature region (4). Notably, FGF-21, as well as FGF-19 shows limited binding to heparin (4). One potential alternate splice form has been reported. It shows a 43 aa substitution for the C-terminal 12 aa of the standard form (5). Mature human FGF-21 shows 81% aa identity to mouse FGF-21, and is known to be active on mouse cells (4, 6). The FGF-19 subfamily is considered endocrine in nature. All three subfamily members impact some aspect of metabolism, all three are induced by a nuclear receptor heterodimer that includes RXR, and all three utilize Klotho family members for signal transduction (7, 8, 9). FGF-21 is produced by hepatocytes in response to free fatty acid (FFA) stimulation of a PPARa/RXR dimeric complex (3, 7, 10, 11). This situation occurs clinically during starvation, or following the ingestion of a high-fat/low-carbohydrate diet. Upon FGF-21 secretion, white adipose tissue is induced to release FFAs from triglyceride stores. Once FFAs reach hepatocytes, they are oxidized and reduced to acetyl-CoA. The acetyl-CoA is recombined into 4-carbon ketone bodies (acetoacetate and b-hydroxybutyrate), released, and transported to peripheral tissues for TCA processing and energy generation (11, 12). \n \nA DNA sequence encoding the mature human FGF-21 (His 29-Ser 209; Accession # Q9NSA1) was fused with 5X histidines at the N-terminus. The protein was expressed in E. coli. \n\nMolecular Mass: Based on N-terminal amino acid sequencing, the recombinant human FGF-21 starts at the histidine tag and has a predicted molecular mass of approximately 20.2kD. \n\nEndotoxin Level: (same/less than) 1 EU/ug of the protein as determined by the LAL method. \n\nBiological Activity: \nMeasured by its ability to stimulate the proliferation of NIH3T3 cells. The ED 50 for this effect is typically 0.12-0.6ug/ml in the presence of 5ug/ml of rmKlotho-beta\nMeasured in a cell proliferation assay using human FGF RIIIc transfected BaF3 mouse pro

Prices direct from United States Biological

Quick response times

Exclusive Biosave savings/discounts

SPECIFICATIONS

Catalog Number

F4212-93A

Size

25ug

Form

Supplied as a lyophilized powder in 10 mM MES, 50 mM sodium sulfate, 0.2 mM EDTA and \n0.2 mM DTT, pH 6.5. Reconstitute with PBS to a concentration of 0.1mg/ml.

Purity

> 97%, as determined by SDS-PAGE and visualized by silver stain. Endotoxin: < 1.0 EU per 1ug of the protein as determined by the LAL method.

References

1. Itoh, N. & D.M. Ornitz (2004) Trends Genet. 20:563. 2. Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107. 3. Huang, X. et al. (2006) Mol. Carcinog. 45:934. 4. Nishimura, T. et al. (2000) Biochim. Biophys. Acta 1492:203. 5. GenBank Accession #: EAW52401 (2006). 6. Ford, A.M. et al. (2005) J. Clin. Invest. 115:1627. 7. Moore, D. D. (2007) Science 316:1436. 8. Ogawa, Y. et al. (2007) Proc. Natl. Acad. Sci. USA 104:7432. 9. Kurosu, H. et. al. (2007) J. Biol. Chem. 282:26687. 10. Lundasen, T. et al. (2007) Biochem. Biophys. Res. Commun. 360:437. 11. Badman, M.K. et al. (2007) Cell Metab. 5:426. 12. Inagaki, T. et al. (2007) Cell Metab. 5:415.