Recombinant Human FGF-21 (Catalog # 2539-FG/CF) stimulates cell proliferation of the BaF3 mouse pro-B cell line transfected with human FGF RIIIc. The ED50 for this effect is 0.06-0.4 μg/mL in the presence of ...read more
1 μg/lane of Recombinant Human FGF-21 was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 24 kDa.
Measured in a cell proliferation assay using BaF3 mouse pro‑B cells transfected with human FGF RIIIc. The ED50 for this effect is 0.06-0.4 µg/mL in the presence of Recombinant Mouse Klotho beta (Catalog # 2619-KB).
Source
E. coli-derived human FGF-21 protein His29-Ser209, with a N-terminal 5-His tag
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
20.2 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
24 kDa, reducing conditions
Publications
Read Publications using 2539-FG/CF in the following applications:
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in MES, Na2SO4, EDTA and DTT.
Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human FGF-21 Protein, CF
FGF21
FGF-21
fibroblast growth factor 21
Background
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 beta -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 show 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 beta -hydroxybutyrate), released, and transported to peripheral tissues for TCA processing and energy generation (11, 12).
Itoh, N. and D.M. Ornitz (2004) Trends Genet. 20:563.
Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
Huang, X. et al. (2006) Mol. Carcinog. 45:934.
Nishimura, T. et al. (2000) Biochim. Biophys. Acta 1492:203.
GenBank Accession #: EAW52401 (2006).
Ford, A.M. et al. (2005) J. Clin. Invest. 115:1627.
Moore, D. D. (2007) Science 316:1436.
Ogawa, Y. et al. (2007) Proc. Natl. Acad. Sci. USA 104:7432.
Kurosu, H. et. al. (2007) J. Biol. Chem. 282:26687.
Lundasen, T. et al. (2007) Biochem. Biophys. Res. Commun. 360:437.
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