Recombinant Mouse FGF-21 stimulated proliferation in NIH-3T3 mouse embryonic fibroblast cells. The ED50 for this effect is 0.4-2 μg/mL in the presence of Recombinant Mouse Klotho beta (Catalog # 2619-KB)
Measured in a cell proliferation assay using NIH‑3T3 mouse embryonic fibroblast cells. The ED50 for this effect is 0.4-2 μg/mL in the presence of Recombinant Mouse Klotho beta (Catalog # 2619-KB).
Source
Mouse myeloma cell line, NS0-derived mouse FGF-21 protein Tyr30-Ser210
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
20 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
22-25 kDa, reducing conditions
Publications
Read Publications using 8409-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 MOPS, Na2SO4 and EDTA.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse 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. Based on its structure, FGF-21 is further classified into a subfamily of FGFs along with FGF-19 and -23 (1). Mouse FGF-21 is a 210 amino acid (aa) polypeptide that contains a 120 aa core FGF domain and a hydrophobic N-terminus signal sequence. The signal sequence is cleaved to release the soluble 180 aa mature FGF-21 protein (2). At the amino acid sequence level, mature mouse FGF-21 is 81% and 92% identical to mature human and rat FGF-21, respectively. In comparison to other FGF subfamilies, a heparin-binding domain is uniquely absent in FGF-19 subfamily members. Lack of this domain confers endocrine function to FGF-19 members and enables them to freely diffuse within tissues and accumulate in the circulatory system (3, 4). The biological activity of FGF-21 requires binding to Klotho beta , a co-receptor that is in complex with cell surface FGF receptors (FGF R) (5, 6). Binding of FGF-21 to Klotho beta facilitates FGF R activation and autophosphorylation resulting in the initiation of multiple downstream signaling cascades (7, 8). FGF-21 cannot independently bind to FGF Rs, thus its effects are restricted to target tissues that express Klotho beta . FGF-21 functions as a physiological regulator of cellular metabolism, including glucose uptake in adipocytes and cellular sensitivity to insulin. FGF-21 is basally expressed in the pancreas, thymus, and liver, as well as in adipose tissue (3, 9). Local and systemic metabolic stress has been shown to induce expression of FGF-21 in the liver, muscles, and fat (10-12). Modulation of FGF-21 expression is associated with a number of metabolic disorders, including obesity and diabetes (7, 13). FGF-21 is also involved in promoting cell survival and proliferation, modulating mesenchymal stem cell differentiation, regulating circadian rhythm, and controlling reproductive capacity during nutrient deprivation (14-18).
Itoh, N. and D.M. Ornitz (2004) Trends Genet. 20:563.
Nishimura, T. et al. (2000) Biochim. Biophys. Acta 1492:203.
Adams, A.C. et al. (2013) Mol. Metab. 2:205.
Goetz, R. et al. (2007) Mol. Cell. Biol. 27:3417.
Suzuki, M. et al. (2008) Mol. Endocrinol. 22:1006.
Kurosu, H. et al. (2007) J. Biol. Chem. 282:26687.
Gimeno, R.E. and D.E. Moller (2014) Trends Endocrinol. Metab. 25:303.
Ogawa, Y. et al. (2007) Proc. Natl. Acad. Sci. U S A 104:7432.
Kharitonenkov, A. et al. (2005) J. Clin. Invest. 115:1627.
Luo, Y. and W.L. McKeehan (2013) Front. Endocrinol. (Lausanne) 4:194.
Yang, C. et al. (2013) BMC Gastroenterol. 13:67.
Keipert, S. et al. (2014) Am. J. Physiol. Endocrinol. Metab. 306:E469.
Zhang, X. et al. (2008) Diabetes 57:1246.
Wei, W. et al. (2012) Proc. Natl. Acad. Sci. USA 109:3143.
Wei, W. et al. (2010) Cell. Metab. 11:503.
Wan, Y. (2013) Int. J. Biochem. Cell. Biol. 45:546.
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