>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
Measured in a cell proliferation assay using BaF3 mouse pro‑B cells transfected with human FGF RIIIc. The ED50 for this effect is 0.2-1 µg/mL in the presence of
Recombinant Human FGF-21 (Catalog # 2539-FG) and Heparin.
Mouse myeloma cell line, NS0-derived mouse Klotho beta protein Phe53-Leu995, with a C-terminal 10-His tag
Recombinant Mouse Klotho beta (Catalog # 2619-KB) stimulates cell proliferation of the BaF3 mouse pro-B cell line transfected with human FGF RIIIc. The ED50 for this effect is 0.2-1 μg/mL in the presence of Recombinant Human FGF‑21 (Catalog # 2539-FG) and Heparin.
1 μg/lane of Recombinant Mouse Klotho beta was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a band at 135 kDa.
Background: Klotho beta
Klotho beta, a divergent structural member of the glycosidase I superfamily, is expressed primarily in the liver and pancreas, with lower expression in adipose tissue (1). Like Klotho, Klotho beta facilitates binding between FGF-19 subfamily members and their receptors via formation of a ternary complex (2). The Klotho beta mediated interaction of FGF-15 (human FGF-19) with FGF Receptor 4 in the liver negatively regulates bile acid synthesis by controlling the secretion of two key bile acid synthase genes, cholesterol 7-alpha hydroxylase (Cyp7a1) and sterol 12-alpha hydroxylase (Cyp8b1) (2-4). Klotho beta is also a cofactor for the interaction of FGF-21 with FGF Receptor 1c in adipocytes, which allows FGF-21 to stimulate GLUT1 expression, up-regulating adipocyte insulin-dependent glucose uptake (2-3, 5). The 1043 amino acid (aa) type I transmembrane protein is composed of a 51 aa signal sequence, a 943 aa extracellular domain (ECD) containing two glycosidase-like regions, a 21 aa transmembrane domain, and 28 aa intracellular tail. Since Klotho-related proteins lack critical active site Glu residues present in beta -glycosidases, it was initially unclear whether they were functional enzymes (1, 6). However, glucuronidase activity has since been demonstrated for Klotho, indicating that physiologically relevant enzymatic activity for Klotho beta is also possible (7). The extracellular domain shares 79%, 79%, 80% and 67% identity with human, bovine, canine and rat Klotho beta, respectively. The low identity with rat reflects aa discordance within rodent ECD.
Mian, I.S. (1998) Blood Cells Mol. Dis. 24:83.
Ito, S. et al. (2005) J. Clin. Invest. 115:2202.
Kurosu, H. et al. (2007) J. Biol. Chem. 282:26687.
Lin, B. C. et al. (2007) J. Biol. Chem. 282:27277.
Ogawa, Y. et al. (2007) Proc. Natl. Acad. Sci USA 104:7432.
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