>95%, 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 by its binding ability in a functional ELISA. When 2 μg/mL (100 μL/well) of Recombinant Human (rh) Klotho beta was immobilized onto a Ms x hKlotho beta coated plate, the concentration of rhFGF-21 that produces 50% of the optimal binding response was found to be approximately 3-18 ng/mL.
Mouse myeloma cell line, NS0-derived human Klotho beta protein Phe53-Leu997, with a C-terminal 10-His tag
Recombinant Human Klotho beta (Catalog # 5889-KB) binds Recombinant Human FGF‑21 in a functional ELISA. 50% of the optimal binding response for 200 ng/well of recombinant human Klotho beta is observed at approximately 3-18 ng/mL of recombinant human FGF-21.
1 μg/lane of Recombinant Human Klotho beta was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 126 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, 2). Like Klotho, Klotho beta facilitates binding between FGF19 subfamily members and their receptors via formation of a ternary complex (3). The Klotho beta mediated interaction of human FGF19 (mouse FGF15) 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) (2-5). Klotho beta is also a cofactor for the interaction of FGF21 with FGF Receptor 1c in adipocytes, which allows FGF21 to stimulate GLUT1 expression, upregulating adipocyte insulin-dependent glucose uptake (2-4, 6). 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, 7). However, glucuronidase activity has since been demonstrated for Klotho, indicating that physiologically relevant enzymatic activity for Klotho beta is also possible (8). The extracellular domain shares 79%, 87%, 87% and 67% identity with mouse, equine, canine and rat Klotho beta, respectively. The low identity with rat reflects aa discordance within rodent ECD.
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Ogawa, Y. et al. (2007) Proc. Natl. Acad. Sci USA 104:7432.
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