>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 Recombinant Human Glypican 4 Fc Chimera is coated at 500 ng/mL (100 μL/well), the concentration of recombinant human FGF basic that produces 50% of the optimal binding response is 0.75-4.5 ng/mL.
Chinese Hamster Ovary cell line, CHO-derived
Human Glypican 4 (Ala23-Ser529) Accession # O75487
When Recombinant Human Glypican 4 Fc Chimera (Catalog # 9195-GP) is coated at500 ng/mL 100 μL/well), the concentration of Recombinant Human FGF basic 146 aa (Catalog # 233-FB) thatproduces 50% of the optimal binding response is 0.75-4.5 ng/mL.
Background: Glypican 4
Glypican 4, also known as K-Glypican, is an approximately 220 kDa GPI-anchored heparan sulfate proteoglycan with a 60 kDa protein core (1, 2). It is expressed in brain, kidney, adrenal gland, and fat tissue (1, 3) and binds to basic FGF (2). Mature human Glypican 4 shares 97% and 96% amino acid (aa) sequence identity with mouse and rat Glypican 4, respectively. An alternative splice isoform lacks the N-terminal 70 aa including the signal peptide. In the developing brain, Glypican 4 is found in lateral ventricles surrounding the telencephalon, the dentate gyrus, proliferating neuroepithelial cells, and neural precursors (1, 2). It inhibits the dopaminergic differentiation of neurons (4). A 30 kDa cleaved form of Glypican 4 binds in cis to PTP sigma and contributes to excitatory synapse development and function (5). Glypican 4 is differentially expressed between adipose tissue depots (3). A soluble form can be released by adipocytes and circulates at elevated levels in obese patients with insulin resistance (3, 6). This form binds and enhances signaling through the Insulin R, and it also supports adipocyte differentiation (3). In zebrafish, Glypican 4 is required for cartilage formation and cardiomyocyte differentiation (7, 8).
Watanabe, K. et al. (1995) J. Cell Biol. 130:1207.
Hagihara, K. et al. (2000) Dev. Dyn. 219:353.
Ussar, S. et al. (2012) Diabetes 61:2289.
Fico, A. et al. (2014) J. Neurosci. 34:8318.
Ko, J.S. et al. (2015) Proc. Natl. Acad. Sci. USA 112:1874.
Zhu, H.J. et al. (2014) J. Endocrinol. Metab. 99:E2697.
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