Human FGF-23 Antibody Summary
Accession # Q9GZV9
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Cell Proliferation Induced by FGF‑23 and Neutralization by Human FGF‑23 Antibody. In the presence of Recombinant Mouse Klotho (5 µg/mL, Catalog # 1819-KL) and heparin (10 µg/mL), Recombinant Human FGF‑23 (Catalog # 2604-FG) stimulates proliferation in the NIH‑3T3 mouse embryonic fibroblast cell line in a dose-dependent manner (orange line). Under these conditions, proliferation elicited by Recombinant Human FGF‑23 (1 µg/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human FGF‑23 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2604). The ND50 is typically 5‑15 µg/mL.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Fibroblast growth factor 23 (FGF-23) is a 30-32 kDa member of the FGF family, within a subfamily that also includes FGF-19 and FGF-21. FGF proteins contain a 120 amino acid (aa) core FGF domain that exhibits a beta -trefoil structure (1, 2). FGF-19 subfamily members are highly diffusible molecules owing to their poor ECM/heparin sulfate binding and plasma-stabilizing intramolecular folds (2-4). Mature human FGF-23 contains an atypical (very low affinity) heparin binding site (aa 134‑162), a proteolytic cleavage site (Arg179-Ser180), and multiple O-linked glycosylation sites with Thr178 being of particular importance (4-7). O-linked glycosylation at Thr178 blocks the cleavage of FGF-23, thereby preventing loss of FGF-23 activity (7, 8). Mature human FGF-23 shows 72% aa identity to mouse FGF-23 and is active on mouse cells (6). FGF-23 exerts its effects through a ternary complex that includes Klotho and an FGF receptor (FGF R4 or the "c" isoforms of FGF R1 or FGF R3). Klotho has a restricted distribution that limits FGF-23 activity (9-11). FGF-23 is produced by osteocytes and osteoblasts in response to high circulating phosphate levels, elevated parathyroid hormone, and circulatory volume loading. It functions as an endocrine phosphatonin by suppressing circulating phosphate levels (12). FGF-23 interaction with renal proximal tubular epithelium decreases the renal resorption of phosphate by downregulating phosphate transporters and by suppressing vitamin D production. It also decreases the intestinal absorption of phosphate (13).
- Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
- Fukumoto, S. (2007) Endocr. J. Sep 14; [Epub ahead of print].
- Goetz, R. et al. (2007) Mol. Cell. Biol. 27:3417.
- Harmer, N.J. et al. (2004) Biochemistry 43:629.
- Yamashita, T. et al. (2000) Biochem. Biophys. Res. Commun. 277:494.
- Shimada, T. et al. (2001) Proc. Natl. Acad. Sci. USA 98:6500.
- Frishberg, Y. et al. (2007) J. Bone Miner. Res. 22:235.
- Kato, K. et al. (2006) J. Biol. Chem. 281:18370.
- Zhang, X. et al. (2006) J. Biol. Chem. 281:15694.
- Urakawa, I. et al. (2006) Nature 444:770.
- Kurosu, H. et al. (2006) J. Biol. Chem. 281:6120.
- Razzaque, M.S. and B. Lanske (2007) J. Endocrinol. 194:1.
- Kurosu, H. et. al. (2007) J. Biol. Chem. 282:26687.
Citations for Human FGF-23 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 3
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FGF23 is synthesised locally by renal tubules and activates injury-primed fibroblasts
Authors: ER Smith, SJ Tan, SG Holt, TD Hewitson
Sci Rep, 2017;7(1):3345.
Sample Types: Whole Cells
FGF23 is endogenously phosphorylated in bone cells.
Authors: Lindberg I, Pang H, Stains J, Clark D, Yang A, Bonewald L, Li K
J Bone Miner Res, 2015;30(3):449-54.
Sample Types: Cell Culture Supernates
FGF23 neutralization improves chronic kidney disease-associated hyperparathyroidism yet increases mortality.
Authors: Shalhoub V, Shatzen EM, Ward SC
J. Clin. Invest., 2012;122(7):2543-53.
Sample Types: In Vivo
Applications: In Vivo
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