Recombinant Human FGF-23 Protein, CF

Recombinant human FGF-23 (2604-FG/CF) induces proliferation in BaF3 mouse pro-B cells transfected with human FGFR3 (IIIc). The ED50 for this effect is 0.1-0.4 μg/mL in the presence of recombinant mouse Klotho (1819-KL) and heparin.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human FGF-23 Protein, CF Summary

• Details of Functionality: Measured in a cell proliferation assay using BaF3 mouse pro‑B cells transfected with human FGF RIIIc. The ED₅₀ for this effect is 0.1‑0.4 µg/mL in the presence of Recombinant Mouse Klotho (Catalog # 1819-KL) and heparin.
• Source: Mouse myeloma cell line, NS0-derived human FGF-23 protein
  Tyr25-Ile251 (Arg179Gln), with a C-terminal 6-His tag
• Accession #: Q9GZV9
• N-terminal Sequence: Tyr25
• Protein/Peptide Type: Recombinant Proteins
• Gene: FGF23
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 26.1 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: 29-34 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, 2 to 8 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in MOPS, Na₂SO₄, EDTA and DTT.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human FGF-23 Protein, CF

• ADHR
• FGF23
• FGF-23
• fibroblast growth factor 23
• HPDR2
• HYPF
• phosphatonin
• PHPTC
• tumor-derived hypophosphatemia inducing factor
• Tumor-derived hypophosphatemia-inducing factor

Background

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 down‑regulating phosphate transporters and by suppressing vitamin D production. It also decreases the intestinal absorption of phosphate (13).

1. Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
2. Fukumoto, S. (2007) Endocr. J. Sep 14; [Epub ahead of print].
3. Goetz, R. et al. (2007) Mol. Cell. Biol. 27:3417.
4. Harmer, N.J. et al. (2004) Biochemistry 43:629.
5. Yamashita, T. et al. (2000) Biochem. Biophys. Res. Commun. 277:494.
6. Shimada, T. et al. (2001) Proc. Natl. Acad. Sci. USA 98:6500.
7. Frishberg, Y. et al. (2007) J. Bone Miner. Res. 22:235.
8. Kato, K. et al. (2006) J. Biol. Chem. 281:18370.
9. Zhang, X. et al. (2006) J. Biol. Chem. 281:15694.
10. Urakawa, I. et al. (2006) Nature 444:770.
11. Kurosu, H. et al. (2006) J. Biol. Chem. 281:6120.
12. Razzaque, M.S. and B. Lanske (2007) J. Endocrinol. 194:1.
13. Kurosu, H. et. al. (2007) J. Biol. Chem. 282:26687.

Publications for FGF-23 (2604-FG/CF)(16)

Publications using 2604-FG/CF

• WB Sneddon, PA Friedman, T Mamonova Mutations in an unrecognized internal NPT2A PDZ motif disrupt phosphate transport causing congenital hypophosphatemia bioRxiv : the preprint server for biology, 2023-03-07;0(0):. 2023-03-07 [PMID: 36945373] (Bioassay, Human)
• PA Friedman, WB Sneddon, T Mamonova, C Montanez-M, S Ramineni, NH Harbin, KE Squires, JV Gefter, CE Magyar, DR Emlet, JR Hepler RGS14 regulates hormone-sensitive NPT2A-mediated renal phosphate uptake via binding to the NHERF1 scaffolding protein The Journal of Biological Chemistry, 2022-03-17;0(0):101836. 2022-03-17 [PMID: 35307350] (Bioassay, Human)
• J Heil, V Olsavszky, K Busch, K Klapproth, C de la Torr, C Sticht, K Sandorski, J Hoffmann, H Schönhaber, J Zierow, M Winkler, CD Schmid, T Staniczek, DE Daniels, J Frayne, G Metzgeroth, D Nowak, S Schneider, M Neumaier, V Weyer, C Groden, HJ Gröne, K Richter, C Mogler, MM Taketo, K Schledzews, C Géraud, S Goerdt, PS Koch Bone marrow sinusoidal endothelium controls terminal erythroid differentiation and reticulocyte maturation Nature Communications, 2021-11-29;12(1):6963. 2021-11-29 [PMID: 34845225] (Bioassay, Human)
• X Zhong, S Jagarlapud, Y Weng, M Ly, JC Rouse, K McClure, T Ishino, Y Zhang, E Sousa, J Cohen, B Tzvetkova, K Cote, JJ Scarcelli, K Johnson, J Palandra, JR Apgar, S Yaddanapud, RG Villalobos, AC Opsahl, K Lam, Q Yao, W Duan, A Sievers, J Zhou, D Ferguson, A D'Antona, R Zollner, HL Zhu, R Kriz, L Lin, V Clerin Structure-function relationships of the soluble form of the antiaging protein Klotho have therapeutic implications for managing kidney disease J. Biol. Chem., 2020-01-31;0(0):. 2020-01-31 [PMID: 32005658] (Cell Culture, Rat)
• I Böckmann, J Lischka, B Richter, J Deppe, A Rahn, DC Fischer, J Heineke, D Haffner, M Leifheit-N FGF23-Mediated Activation of Local RAAS Promotes Cardiac Hypertrophy and Fibrosis Int J Mol Sci, 2019-09-18;20(18):. 2019-09-18 [PMID: 31540546] (Bioassay, Rat)
• M Rodrat, K Wongdee, N Panupinthu, J Thongbunch, J Teerapornp, N Krishnamra, N Charoenpha Prolonged exposure to 1,25(OH)2D3 and high ionized calcium induces FGF-23 production in intestinal epithelium-like Caco-2 monolayer: A local negative feedback for preventing excessive calcium transport Arch. Biochem. Biophys., 2018-01-06;640(0):10-16. 2018-01-06 [PMID: 29317227] (Bioassay, Human)
• K Yang, H Peretz-Sor, J Wu, L Zhu, X Cui, M Zhang, C Rigatto, Y Liu, F Lin Fibroblast growth factor 23 weakens chemotaxis of human blood neutrophils in microfluidic devices Sci Rep, 2017-06-08;7(1):3100. 2017-06-08 [PMID: 28596573] (Bioassay, Human)
• CP Chung, YC Chang, Y Ding, K Lim, Q Liu, L Zhu, W Zhang, TS Lu, G Molostvov, D Zehnder, LL Hsiao ?-Klotho expression determines nitric oxide synthesis in response to FGF-23 in human aortic endothelial cells PLoS ONE, 2017-05-02;12(5):e0176817. 2017-05-02 [PMID: 28463984] (Bioassay, Human)
• Convergent Signaling Pathways Regulate Parathyroid Hormone and Fibroblast Growth Factor-23 Action on NPT2A-mediated Phosphate Transport J Biol Chem, 2016-07-18;0(0):. 2016-07-18 [PMID: 27432882] (Bioassay, Human)
• K van der Me, HW van Essen, FW Bloemers, EA Schulten, P Lips, N Bravenboer Regulation of CYP27B1 mRNA Expression in Primary Human Osteoblasts Calcif Tissue Int, 2016-03-25;0(0):. 2016-03-25 [PMID: 27016371] (Bioassay, Human)
• Six I, Okazaki H, Gross P, Cagnard J, Boudot C, Maizel J, Drueke T, Massy Z Direct, acute effects of Klotho and FGF23 on vascular smooth muscle and endothelium. PLoS ONE, 2014-04-02;9(4):e93423. 2014-04-02 [PMID: 24695641] (Bioassay, Human)
• Coe , Lindsay, Madathil , Sangeeth, Casu , Carla, Lanske , Beate, Rivella , Stefano, Sitara , Despina FGF-23 is a negative regulator of prenatal and postnatal erythropoiesis. J Biol Chem, 2014-02-07;289(14):9795-810. 2014-02-07 [PMID: 24509850] (Bioassay, In Vivo, Mouse)
• Kharitonenkov , Alexei, Beals , John M, Micanovic , Radmila, Strifler , Beth A, Rathnachalam , Radhakri, Wroblewski , Victor J, Li , Shun, Koester , Anja, Ford , Amy M, Coskun , Tamer, Dunbar , James D, Cheng , Christin, Frye , Christop, Bumol , Thomas F, Moller , David E Rational design of a fibroblast growth factor 21-based clinical candidate, LY2405319. PLoS ONE, 2013-03-11;8(3):e58575. 2013-03-11 [PMID: 23536797] (Bioassay, Human)
• Wu , Ai-Luen, Feng , Bo, Chen , Mark Z, Kolumam , Ganesh, Zavala-Solorio , Jose, Wyatt , Shelby K, Gandham , Vineela, Carano , Richard, Sonoda , Junichir Antibody-mediated activation of FGFR1 induces FGF23 production and hypophosphatemia. PLoS ONE, 2013-02-22;8(2):e57322. 2013-02-22 [PMID: 23451204] (Bioassay, Rat)
• Smith R Circulating alphaKlotho influences phosphate handling by controlling FGF23 production. J. Clin. Invest., 2012-11-26;122(12):4710-5. 2012-11-26 [PMID: 23187128] (Bioassay, Human)
• Tomlinson DC, Knowles MA Altered splicing of FGFR1 is associated with high tumor grade and stage and leads to increased sensitivity to FGF1 in bladder cancer. Am. J. Pathol., 2010-10-01;177(5):2379-86. 2010-10-01 [PMID: 20889570] (Bioassay, Human)

Bioinformatics

• Gene Symbol: FGF23
• Uniprot:
  • Q9GZV9()