Recombinant Human FGF-9 Protein


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Recombinant Human FGF-9 Protein Summary

Details of Functionality
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. Rubin, J.S. et al. (1991) Proc. Natl. Acad. Sci. USA 88:415. The ED50 for this effect is 1-5 ng/mL.
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human FGF-9 protein
Met1-Ser208 & Ala2-Ser208
Accession #
N-terminal Sequence
Met1 & Ala2
Protein/Peptide Type
Recombinant Proteins
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.


Theoretical MW
23 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.
Multiple bands between 22-29 kDa, reducing conditions
Read Publications using
273-F9 in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4 and EDTA with BSA as a carrier protein.
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.


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

Alternate Names for Recombinant Human FGF-9 Protein

  • FGF9
  • FGF-9
  • fibroblast growth factor 9 (glia-activating factor)
  • Fibroblast growth factor 9
  • GAF
  • glia-activating factor
  • HBFG-9
  • HBGF-9
  • Heparin-binding growth factor 9
  • MGC119914
  • MGC119915
  • SYNS3


FGF-9 (fibroblast growth factor-9), also called HBGF-9 (heparin-binding growth factor-9) and GAF (glia-activating factor), is an approximately 26 kDa secreted glycoprotein of the FGF family (1-3). FGFs exhibit heparin-dependent regulation of cell proliferation, differentiation, and function, and are characterized by a core heparin-binding FGF domain of approximately 120 amino acids (aa) that exhibits a beta -trefoil structure (1). FGF-9, -16 and -20 form a subfamily that shares 65-71% aa sequence identity, binds FGF R3 (IIIb), and are efficiently secreted despite having an uncleavable, bipartite signal sequence (1-3). Secreted human FGF-9 is a
205-207 aa protein that lacks the N-terminal 1-3 aa and shares 98% sequence identity with mouse, rat, equine, porcine and bovine FGF-9. In addition to FGF R3 (IIIb), FGF-9 binding to the IIIc splice forms of FGF R1, R2 and R3 are variably reported (3-5). An unusual constitutive dimerization of FGF-9 buries receptor interaction sites which lowers its activity, and increases heparin affinity which inhibits diffusion (4-6). A spontaneous mouse mutant, Eks, interferes with dimerization, resulting monomeric, diffusible FGF-9 that causes elbow and knee synostoses (joint fusions) due to FGF-9 misexpression in developing joints (6). In humans, FGF-9 mutations that lower receptor binding cause multiple synostoses syndrome (SYNS) (7). Expression in brain and kidney are reported in the adult rat (2, 8). In the mouse embryo the location and timing of FGF-9 expression affects development of the skeleton, cerebellum, lungs, heart, vasculature, digestive tract, and testes (1, 6-11). Deletion of mouse FGF-9 is lethal at birth due to lung hypoplasia, and causes rhizomelia, or shortening of the proximal skeleton (1, 10, 11). Altered FGF-9 expression or function is reported in human colon, endometrial, and ovarian cancers, correlating with progression, invasiveness, and survival (12-15).

  1. Itoh, N. and D.M. Ornitz (2008) Dev. Dyn. 237:18.
  2. Miyamoto, M. et al. (1993) Mol. Cell. Biol. 13:4251.
  3. Santos-Ocampo, S. et al. (1996) J. Biol. Chem. 271:1726.
  4. Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
  5. Plotnikov, A.N. et al. (2001) J. Biol. Chem. 276:4322.
  6. Harada, M. et al. (2009) Nat. Genet. 41:289.
  7. Wu, X.L. et al. (2009) Am. J. Hum. Genet. 85:53.
  8. Colvin, J.S. et al. (1999) Dev. Dyn. 216:72.
  9. Lin, Y. et al. (2009) Dev. Biol. 329:44.
  10. Hung, I.H. et al. (2007) Dev. Biol. 307:300.
  11. Colvin, J.S. et al. (2001) Dev. Dyn 128:2095.
  12. Krejci, P. et al. (2009) Hum. Mutat. 30:1245.
  13. Leushacke, M. et al. (2011) PLoS ONE 6:e23381.
  14. Hendrix, N.D. et al. (2006) Cancer Res. 66:1354.
  15. Abdel-Rahman, W.M. et al. (2008) Hum. Mutat. 29:390.

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Publications for FGF-9 (273-F9)(24)

We have publications tested in 5 confirmed species: Human, Mouse, Rat, Bovine, Chicken.

We have publications tested in 3 applications: Bioassay, In Vivo, cell culture.

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In Vivo
cell culture
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Showing Publications 1 - 10 of 24. Show All 24 Publications.
Publications using 273-F9 Applications Species
WKW Ho, L Freem, D Zhao, KJ Painter, TE Woolley, EA Gaffney, MJ McGrew, A Tzika, MC Milinkovit, P Schneider, A Drusko, F Matthäus, JD Glover, KL Wells, JA Johansson, MG Davey, HM Sang, M Clinton, DJ Headon Feather arrays are patterned by interacting signalling and cell density waves PLoS Biol., 2019;17(2):e3000132. 2019 [PMID: 30789897] (Bioassay, Chicken) Bioassay Chicken
H Wu, K Uchimura, EL Donnelly, Y Kirita, SA Morris, BD Humphreys Comparative Analysis and Refinement of Human PSC-Derived Kidney Organoid Differentiation with Single-Cell Transcriptomics Cell Stem Cell, 2018;0(0):. 2018 [PMID: 30449713] (Bioassay, Human) Bioassay Human
CW van den Be, L Ritsma, MC Avramut, LE Wiersma, BM van den Be, DG Leuning, E Lievers, M Koning, JM Vanslambro, AJ Koster, SE Howden, M Takasato, MH Little, TJ Rabelink Renal Subcapsular Transplantation of PSC-Derived Kidney Organoids Induces Neo-vasculogenesis and Significant Glomerular and Tubular Maturation In�Vivo Stem Cell Reports, 2018;0(0):. 2018 [PMID: 29503086] (Bioassay, Human) Bioassay Human
KE Tumelty, N Higginson-, X Fan, P Bajaj, KM Knowlton, M Shamashkin, AJ Coyle, W Lu, SP Berasi Identification of direct negative crosstalk between the SLIT2 and Bone Morphogenetic Protein-Gremlin signaling pathways J. Biol. Chem., 2018;0(0):. 2018 [PMID: 29317497] (Bioassay, Human) Bioassay Human
A Taguchi, R Nishinakam Higher-Order Kidney Organogenesis from Pluripotent Stem Cells Cell Stem Cell, 2017;0(0):. 2017 [PMID: 29129523] (Bioassay, Human) Bioassay Human
R Doi, T Tsuchiya, N Mitsutake, S Nishimura, M Matsuu-Mat, Y Nakazawa, T Ogi, S Akita, H Yukawa, Y Baba, N Yamasaki, K Matsumoto, T Miyazaki, R Kamohara, G Hatachi, H Sengyoku, H Watanabe, T Obata, LE Niklason, T Nagayasu Transplantation of bioengineered rat lungs recellularized with endothelial and adipose-derived stromal cells Sci Rep, 2017;7(1):8447. 2017 [PMID: 28814761] (Bioassay, Rat) Bioassay Rat
JD Glover, KL Wells, F Matthäus, KJ Painter, W Ho, J Riddell, JA Johansson, MJ Ford, CAB Jahoda, V Klika, RL Mort, DJ Headon Hierarchical patterning modes orchestrate hair follicle morphogenesis PLoS Biol., 2017;15(7):e2002117. 2017 [PMID: 28700594] (Bioassay, Mouse) Bioassay Mouse
N Pode-Shakk, R Gershon, G Tam, D Omer, Y Gnatek, I Kanter, S Oriel, G Katz, O Harari-Ste, T Kalisky, B Dekel Evidence of In�Vitro Preservation of Human Nephrogenesis at the Single-Cell Level Stem Cell Reports, 2017;0(0):. 2017 [PMID: 28552604] (Bioassay, Human) Bioassay Human
E El Agha, V Kheirollah, A Moiseenko, W Seeger, S Bellusci Ex vivo analysis of the contribution of FGF10(+) cells to airway smooth muscle cell formation during early lung development Dev. Dyn., 2017;0(0):. 2017 [PMID: 28387977] (Bioassay, Mouse) Bioassay Mouse
Generation of nephron progenitor cells and kidney organoids from human pluripotent stem cells Nat Protoc, 2017;12(1):195-207. 2017 [PMID: 28005067] (Bioassay, Human) Bioassay Human
Show All 24 Publications.

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Gene Symbol FGF9