Recombinant Mouse FGF-9 Protein

• Reactivity: Mu
• Applications: Bioactivity

Recombinant Mouse 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 1.5‑7.5 ng/mL.
• Source: E. coli-derived mouse FGF-9 protein
  Met1-Ser208
• Accession #: NP_037084
• N-terminal Sequence: Pro3
• Structure / Form: Monomer
• Protein/Peptide Type: Recombinant Proteins
• Gene: Fgf9
• 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: 23.2 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: 24 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.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in MOPS, Na₂SO₄ and EDTA with BSA as a carrier protein.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 250 μg/mL in sterile, deionized water.

Notes

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

Alternate Names for Recombinant Mouse 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

Background

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 mouse FGF-9 is a 205‑207 aa protein that lacks the N-terminal 1-3 aa and shares >98% sequence identity with rat, human, 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.

Publications for FGF-9 (7399-F9)(6)

Publications using 7399-F9

• Xu, M;Thottappillil, N;Cherief, M;Li, Z;Zhu, M;Xing, X;Gomez-Salazar, M;Mwirigi, JM;Sankaranarayanan, I;Tavares-Ferreira, D;Zhang, C;Wang, XW;Archer, M;Guan, Y;Tower, RJ;Cahan, P;Price, TJ;Clemens, TL;James, AW; Mapping Somatosensory Afferent Circuitry to Bone Identifies Neurotrophic Signals Required for Fracture Healing bioRxiv : the preprint server for biology 2024-06-07 [PMID: 38895367] (Bioassay, Mouse)
• K Imura-Kish, A Uchida, N Tsunekawa, H Suzuki, HM Takase, Y Hirate, M Kanai-Azum, R Hiramatsu, M Kurohmaru, Y Kanai Low retinoic acid levels mediate regionalization of the Sertoli valve in the terminal segment of mouse seminiferous tubules Scientific Reports, 2021-01-13;11(1):1110. 2021-01-13 [PMID: 33441739] (Bioassay, Mouse)
• 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., 2017-07-11;15(7):e2002117. 2017-07-11 [PMID: 28700594] (Bioassay, Mouse)
• Wallner C, Schira J, Wagner J, Schulte M, Fischer S, Hirsch T, Richter W, Abraham S, Kneser U, Lehnhardt M, Behr B Application of VEGFA and FGF-9 enhances angiogenesis, osteogenesis and bone remodeling in type 2 diabetic long bone regeneration. PLoS ONE, 2015-03-05;10(3):e0118823. 2015-03-05 [PMID: 25742620] (In Vivo, Mouse)
• Lai , Meng-Sha, Cheng , Yu-Sheng, Chen , Pei-Rong, Tsai , Shaw-Jen, Huang , Bu-Miin Fibroblast growth factor 9 activates akt and MAPK pathways to stimulate steroidogenesis in mouse leydig cells. PLoS ONE, 2014-03-06;9(3):e90243. 2014-03-06 [PMID: 24603862] (Bioassay, Mouse)
• Guo T, Landsman L, Li N, Hebrok M Factors expressed by murine embryonic pancreatic mesenchyme enhance generation of insulin-producing cells from hESCs. Diabetes, 2013-01-10;62(5):1581-92. 2013-01-10 [PMID: 23305648] (Bioassay, Mouse)

Bioinformatics

• Gene Symbol: Fgf9
• Uniprot:
  • NP_037084()