Recombinant Human FGF-9, Animal-Free Protein

FGF-9 activity is determined using the Promega serum response element luciferase reporter assay (*) in transfected HEK293T cells. Cells are treated in triplicate with a serial dilution of FGF-9 for 3 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. EC50 = 5.7 ng/ml (0.25 nM).*Promega pGL4.33[luc2P/SRE/Hygro] #E1340

FGF-9 protein migrates as a single band at 23 kDa in non-reducing (NR) conditions and upon reduction (R). No contaminating protein bands are visible. Purified recombinant protein (3 µg) was resolved using 15% w/v SDS-PAGE in reduced (+ beta -mercaptothanol, R) and non-reduced (NR) conditions and stained with Coomassie Brilliant Blue R250.

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

Recombinant Human FGF-9, Animal-Free Protein Summary

• Details of Functionality: No significant difference between EC₅₀ of reference and test lots
• Source: E. coli-derived human FGF-9 protein
• Accession #: P31371.3
• Protein/Peptide Type: Animal-Free Recombinant Proteins
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• 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.
• SDS-PAGE: Monomeric FGF-9 protein only

Packaging, Storage & Formulations

• Storage: Store lyophilized protein between -20 and -80 °C until the date of expiry. Avoid freeze-thaw cycles.
• Buffer: Lyophilized from HEPES/NaCl
• Reconstitution Instructions: Resuspend in water at >100 µg/ml, prepare single use aliquots, add carrier protein if desired.

Notes

The above product was manufactured, tested and released by R&D System's contract manufacturer, Qkine Ltd, at 1 Murdoch House, Cambridge, UK, CB5 8HW. The product is for research use only and not for the diagnostic or theraputic use.

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

Alternate Names for Recombinant Human FGF-9, Animal-Free 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

Fibroblast growth factor 9 (FGF-9), also known as HBGF9 and GAF, is a member of the FGF family of secreted glycoproteins involved in mammalian skeleton morphogenesis and growth (1). The FGF family is characterized by a core heparin-binding FGF domain of approximately 120 amino acids (aa) that exhibits a beta -trefoil structure (2). Mature mouse FGF-9 shares 99% and 100% aa sequence identity with human and rat FGF-9, respectively. FGF-9, along with FGF-16 and -20, form a FGF subfamily that shares 65-71% aa sequence identity, binds FGFR3(IIIb), and are efficiently secreted despite having an uncleavable, bipartite signal sequence (2-4). In addition to FGFR3(IIIb), FGF-9 binding to the IIIc splice forms of FGFR-1, -2 and -3 have been reported (1,4,6). 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 (2, 6-11). Deletion of mouse FGF-9 is lethal at birth due to lung hypoplasia, and causes rhizomelia, or shortening of the proximal skeleton (2,10,11). Additionally, a mutation in mouse FGF-9 is responsible for Elbow knee synostosis (Eks), which causes joint fusions in the elbow and knee (6). In humans, FGF9 mutations that lower receptor binding can result multiple synostoses syndrome (SYNS) (7). Altered FGF-9 expression or function is reported in human colon, endometrial, and ovarian cancers, correlating with progression, invasiveness, and survival (12-15).

1. Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
2. Itoh, N. and D.M. Ornitz (2008) Dev. Dyn. 237:18.
3. Miyamoto, M. et al. (1993) Mol. Cell. Biol. 13:4251.
4. Santos-Ocampo, S. et al. (1996) J. Biol. Chem. 271:1726.
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.

Bioinformatics

• Uniprot:
  • P31371.3()