Recombinant Human FGF-9 (HEK293-expressed) Protein, CF

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 1.00-5.00 ng/mL.

2 μg/lane of Recombinant Human FGF-9 (HEK293-expressed) Protein (Catalog # 11233-F9) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 23-30 kDa.

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

Recombinant Human FGF-9 (HEK293-expressed) Protein, CF 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 1.00-5.00 ng/mL.
• Source: Human embryonic kidney cell, HEK293-derived human FGF-9 protein
  Ala2-Ser208 & Leu4-Ser208
• Accession #: P31371.3
• N-terminal Sequence: Ala2 & Leu4
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• 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: 23-30 kDa, under 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 Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 250 μg/mL in sterile water.

Notes

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

Alternate Names for Recombinant Human FGF-9 (HEK293-expressed) Protein, CF

• 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.

Publications for FGF-9 (11233-F9)(1)

Publication using 11233-F9

• Maylem, ERS;Spicer, LJ;Batalha, IM;Sch�tz, LF; Developmental and hormonal regulation of FBN1 and OR4M1 mRNA in bovine granulosa cells Domestic animal endocrinology 2023-04-25 [PMID: 37167929] (Bioassay, Bovine)

Bioinformatics

• Uniprot:
  • P31371.3()