- Other Names
- Fibroblast Growth Factor 9, Glia-Activating Factor (GAF), Heparin-Binding Growth Factor 9 (HBGF-9), HBFG-9, SYNS3
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- Product Citations
FGF-9 is a member of the fibroblast growth factor family. It is a potent mitogen and can stimulate proliferation and invasion capacity of epithelial cells. FGF-9 also plays an important role in lung development and maintenance in the adult organ. FGF-9 is expressed in the lung mesothelium and epithelium. FGF-9 regulates lung branching by stimulating mesenchymal proliferation and inducing FGF-10 expression in the mesenchyme. FGF-9 deficient mice exhibit severely impaired lung development and die in the perinatal period. FGF-9 deficient mice also exhibit other phenotypes including testicular hypoplasia and male-to-female sex reversion. Additional studies have shown that FGF-9 is required for normal sex determination by maintaining SOX9 expression. FGF-9 also regulates testosterone production in the mouse Leydig cell through AKT and MAPK signaling pathways. FGF-9 can be detected in the central nervous system and promotes the differentiation and survival of both neurons and glia cells. FGF-9 also regulates gap-junction formation in cultured astroglial cells. FGF-9 is also involved in bone formation, retinal differentiation and maturation, wound healing, and maintaining the stemness of kidney nephron progenitors. Expression of FGF-9 can be transcriptionally induced by prostaglandin E2, estrogen, and hypoxia. It has been shown that FGF-9 can form dimers and the dimeric FGF-9 binds to heparin with a higher affinity than the monomeric FGF-9. Overexpression of FGF-9 has been associated with many human cancers such as ovarian endometrioid adenocarcinomas, glioma, prostate cancer, and endometriosis.Product Details
- Human FGF-9, amino acids (Met1-Ser208) (Accession# NP_002001.1), was expressed in E. coli.
- Molecular Mass
- The 208 amino acid recombinant protein has a predicted molecular mass of approximately 23 kD. The DTT-reduced and non-reduced protein migrate at approximately 23 kD by SDS-PAGE. The predicted N-terminal amino acid is Met.
- >95%, as determined by Coomassie stained SDS-PAGE.
- 0.22 µm filtered protein solution is in 20 mM Tris, pH 8.0, 10% glycerol, 100 mM NaCl, and 1% CHAPS.
- Endotoxin Level
- Less than 0.01 ng per µg cytokine as determined by the LAL method.
- 10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial (please contact technical support for concentration, or use our Lookup tool if you have a lot number.) Please note, new lots of the 100 µg size will be lot-specific and may differ from previous lots that had a fixed concentration.
- Storage & Handling
- Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
- The ED50 is 0.2 - 1.0 ng/ml, corresponding to a specific activity of 1.0 - 5.0 x 106 units/mg, as determined by a dose-dependent stimulation of NIH3T3 cell proliferation without heparin added to the culture.
- Application Notes
BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are verified in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at email@example.com.
- Growth factor.
Expression of FGF-9 has been reported in lung, Î³δ T cells, central nervous systems, the epithelium of tooth germs, and the prostate epithelium.
- FGF-9 is involved in embryonic development and many biological functions at adulthood. FGF-9 is induced by PGE2.
- Leydig cells, intestinal mesenchymal stem cells, lung mesenchymal cells, cranial mesenchymal cells, glial cells, fibroblasts, and epithelial cells.
- FGF-9 binds and activates the IIIc isoforms of FGFR1, FGFR2, and FGFR3 and the IIIb isoform of FGFR3.
- Cell Type
- Embryonic Stem Cells, Hematopoietic stem and progenitors, Mesenchymal Stem Cells, Neural Stem Cells
- Biology Area
- Cell Biology, Neuroscience, Stem Cells, Synaptic Biology
- Molecular Family
- Cytokines/Chemokines, Growth Factors
- Antigen References
1. Hendrix ND, et al. 2006. Cancer Res. 66:1354.
2. Colvin JS, et al. 2001. Cell 104:875.
3. Colvin JS, et al. 2001. Development 128:2095.
4. Zhang X, et al. 2006. J. Biol. Chem. 281:15694.
5. Gay D, et al. 2013. Nat. Med. 7:916.
6. Harada M, et al. 2009. Nat. Genet. 41:289.
7. Lai MS, et al. 2014. PLoS One 9:e90243.
8. Barak H, et al. 2012. Dev. Cell 22:1191.
9. Santos-Ocampo S, et al. 1996. J. Biol. Chem. 271:1726.
10. Geske M, et al. 2008. Development 135:2959.
- Gene ID
- 2254 View all products for this Gene ID
- View information about FGF-9 on UniProt.org
- Does specific activity of a recombinant protein vary between lots?
Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.
- Have your recombinants been tested for stability?
Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.
- How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
- Use formula Specific activity (Units/mg) = 10e6/ ED50 (ng/mL)
- How does the activity of your recombinant proteins compare to competitors?
We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!
- What is the specific activity or ED50 of my recombinant protein?
The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.