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- Regulatory Status
- RUO
- Other Names
- Fibroblast Growth Factor-9, Glia-activating factor (GAF), Heparin-binding growth factor 9 (HBGF-9)
- Ave. Rating
- Submit a Review
- Product Citations
- publications
| Cat # | Size | Price | Save |
|---|---|---|---|
| 710604 | 20 µg | ¥50,350 |
This product is not available for shipping outside of the United States.
Select size of product is eligible for a 40% discount! Promotion valid until December 31, 2024. Exclusions apply. To view full promotion terms and conditions or to contact your local BioLegend representative to receive a quote, visit our webpage.
FGF-9 is a heparin-binding growth factor belonging to the fibroblast growth factor (FGF) family. FGF-9 was first identified as a secretory protein from the human glioma cell line NMC-G1 and is reported to be widely expressed in rat brain. In the central nervous system, FGF-9 acts as an autocrine and a paracrine growth factor that is required for the development, growth, and survival of neuronal cells. During prenatal stages, FGF-9 expression is crucial for normal lung and airway development. FGF-9 null mutant mice show the phenotype of severe lung hypoplasia, which results in perinatal death. FGF-9 is key in stimulating cell proliferation after arterial, skeletal, and hepatic injuries. FGF-9 is also involved in tumorgenesis, enhancing transformation and progression of several malignant diseases, including prostate, lung, and colon cancer.
Product DetailsProduct Details
- Source
- Human FGF-9, amino acids (Pro3 - Ser208) (Accession# NP_002001.1), was expressed in E. coli.
- Molecular Mass
- The 206 amino acid recombinant protein has a predicted molecular mass of approximately 23.2 kD. The predicted N-terminal amino acid is Pro.
- Purity
- >95%, as determined by Coomassie stained SDS-PAGE gel and HLPC analysis.
- Formulation
- Lyophilized, carrier-free.
- Endotoxin Level
- Less than 0.1 ng per µg of protein.
- Concentration
- This product is bottled at the concentration indicated on the vial.
- Storage & Handling
- Unopened vial can be stored at -20°C or -70°C. For maximum results, quick spin vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. It is recommended to further dilute in a buffer, such as 5% Trehalose, and store working aliquots at -20°C to -80°C. Avoid repeated freeze/thaw cycles.
- Activity
- ED50 ≤ 0.5 ng/ml, corresponding to a specific activity of ≥ 2.0 x 106 units/mg, as measured by its ability to stimulate thymidine uptake by BaF3 cells expressing FGF receptors in a dose dependent manner.
- Application
-
Bioassay
- Application Notes
-
This product is reactive with human and mouse.
Antigen Details
- Structure
- Growth factor
- Distribution
-
FGF-9 is a secreted protein, widely expressed in central nervous system. FGF-9 is expressed in lung mesothelium and epithelium during organogenesis.
- Function
- FGF-9 is a growth factor and is involved in embryonic development, cell growth, cell differentiation, cell migration, and carcinogenesis. FGF-9 is required for the development of glial cells in nervous system.
- Interaction
- FGF-9 targets glial cells in nervous system.
- Ligand/Receptor
- FGFR1-IIIc, FGFR2-IIIc, FGFR3-IIIb, FGFR3-IIIc, and FGFR4.
- Bioactivity
- Human FGF-9 is able to induce proliferation of BaF3 cells expression FGFR.
- Cell Type
- Neural Stem Cells, Mesenchymal Stem Cells, Hematopoietic stem and progenitors, Embryonic Stem Cells
- Biology Area
- Angiogenesis, Cell Biology, Cell Cycle/DNA Replication, Cell Motility/Cytoskeleton/Structure, Neuroscience, Stem Cells, Synaptic Biology
- Molecular Family
- Growth Factors, Cytokines/Chemokines
- Antigen References
-
1. Reuss B, et al. 2003. Cell Tissue Res. 313:139.
2. Tsai SJ, et al. 2002. Endocrinology. 143:2715.
3. White AC, et al. 2006. Development. 133:1507.
4. Workalemahu G, 2004. J. Leukoc. Biol. 75:657.
5. Teishima J, 2014. Anticancer Res. 34:695.
6. Behr B, 2010. Proc. Natl. Acad. Sci. USA. 107:11853. - Gene ID
- 2254 View all products for this Gene ID
- UniProt
- View information about FGF-9 on UniProt.org
Related FAQs
- Why choose BioLegend recombinant proteins?
-
• Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
• Greater than 95% Purity or higher, tested on every lot of product.
• 100% Satisfaction Guarantee for quality performance, stability, and consistency.
• Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
• Bulk and customization available. Contact us.
• Learn more about our Recombinant Proteins. - 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.
- Have your recombinants been tested for stability?
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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.
- Does specific activity of a recombinant protein vary between lots?
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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.
- How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
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Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)
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