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- Regulatory Status
- RUO
- Other Names
- Fibroblast growth factor 8, FGF8, Androgen-induced growth factor, AIGF, Heparin-binding growth factor 8, HBGF-8
- Ave. Rating
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- Product Citations
- publications
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Recombinant human FGF-8a induces proliferation of BALB/c 3T3 cell in a dose dependent manner with ED50 of 0.1 - 0.4 µg/mL. The Deep Blue Cell Viability™ Kit (Cat. No. 424702) was used measure the number of cells. -
Stability testing for human FGF-8a. Human FGF8-8a was aliquoted in 20 mM Tris, 150 mM Na2SO4, 1 mM EDTA, pH 8, 10% glycerol at 0.2 mg/ml. One aliquot was freeze and thawed four times (4x freeze/thaws), and compared to a control kept at 4°C (control). The samples were tested in BALB/c 3T3 cell proliferation assay.
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FGF-8 belongs to the fibroblast growth factor (FGF) family and plays an important role in cell growth, embryogenesis, and tumorigenesis. Four isoforms of FGF-8 in human (a, b, e, f) and eight isoforms in mouse (a-h) generated by alternative splicing of the mRNA have been described. Comparing human and mouse, FGF-8a and FGF-8b show identical sequence homology. FGF-8b is predominant form and co-expressed with FGF-8a. The isoforms have different biological functions during embryogenesis. During prenatal stages, FGF-8 is required for the normal development of various organs, including limbs and central nervous system. Misexpression of FGF-8a and 8b proteins results in dysregulation of fate determination in developing brain. In addition, FGF-8 was first cloned from SC-3 mouse mammary carcinoma cells and was found to be induced in response to androgenic stimuli. The isoform FGF-8b has the highest affinity to FGF receptors, elucidating the stronger transforming capacity than FGF-8a. FGF-8b is detected in human prostate and breast carcinoma specimens and cell lines. FGF-8f is associated with the prognosis of esophageal carcinomas. FGF-8e mutation is associated with deficiency of gonadotropin-releasing hormone (GnRH).
Product DetailsProduct Details
- Source
- Human FGF-8a, amino acids Gln23 - Arg204 (Accession #: NP_149355), with an N-terminal Met, was expressed in E. coli.
- Molecular Mass
- The 183 amino acid recombinant protein has a predicted molecular mass of approximately 21.3 kD. The DTT-reduced and non-reduced protein migrates at approximately 22 kD respectively by SDS-PAGE. The predicted N-terminal amino acid is Met.
- Formulation
- 0.22 µm filtered protein solution is in 20 mM Tris, 150 mM Na2SO4, 1 mM EDTA, pH 8, 10% glycerol.
- Endotoxin Level
- Less than 0.1 EU per µg protein as determined by the LAL method.
- Preparation
- > 98%, as determined by Coomassie stained SDS-PAGE.
- Concentration
- 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. To obtain lot-specific concentration and expiration, please enter the lot number in our Certificate of Analysis online tool.
- 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.
- Activity
- The ED50 is 0.1 - 0.4 µg/mL, as determined by a dose-dependent stimulation of BALB/c 3T3 cell proliferation in the presence of 10 µg/mL heparin.
- Application
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Bioassay
- Application Notes
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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 tech@biolegend.com.
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Application References
(PubMed link indicates BioLegend citation) -
- Falardeau J, et al. 2008. J. Clin. Invest. 118:2822.
- Turner N, Grose R. 2010. Nat. Rev. Cancer. 10:116.
- Tanaka S, et al. 2001. Dig. Dis. Sci. 46:1016.
- Payson RA, et al. 1996. Oncogene. 13:47.
- Gemel J, et al. 1996. Genomics. 35:253.
- Han MJ, et al. 2001. Dev Dyn. 220:40.
- Sunmonu NA, et al. 2011. J. Cell. Physiol. 226:1722.
Antigen Details
- Structure
- Growth factor
- Distribution
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Secreted protein; widely expressed during embryonic stages, such as the primitive streak, limb bud and midbrain-hindbrain junction; low expression levels in adult hematopoietic cells and gonads.
- Function
- FGF-8 is involved in the regulation of cell proliferation and cell differentiation during embryonic development.
- Ligand/Receptor
- FGFR1, FGFR2, FGFR3 and FGFR4.
- Bioactivity
- Measured by its ability to induce proliferation of BALB/c 3T3 cells.
- Cell Targets
- Embryonic progenitor cells.
- Cell Type
- Embryonic Stem Cells
- Biology Area
- Stem Cells
- Gene ID
- 2253 View all products for this Gene ID
- UniProt
- View information about FGF-8a on UniProt.org
Related FAQs
- Why choose BioLegend recombinant proteins?
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• 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?
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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?
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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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