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- Regulatory Status
- RUO
- Other Names
- Fibroslast Growth Factor 4 (FGF-4), Heparin-Binding Growth Factor 4 (HBGF-4), HST-1, K-FGF, KS3, Kaposi Sacrcoma Oncogene, Heparin Secretory Transforming Protein 1 (HSTF-1)
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- Product Citations
- publications
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NIH3T3 proliferation induced by human FGF-4.
| Cat # | Size | Price | Quantity Check Availability | Save | ||
|---|---|---|---|---|---|---|
| 592204 | 25 µg | 218 CHF | ||||
| 592206 | 100 µg | 692 CHF | ||||
FGF-4 was first identified as HST-1 gene by a NIH3T3 transforming assay. It belongs to the FGF family that includes 22 members FGF1-FGF23. FGF15 has not been identified in humans. FGF-4 exhibits strong effects on many different cell types and tissues, and plays important roles in both embryogenesis and adult tissue stem cell development in a variety of organisms. FGF-4 can stimulate limb mesenchyme proliferation and can provide all the signals required for normal outgrowth and patterning of the limb. FGF-4 mRNA has been detected in the apical ectodermal ridge of the limb bud in Days 11 and 12 embryos. FGF-4 is also involved in early heart development by supporting the proliferation and differentiation of precardiac myoblasts. In adults, FGF-4 is expressed in the testis and its overexpression results in enhanced spermatogenesis. FGF-4 is also a potent inducer of platelet production from megakaryocytes. FGF-4 expression has been detected in the brain at both neonatal and adult stages. FGF-4 can induce neural stem cell proliferation and neuronal differentiation. The diverse functions of FGF-4 are mediated by FGF receptors (FGFR) that contain an extracellular ligand-binding domain with three immunoglobulin-like domains. Like other FGFs, FGF-4 also binds to anionic glycosaminoglycans heparin and heparin sulfate with high affinity. Heparin sulfate availability has been shown to regulate the binding between FGF-4 and its receptors. The role of FGF-4 in cancer has also been extensively investigated. FGF-4 is an angiogenic protein, and amplification of FGF-4 gene has been found in many human tumors. It has been shown that FGF-4 is a potential target for the treatment of human testicular tumors.
Product DetailsProduct Details
- Source
- Human FGF4, amino acids Ser54-Leu206 (Accession# P08620) was expressed in E. coli.
- Molecular Mass
- The 153 amino acid recombinant protein has a predicted molecular mass of approximately 19.7 kD. The non-reduced and DTT-reduced protein migrates at approximately 19.7 kD by SDS-PAGE. The predicted N-terminal amino acid is Serine.
- Purity
- >95%, as determined by Coomassie stained SDS-PAGE.
- Formulation
- 0.22 µm filtered protein solution is in PBS.
- Endotoxin Level
- Less than 0.01 ng per µg cytokine as determined by the LAL method.
- 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 0.2-1 ng/ml, corresponding to a specific activity 1-5 x 106 units/mg, as determined by a dose-dependent stimulation of NIH3T3 cell proliferation.
- 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.
- Product Citations
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Antigen Details
- Structure
- Growth factor.
- Distribution
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Expression of FGF-4 is highly restricted to undifferentiated stem cells.
- Function
- FGF-4 is a mitogenic, angiogenic, and survival factor. It is involved in cell proliferation and differentiation in embryonic development processes. N-glycosylation may negatively regulate FGF-4 activity.
- Interaction
- Precardiac myoblasts, megacariocytes, neural stem cells.
- Ligand/Receptor
- FGFR-I, IIIc; FGFR-2, IIIc; FGFR-3, IIIc, FGFR-4.
- Cell Type
- Embryonic Stem Cells, Hematopoietic stem and progenitors, Mesenchymal Stem Cells, Neural Stem Cells
- Biology Area
- Apoptosis/Tumor Suppressors/Cell Death, Cell Biology, Cell Cycle/DNA Replication, Neuroscience, Stem Cells, Synaptic Biology, Transcription Factors
- Molecular Family
- Cytokines/Chemokines, Growth Factors
- Antigen References
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1. Konishi H, et al. 1996. Oncogene. 13:9.
2. Sun X, et al. 2000. Nat. Genet. 25:83.
3. Yamamoto H, et al. 2002. Oncogene 21:899.
4. Kosaka N, et al. 2006. FASEB J. 20:1484.
5. Kosaka N, et al. 2009. Dev. Dyn. 238:265.
6. Arao T, et al. 2013. Hepatology 57:1407.
7. Itoh N and Ohta H. 2013. Front. Physiol. 4:247. - Gene ID
- 2249 View all products for this Gene ID
- UniProt
- View information about FGF-4 on UniProt.org
Related Pages & Pathways
Pathways
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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