- Regulatory Status
- Other Names
- CD334, Fibroblast growth factor receptor 4
- Ave. Rating
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- Product Citations
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Fibroblast growth factor receptors (FGFRs) are transmembrane tyrosine kinase receptors that belong to the immunoglobulin (Ig) superfamily and bind to fibroblast growth factors (FGFs). The activation of FGFRs is involved in cell survival, proliferation, migration, and differentiation. There are four human FGFR genes (FGFR1-4). Each FGFR comprises of an extracellular ligand binding domain, a single transmembrane domain, and an intracellular tyrosine kinase domain. The extracellular ligand binding domain contains three immunoglobulin-like (Ig-like) loops, a short cluster of conserved acidic amino acids, and a heparin binding domain. The Ig-like loop III is the core of the ligand-binding site. Alternative splicing in Ig-like loop III results in IIIb and IIIc isoforms of FGFR1-3, which change the specificity of the receptor. Unlike FGFR1-3, FGFR4 is expressed as a single isoform. The overexpression of FGFR4 has been reported in many tumors including prostate, breast, pancreatic, pituitary, hepatocellular, and gynecological tumors. Overexpression and polymorphism (Gly388Arg) of FGFR4 have been associated with a more aggressive tumor behavior and anti-cancer drug resistance. Also, the overexpression of FGFR4 Arg388 can up-regulate genes including uPAR and Ehm2, which are known to promote invasion and metastasis. FGFR4 Arg388 also promotes cancer cell migration and invasion by interacting and stabilizing membrane-type 1 matrix metalloproteinase. In vitro studies have shown that FGFR4 can respond to FGF-1, -8, -17, -18, -19, -21, and -23. The FGF19/FGFR4 axis plays an important role in liver bile acid metabolism. Abnormal FGF19/FGFR4 signaling has been shown to cause hepatocellular carcinomas in mice.Product Details
- Human FGFR4, amino acids (Leu22-Asp369) (Accession# BC011847), with a linker sequence (GSSR) and a C-terminal human IgG1 (Pro100 - Lys330) was expressed in 293E cells.
- Molecular Mass
- The 583 amino acid recombinant protein has a predicted molecular mass of approximately 64.8 kD. The protein migrates approximately at 95-100 kD in DTT-reducing conditions and at 160-170 kD in non-reducing conditions by SDS-PAGE. The predicted N-terminal amino acid is Leu.
- >95%, as determined by Coomassie stained SDS-PAGE.
- 0.22 µm filtered protein solution is in PBS, pH 7.2.
- 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.
- ED50 = 5 - 10 ng/ml, corresponding to a specific activity of 1 - 2 x 105 units/mg, as determined by a dose-dependent inhibition of FGF acidic-dependent NIH3T3 cell proliferation. The concentration of FGF acidic (Cat. No. 599202) used in the assay was 0.5 ng/ml. The inhibition of proliferation was measured by the colorimetric MTS assay.
- 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 receptor, in a chimeric format.
FGFR4 can be detected in human adult tissues including the liver, sublingual gland ducts, kidney, ureter, and in the media of some arterioles and veins in most tissues.
- FGFR4 is a conserved tyrosine kinase receptor that regulates cell proliferation, differentiation, migration, and cellular metabolism.
- FGF-1, FGF-8, FGF-17, FGF-18, FGF-19, FGF-21, and FGF-23. ßKlotho protein is a co-receptor of FGFR4 for FGF-19 binding.
- 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
- Cytokine/Chemokine Receptors, Soluble Receptors
- Antigen References
1. Zhang X, et al. 2006. J. Biol. Chem. 281:15694.
2. Beenken A and Mohammadi M. 2009. Nat. Rev. Drug Discov. 8:235.
3. Wang J, et al. 2008. Neoplasia. 8:847.
4. Thussbas C, et al. 2006. J. Clin. Oncol. 24:3747.
5. Lin BC, et al. 2007. J. Biol. Chem. 282:27277.
6. Gauglhofer C, et al. 2014. Carci. 35:2331.
7. Wang J, et al. 2004. Clin. Cancer Res. 10:6169.
8. Sugiyama N, et al. 2010. Cancer Res. 70:7851.
9. Hughes SE. 1997. J. Histochem. Cytochem. 45:1005.
- Gene ID
- 2264 View all products for this Gene ID
- View information about FGFR4 on UniProt.org
- 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?
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?
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?
- Use formula Specific activity (Units/mg) = 10e6/ ED50 (ng/mL)