- Regulatory Status
- Other Names
- FGF-2, HBGF-2, BFGF, FGFB, Fibroblast Growth Factor 2, Basic Fibroblast Growth Factor, Heparin binding growth factor 2, HBGF2
- Ave. Rating
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- Product Citations
FGF-basic, also known as FGF-2, is a member of the fibroblast growth factor (FGF) family, which includes 22 members. FGF-acidic and FGF-basic do not have classical secretory signal peptides. The secretion of FGF-2 occurs by direct translocation across the plasma membrane. Multiple forms of FGF-2 derived by alternative translation from AUG and CUG codons from the same mRNA transcript have been described. FGF-2 is expressed in almost all tissues and plays an important role in a variety of normal and pathological processes, including development, wound healing, and neoplastic transformation. FGF-2 is mitogenic for many cell types, both epithelial and mesenchymal. It shows potent angiogenic activity and has been implicated in tumor angiogenesis. FGF-2 significantly promotes the proliferation of adipose-derived mesenchymal cells (AMC) and enhances chondrogenesis in three-dimensional micromass culture. FGF-2 binds to a family of four distinct, high affinity tyrosine kinase receptors, designated FGFR-1 to FGFR-4. In addition, FGF-2 binds to the extracellular matrix (ECM) and heparan sulfate (HS), and is an essential and dynamic regulator of fibroblast growth factor (FGF) signaling. Two fundamentally different crystallographic models have been proposed to explain, at the molecular level, how heparan sulphate enables FGF and FGF receptor (FGFR) to assemble into a functional dimer on the cell surface, although there is controversy regarding the exact manner by which this occurs. FGF-2, αvβ3 integrin, and FGFR-1, form a trimolecular complex required for ERK1/2 activation. MT1-MMP (MMP-14) downregulates the amount of FGF-2 bound to the cell surface, and therefore, it reduces FGF-2 signaling.Product Details
- Human FGF-basic (146 aa), amino acid Pro143-Ser288 (Accession # P09038) was expressed in E.coli.
- Molecular Mass
- The 146 amino acid recombinant protein has a predicted molecular mass of approximately 16.5 kD. The DTT-reduced and non-reduced protein migrates at approximately 17 kD by SDS-PAGE. The predicted N-terminal amino acid is Pro.
- > 95%, as determined by Coomassie stained SDS-PAGE
- 0.22 µm filtered protein solution is in pH 7.5, 20 mM Tris, 150 mM NaCl.
- Endotoxin Level
- Less than 0.1 EU 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. 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.
- Recombinant human FGF-basic (146 aa) induces the proliferation of NIH/3T3 cells in a dose-dependent manner. The ED50 for this effect is 0.015 - 0.075 ng/mL.
- 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.
Brain, retina, pituitary, kidney, placenta, testis, corpus luteum, adrenal glands, monocytes, prostate, bone, liver, cartilage, endothelial cells, and epithelial cells
- Possesses broad mitogenic and potent angiogenic activity, plays a key role in physiological and pathological conditions, including embryonic development, wound repair, inflammation, and tumor growth. MT1-MMP downregulates fibroblast growth factor-2 (FGF-2) signaling.
- FGF-basic binds to αvβ3 integrin. Fibroblasts, myoblasts, osteoblasts, neuronal cells, endothelial cells, keratinocytes, chondrocytes, astrocytes, oligodendrocytes, and smooth muscle cells.
- FGFR1, FGFR2, FGFR3 and FGFR4. Low affinity coreceptor heparan sulfate (HS) and heparan sulfate proteoglycans (HSPG) required for full activity.
- Recombinant human FGF-basic (146 aa) induces the proliferation of NIH/3T3 cells in a dose-dependent manner.
- Cell Type
- Astrocytes, Embryonic Stem Cells, Endothelial cells, Epithelial cells, Fibroblasts, Hematopoietic stem and progenitors, Mesenchymal cells, Mesenchymal Stem Cells, Neural Stem Cells, Osteoblasts, Osteoclasts
- Biology Area
- Angiogenesis, Cancer Biomarkers, Cardiovascular Biology, Cell Proliferation and Viability, Stem Cells
- Molecular Family
- Growth Factors
- Antigen References
- Schlessinger J, et al. 2000. Mol Cell. 6:743-50.
- Ibrahimi OA, et al. 2001. Proc Natl Acad Sci USA. 98:7182-7.
- Yu PJ, et al. 2007. J Cell Biochem. 100:1100-8.
- Beenken A & Mohammadi M. 2009. Nat Rev Drug Discov. 8:235-53.
- Prudovsky I, et al. 2013. Int J Mol Sci. 14:3734-72.
- Tassone E, et al. 2015. J Cell Physiol. 230:366-77.
- Ornitz DN & Itho N. 2015. Wiley Interdiscip Rev Dev Biol. 4:215-66.
- Chien SY, et al. 2016. Clin Sci (Lond). 130:667-81.
- Gene ID
- 2247 View all products for this Gene ID
- View information about FGF-basic 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) = 10^6/ ED50 (ng/mL)