- Regulatory Status
- Other Names
- Fibroblast Growth Factor-acidic (FGF-1), HBGF-1, ECGF-beta
- Ave. Rating
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- Product Citations
|Cat #||Size||Price||Quantity Check Availability||Save|
|710204||50 µg||237 CHF|
FGF-1, one of the most studied members of the fibroblast growth factor family, is a powerful mitogen exhibiting strong actions on many different cell types. FGF-1 activities can be mediated not only by autocrine/paracrine pathway but also intracrine pathway. FGF-1 lacks a secretion signal peptide and is exported through a non-classical pathway. Endogenous FGF-1 is found in the nucleus in most of the cell types tested. Nuclear localization is required for FGF-1 mitogenic activity. FGF-1 promotes tumor development by promoting cancer cell proliferation and survival. Increased FGF-1 expression in early stages of many different cancers has been reported. MCF-7 breast cells overexpressing FGF-1 can form vascularized, metastatic tumors in ovariectomized or tamoxifen-treated nude mice. FGF-1 also induces angiogenesis in vitro and in vivo. Now FGF-1 is an attractive candidate for cancer immunotargeting. FGF-1 is also involved in neuronal cell differentiation and survival. FGF-1 is highly expressed in motor neurons. In response to damage, motor neurons can release FGF-1, resulting in astrocyte activation. Under oxidative stress, astrocytes can also release FGF-1 which stimulates apoE/HDL generation in an autocrine manner for protection of the brain against oxidative stress. Involvement of FGF-1 in inflammation, cardioprotection, wound healing, adipocyte remodeling, and restenosis are also reported.Product Details
- Human FGF-1, amino acids (Phe16 - Asp155) (Accession# NP_000791.1) containing a N-terminal Met, was expressed in E. coli.
- Molecular Mass
- The 141 amino acid recombinant protein has a predicted molecular mass of approximately 16 kD. The predicted N-terminal amino acid is Met.
- >95%, as determined by Coomassie stained SDS-PAGE gel and HPLC analysis.
- Lyophilized, carrier-free.
- Endotoxin Level
- Less than 0.1 ng per µg of protein.
- Storage & Handling
- Unopened vial can be stored at -20°C or -70°C. For maximum results, quick spin vial prior to opening. Reconstitute in 5 mM sodium phosphate, pH 8.0 to a concentration of <0.5 mg/ml. 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.
- ED50 ≤ 0.5 ng/ml, corresponding to a specific activity of ≥ 2.0 x 106 units/mg, as measured by its ability to stimulate proliferation of BALB/c 3T3 cells in the presence of 10 µg/ml of heparin.
- Recommended Usage
- Application Notes
This product is reactive with human, cow, mouse, pig, rat, shark, and squid.
- Growth factor
FGF-1 is widely expressed in developing and adult tissues.
- FGF-1 plays important roles in many biological processes, including cell proliferation, inflammation and angiogenesis. FGF-1 has low stability and a very short half-life in vivo. Binding to heparin increases the stability of FGF-1 and is also important for the formation of active FGF-acidic/FGFR complex.
- Intracellular FGF-1 can interact directly with CK2, FIBP, mortalin and the ribosome-binding protein p34/leucine-rich repeat containing 59 (LRRC59).
- FGF-1 can signal through all known cell surface FGFR isoforms (FGFR1b, 1c, 2b, 2c, 3b, 3c and 4). FGF-1 also binds to heparin and heparin sulfate proteoglycans on the cell surface.
- Human FGF-1-acidic is able to stimulate proliferation of Balb/c 3T3 cells.
- Cell Type
- Embryonic Stem Cells, Hematopoietic stem and progenitors, Mesenchymal Stem Cells, Neural Stem Cells
- Biology Area
- Angiogenesis, Apoptosis/Tumor Suppressors/Cell Death, Cell Biology, Cell Cycle/DNA Replication, Cell Motility/Cytoskeleton/Structure, Neuroscience, Stem Cells, Synaptic Biology
- Molecular Family
- Cytokines/Chemokines, Growth Factors
- Antigen References
1. Preta M, et al. 2005. Cytokine Growth Factor Rev. 16:159.
2. Krzewska M, et al. 2008. Crit. Rev. Clin. Lab Sci. 45:91.
3. Zhang L, et al. 1997. Oncogene. 15:2093.
4. Lin YZ, et al. 1996. J. Biol. Chem. 271:75305.
5. Culajay JF, et al. 2000. Biochemistry. 39:7153.
6. Cassina P, et al. 2005. J. Neurochem. 93:38.
7. Pehar M, et al. 2005. Neurodegener. Dis. 2:139.
8. Jonker JW, et al. 2012. Nature. 485:391.
9. Compagni A, et al. 2000. Cancer Res. 60:7163.
- Gene ID
- 2246 View all products for this Gene ID
- View information about FGF-1-acidic 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)