Bovine FGF acidic/FGF1 Protein Summary
Product Specifications
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
132-FA
| Formulation | Lyophilized from a 0.2 μm filtered solution in Tris-HCl and NaCl with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 25 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
132-FA/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in Tris-HCl and NaCl. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
Background: FGF acidic/FGF1
FGF acidic, also known as FGF1, ECGF, and HBGF-1, is a 17 kDa nonglycosylated member of the FGF family of mitogenic peptides. FGF acidic, which is produced by multiple cell types, stimulates the proliferation of all cells of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin. It plays a number of roles in development, regeneration, and angiogenesis (1-3). Bovine FGF acidic shares 53% amino acid sequence identity with FGF basic and 11%-31% with other bovine FGFs. It shares 92%, 91%, 88%, and 91% aa sequence identity with human, mouse, porcine, and rat FGF acidic, respectively, and exhibits considerable species crossreactivity. During its nonclassical secretion, FGF acidic associates with S100A13, copper ions, and the C2A domain of synaptotagmin 1 (4). It is released extracellularly as a disulfide-linked homodimer and is stored in complex with extracellular heparan sulfate (5). The ability of heparan sulfate to bind FGF acidic is determined by its pattern of sulfation, and alterations in this pattern during embryognesis thereby regulate FGF acidic bioactivity (6). The association of FGF acidic with heparan sulfate is a prerequisite for its subsequent interaction with FGF receptors (7, 8). Ligation triggers receptor dimerization, transphosphorylation, and internalization of receptor/FGF complexes (9). Internalized FGF acidic can translocate to the cytosol with the assistance of Hsp90 and then migrate to the nucleus by means of its two nuclear localization signals (10-12). The phosphorylation of FGF acidic by nuclear PKC delta triggers its active export to the cytosol where it is dephosphorylated and degraded (13, 14). Intracellular FGF acidic functions as a survival factor by inhibiting p53 activity and proapoptotic signaling (15).
- Gimenez-Gallego, G. et al. (1985) Science 230:1385.
- Galzie, Z. et al. (1997) Biochem. Cell Biol. 75:669.
- Presta, M. et al. (2005) Cytokine Growth Factor Rev. 16:159.
- Rajalingam, D. et al. (2007) Biochemistry 46:9225.
- Guerrini, M. et al. (2007) Curr. Pharm. Des. 13:2045.
- Allen, B.L. and A.C. Rapraeger (2003) J. Cell Biol. 163:637.
- Robinson, C.J. et al. (2005) J. Biol. Chem. 280:42274.
- Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
- Wiedlocha, A. and V. Sorensen (2004) Curr. Top. Microbiol. Immunol. 286:45.
- Wesche, J. et al. (2006) J. Biol. Chem. 281:11405.
- Imamura, T. et al. (1990) Science 249:1567.
- Wesche, J. et al. (2005) Biochemistry 44:6071.
- Wiedlocha, A. et al. (2005) Mol. Biol. Cell 16:794.
- Nilsen, T. et al. (2007) J. Biol. Chem. 282:26245.
- Bouleau, S. et al. (2005) Oncogene 24:7839.
Citations for Bovine FGF acidic/FGF1 Protein
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Recombinant spider silk protein eADF4(C16)-RGD coatings are suitable for cardiac tissue engineering
Authors: JPM Kramer, TB Aigner, J Petzold, K Roshanbinf, T Scheibel, FB Engel
Sci Rep, 2020-05-29;10(1):8789.
Species: Rat
Sample Types: Whole Cells
Applications: Bioassay -
Common Regulatory Pathways Mediate Activity of MicroRNAs Inducing Cardiomyocyte Proliferation
Authors: C Torrini, RJ Cubero, E Dirkx, L Braga, H Ali, G Prosdocimo, MI Gutierrez, C Collesi, D Licastro, L Zentilin, M Mano, S Zacchigna, M Vendruscol, M Marsili, A Samal, M Giacca
Cell Rep, 2019-05-28;27(9):2759-2771.e5.
Species: Rat
Sample Types: Whole Cells
Applications: Bioassay -
Different aspects of gliosis in retinal Muller glia can be induced by CNTF, insulin, and FGF2 in the absence of damage.
Authors: Fischer AJ, Omar G, Eubanks J, McGuire CR, Dierks BD, Reh TA
Mol. Vis., 2004-12-22;10(0):973-86.
Species: Chicken
Sample Types: In Vivo
Applications: In Vivo
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