详细说明
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
Measured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Rizzino, A. et al. (1988) Cancer Res. 48:4266; Thomas, K. et al. (1987) Methods Enzymol. 147:120. The ED 50 for this effect is 0.05-0.25 ng/mL in the presence of 10 µg/mL heparin.
Source
E. coli-derived Phe16-Asp155, with an N-terminal Met
Accession #
N-terminal Sequence
AnalysisMet
Predicted Molecular Mass
16 kDa
Carrier Free
What does CF mean?
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.
What formulation is right for me?
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.
4686-FA |
| 4686-FA/CF |
Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, Na 2SO 4, EDTA and DTT with BSA as a carrier protein. | Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, Na 2SO 4, EDTA and DTT. | |
Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. | 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. | 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.
| Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: FGF acidic
FGF acidic, also known as FGF-1, 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). Mouse FGF acidic shares 52% amino acid (aa) sequence identity with FGF basic and 15% - 35% with other mouse FGFs. It shares 91%, 96%, 94%, and 100% aa sequence identity with bovine, human, 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). The secreted FGF acidic 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 embryogenesis thereby regulating 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).
References:
Madiai, F. et al. (1996) Gene 179:231.
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.
Long Name:
Fibroblast Growth Factor acidic
Entrez Gene IDs:
2246 (Human); 14164 (Mouse); 25317 (Rat); 281160 (Bovine)
Alternate Names:
AFGF; alpha; alpha-ECGF; beta-ECGF; ECGF; ECGFB; ECGF-betaAcidic fibroblast growth factor; endothelial cell growth factor, beta; FGF acidic; FGF1; FGF-1; FGFABeta-endothelial cell growth factor; FGF-alpha; fibroblast growth factor 1 (acidic); GLIO703; HBGF1; HBGF-1; heparin-binding growth factor 1