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 ED50 for this effect is 0.05-0.25 ng/mL in the presence of 10 µg/mL heparin.
Source
E. coli-derived mouse FGF acidic/FGF1 protein Phe16-Asp155, with an N-terminal Met
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
16 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using 4686-FA/CF in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4, EDTA and DTT.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse FGF acidic/FGF1 Protein, CF
AFGF
alpha
alpha-ECGF
beta-ECGF
ECGF
ECGFB
ECGF-betaAcidic fibroblast growth factor
endothelial cell growth factor, beta
FGF acidic
FGF-1
FGFABeta-endothelial cell growth factor
FGF-alpha
fibroblast growth factor 1 (acidic)
GLIO703
HBGF1
HBGF-1
heparin-binding growth factor 1
Background
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). 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).
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.
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