Source E. coliderived
Accession # P13109
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 ED50 for this effect is typically 0.31.8
Endotoxin Level <1.0 EU per 1 μg of the protein by the LAL method.
Purity >95%, by SDSPAGE
under reducing conditions and visualized by silver stain.
Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4, EDTA and DTT with BSA as a carrier protein. See Certificate of Analysis for
PREPARATION AND STORAGE
Reconstitution Reconstitute at 100 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 immediay at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freezethaw
l 12 months from date of receipt, 20
°C as supplied.
l 1 month, 2 to 8 °C under sterile conditions after reconstitution.
l 3 months, 20
°C under sterile conditions after reconstitution.
FGF basic （FGF2,
is one of at least 22 mitogenic proteins of the FGF family, which show 35 60%
amino acid conservation （1 3）.
Unlike other FGFs,
FGF acidic and basic lack signal peptides and are secreted by an alternate pathway. Storage pools within the cell or on cell surface heparan sulfate proteoglycans
（HSPG） are likely. The predicted 18 kDa FGF basic isoform can be located in both the cytoplasm and the nucleus and is presumed to be the form secreted （4）.
Transcription from alternate start sites produces 21 23
kDa forms found only in the nucleus. High and low molecular weight human FGF basic targets the expression
of different genes when expressed in NIH3T3
cells （5）. The 18 kDa rat sequence has 98% amino acid （aa） identity with mouse, and 96 97%
aa identity with human,
bovine and sheep FGF basic （6, 7）. Autocrine, intracrine and paracrine actions of FGF basic have been identified. Binding of FGF to heparin or cell surface HSPG is
necessary for binding, dimerization and activation of tyrosine kinase FGF receptors. FGF basic binds other proteins, polysaccharides and lipids with lower affinity （3）.
Expression of FGF basic is nearly ubiquitous but disruption of the mouse FGF basic gene gives a relatively mild phenotype, suggesting compensation by other FGF
family members. FGF basic modulates such normal processes as angiogenesis, wound healing and tissue repair, embryonic development and differentiation, neuronal
function and neural degeneration. Transgenic overexpression of FGF basic results in excessive proliferation and angiogenesis reminiscent of a variety of pathological
conditions （1 3）.
1. Coulier, F. et al. （1997） J. Mol. Evol. 44:43.
2. Fernig, D. et al. （1994） Prog. Growth Factor Res. 5:353.
3. Presta, M. et al. （2005） Cytokine Growth Factor Rev. 16:159.
4. Claus, P. et al. （2003） J. Biol. Chem. 278:479.
5. Quarto, N. et al. （2005） Gene 356:49.
6. Tsuneto, M. et al. （2005） Biochem. Biophys. Res. Commun. 335:1239.
7. Shimasaki, S. et al. （1988） Biochem. Biophys. Res. Commun. 157:256.
Recombinant Rat FGF basic
Catalog Number: 3339-FB