F3685
Fibroblast Growth Factor-Basic
FGF-Basic, from human, recombinant, expressed in E. coli, carrier free
Synonym(s):
FGB-b, FGF-2, HBGF-2, HBGH-2, Prostatropin, bFGF
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About This Item
UNSPSC Code:
12352202
NACRES:
NA.77
biological source
human
Quality Level
recombinant
expressed in E. coli
Assay
≥97% (SDS-PAGE)
form
lyophilized powder
potency
<1 ng/mL Biological Activity EC50
mol wt
16.0 kDa
packaging
pkg of 4X25 μg
pkg of 25 μg
storage condition
avoid repeated freeze/thaw cycles
color
white to faint yellow cast
solubility
water: soluble 0.025 mg, clear, colorless to faintly yellow
UniProt accession no.
storage temp.
−20°C
Gene Information
human ... FGF2(2247)
Related Categories
General description
Since FGF-Basic is found in a variety of organs, acts on a wide range of cell types, and has multifunctional actions, it has acquired numerous synonyms, including heparin-binding growth factor (class II or beta), eye-derived growth factor I, cartilage-derived growth factor, and astroglial growth factor II5. Purified bovine and human FGF-basic differ by 3 amino acids in sequence3, and are biologically and immunologically cross-reactive.
Citation
1. Gospodarowicz, D., Localization of a fibroblast growth factor and its effect alone and with hydrocortisone on 3T3 cell growth. Nature, 249, 123-127 (1974).
2. Gospodarowicz, D. et al., Structural characterization and biological functions of fibroblast growth factor. Endo. Rev., 8, 95-114 (1987).
3. Esch, F. et al., Primary structure of bovine pituitary basic fibroblast growth factor (FGF) and comparison with the amino-terminal sequence of bovine brain acidic FGF. Proc. Natl. Acad. Sci. USA, 82, 6507-6511 (1985).
4. Neufeld, G., and Gospodarowicz, D., Basic and acidic fibroblast growth factors interact with the same cell surface receptors. J. Biol. Chem., 261, 5631-5637 (1986).
5. Lobb, R.R. et al., Purification of heparin-binding growth factors. Anal. Biochem., 154, 1-14 (1986).
6. Abraham, J.A., Human basic fibroblast growth factor: nucleotide sequence and genomic organization. EMBO J., 5, 2523- 2528 (1986).
2. Gospodarowicz, D. et al., Structural characterization and biological functions of fibroblast growth factor. Endo. Rev., 8, 95-114 (1987).
3. Esch, F. et al., Primary structure of bovine pituitary basic fibroblast growth factor (FGF) and comparison with the amino-terminal sequence of bovine brain acidic FGF. Proc. Natl. Acad. Sci. USA, 82, 6507-6511 (1985).
4. Neufeld, G., and Gospodarowicz, D., Basic and acidic fibroblast growth factors interact with the same cell surface receptors. J. Biol. Chem., 261, 5631-5637 (1986).
5. Lobb, R.R. et al., Purification of heparin-binding growth factors. Anal. Biochem., 154, 1-14 (1986).
6. Abraham, J.A., Human basic fibroblast growth factor: nucleotide sequence and genomic organization. EMBO J., 5, 2523- 2528 (1986).
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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