Recombinant Human FGF basic/FGF2/bFGF (145 aa) Protein, CF
Recombinant Human FGF basic/FGF2/bFGF (145 aa) Protein, CF Summary
The specific activity of Recombinant Human FGF basic/FGF2/bFGF (Catalog # 3718-FB) is approximately 3.1 x 106 IU/mg, which is calibrated against human FGF basic/FGF2/bFGF WHO International Standard (NIBSC code: 90/712). Specific activity is for reference purposes only and is not routinely tested.
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.
|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 with polar packs. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Measured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Raines, E.W.et al. (1985) Methods Enzymol.109:749. The ED50 for this effect is 0.1-0.6 ng/mL.
Background: FGF basic/FGF2/bFGF
FGF basic (also known as FGF-2 and HBGF-2) is an 18-34 kDa, heparin-binding member of the FGF superfamily of molecules (1-3). Superfamily members are characterized by the presence of a centrally placed beta -trefoil structure. FGF acidic (FGF-1) and FGF basic (FGF-2) were the first two identified FGFs, and the designations acidic and basic refer to their relative isoelectric points. Human FGF basic is 288 amino acids (aa) in length. There are multiple start sites, four of which utilize atypical CUG codons, and one that initiates at an AUG start site (4-6). The four CUG start sites generate high molecular weight (HMW) FGF basic. There is a 34 kDa, 288 aa form, a 24 kDa, 210 aa form, a 22.5 kDa, 201 aa form, and a 22 kDa, 196 aa form. All are retained intracellularly, undergo extensive methylation, and possess one or more nuclear localization signals (NLS) (7-9). The AUG initiating form is 18 kDa and 155 aa in length. There is no signal sequence (ss). It is, however, secreted directly through the plasma membrane via a mechanism that appears to be dependent upon tertiary structure (10). In place of a ss, there is purportedly a 9 aa N-terminal prosegment that precedes a 146 aa mature segment (11). Early isolations of 18 kDa bovine FGF basic yielded 146 aa molecules, an effect attributed to the presence of acid proteases (12). The molecule contains a heparin-binding site (aa residues 128-144), and undergoes phosphorylation at Ser117 (13). There is also an ill-defined C-terminal NLS that may be more “functional” (or 3-dimensional) than structural (7). Human 146 aa FGF basic is 97% aa identical to mouse FGF basic (14).
- Sorenson, V. et al. (2006) BioEssays 28:504.
- Kardami, E. et al. (2004) Cardiovasc. Res. 63:458.
- Nugent, M.A. and R.V. Lozzo (2000) Int. J. Biochem. Cell Biol. 32:115.
- Abraham, J.A. et al. (1986) EMBO J. 5:2523.
- Prats, H. et al. (1989) Proc. Natl. Acad. Sci. USA 86:1836.
- Arnaud, E. et al. (1999) Mol. Cell. Biol. 19:505.
- Foletti, A. et al. (2003) Cell. Mol. Life Sci. 60:2254.
- Arese, M. et al. (1999) Mol. Biol. Cell 10:1429.
- Pintucci, G. et al. (1996) Mol. Biol. Cell 7:1249.
- Nickel, W. (2005) Traffic 6:607.
- SwissProt # P09038.
- Klagsbrun, M. et al. (1987) Proc. Natl. Acad. Sci. USA 84:1839.
- Bailly, K. et al. (2000) FASEB J. 14:333.
- Hebert, J.M. et al. (1990) Dev. Biol. 138:454.
Citation for Recombinant Human FGF basic/FGF2/bFGF (145 aa) Protein, CF
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.
1 Citation: Showing 1 - 1
Low dose amiodarone reduces tumor growth and angiogenesis
Authors: E Steinberg, A Fluksman, C Zemmour, K Tischenko, A Karsch-Blu, Y Brill-Karn, AE Birsner, RJ D'Amato, O Benny
Sci Rep, 2020;10(1):18034.
Sample Types: In Vivo
What receptors does FGF basic bind?
FGF receptor specificity has been reviewed in multiple citations. Please find more information at: //www.rndsystems.com/resources/articles/fibroblast-growth-factors-and-their-receptors
Does human FGF basic show activity on mouse cells?
Yes, it does. The bioassay uses NR-6 mouse fibroblast cells. There is 95% homology between the human and mouse protein and 98% homology between the human and mouse receptor.
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