Recombinant Human FGF basic/FGF2/bFGF Protein, CF
Recombinant Human FGF basic/FGF2/bFGF Protein, CF Summary
Product Specifications
Ala135-Ser288
Analysis
Product Datasheets
BT-FGFB
Carrier Free
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.
BT-FGFB
Formulation | Lyophilized from a 0.2 μm filtered solution in HEPES and Sodium Sulfate with Trehalose. |
Reconstitution | Reconstitute the 20 μg size at 100 μg/mL in sterile deionized water. Reconstitute all other sizes at 500 μg/mL in sterile deionized water. |
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.
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Scientific Data
Equivalent bioactivity of GMP (BT-FGFB-GMP), Animal-Free (BT-FGFB-AFL) and RUO (Catalog # BT-FGFB) grades of Recombinant Human FGF basic/FGF2/bFGF as measured in a cell proliferation assay using NR6R-3T3 mouse fibroblast cell line (orange, green, red, respectively).
Recombinant Human FGF basic/FGF2/bFGF (Catalog # BT-FGFB) stimulates proliferation of the NR6R-3T3 mouse fibroblast cell line. The ED50 for this effect is 0.100‑1.00 ng/mL.
2 μg/lane of Recombinant Human FGF basic/FGF2/bFGF Protein (Catalog # BT-FGFB) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 18 kDa.
Background: FGF basic/FGF2/bFGF
FGF basic (also known as FGF2 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 (FGF2) 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.
Citations for Recombinant Human FGF basic/FGF2/bFGF 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.
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Generation of a human induced pluripotent stem cell line (FDCHi012-A) from a patient with DYRK1A-related intellectual disability syndrome carrying DYRK1A mutation (c.1024G > T)
Authors: Ge, Y;Cheng, Y;Yin, T;Peng, X;Xiong, Z;Wu, B;Wang, H;Xiong, M;Zhou, W;
Stem cell research
Species: Mouse
Sample Types: Embryo
Applications: Bioassay -
Development of an accelerated cellular model for early changes in Alzheimer's disease
Authors: Xue, H;Gate, S;Gentry, E;Losert, W;Cao, K;
Scientific reports
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Identification of a fundamental cryoinjury mechanism in MSCs and its mitigation through cell-cycle synchronization prior to freezing
Authors: Johnstone, BH;Gu, D;Lin, CH;Du, J;Woods, EJ;
Cryobiology
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
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