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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.
233-FB
Formulation | Lyophilized from a 0.2 μm filtered solution in Tris-HCl and NaCl with BSA as a carrier protein. |
Reconstitution | Reconstitute at 100-250 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 immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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233-FB/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in Tris-HCl and NaCl. |
Reconstitution | Reconstitute at 100-250 μg/mL in sterile PBS. |
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.
|
Recombinant Human FGF basic/FGF2/bFGF (146 aa) Protein Summary
Product Specifications
Pro143-Ser288, with an N-terminal Ala
Analysis

Background: FGF basic/FGF2/bFGF
FGF basic (also known as FGF-2 and HBGF-2) is a member of the FGF superfamily of mitogenic proteins which show 35-60% amino acid conservation. FGF acidic and basic are unique from other members of the family in that they lack classical secretory signal peptides. However, they are both readily secreted from cells by an alternative secretory pathway involving direct translocation and aided by several chaperones. 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. The full length human FGF basic protein is 288 amino acids, but there are multiple start sites which produce various shorter forms. Further adding to the complexity, a variety of forms of FGF basic are produced as a result of N-terminal extensions. These extensions affect localization of FGF basic in cellular compartments but do not affect biological activity. FGF basic has been isolated from a number of sources, including neural tissue, adrenal cortex, pituitary gland, corpus luteum, and placenta. Binding of FGF to heparin or cell surface heparan sulfate proteoglycans is required for FGF binding with high affinity to FGF receptors. FGF basic stimulates proliferation of all cells of mesodermal origin as well as many cells of neuroectodermal, ectodermal, and endodermal origin. FGF basic also induces neuronal differentiation, survival, and regeneration, and modulates embryonic development and differentiation. These observed in vitro functions suggest FGF basic may play a role in vivo in the modulation of such normal processes as angiogenesis, wound healing and tissue repair, embryonic development and differentiation, and neuronal function and neural degeneration. Additionally, FGF basic may also participate in the development of several pathological conditions resulting from excessive cell proliferation and/or angiogenesis.
- Coulier, F. et al. (1997) J. Mol. Evol. 44:43.
- Chen, C.H. et al. (2004) Curr. Vasc. Pharmacol. 2:33.
- Mohammadi, M. et al. (2005) Curr. Opin. Struct. Biol. 15:506.
- Fernig, D. et al. (1994) Prog. Growth Factor Res. 5:353.


参考图片
1 µg/lane of Recombinant Human FGF basic (146 aa) was resolved by SDS-PAGE with silver staining, under reducing (R) conditions, showing a band at 17 kDa.
Recombinant Human FGF basic (146aa) (Catalog # 233-FB) stimulates cell proliferation of the NR6R‑3T3 mouse fibroblast cell line. The ED50 for this effect is typically 0.1-0.6 ng/mL.