Recombinant Bovine FGF basic/FGF2/bFGF Protein Summary
Product Specifications
Pro10-Ser155, with an N-terminal Ala
Analysis
Product Datasheets
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.
2099-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 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.
|
2099-FB/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in Tris-HCl and NaCl with Trehalose. |
| Reconstitution | Reconstitute at 100 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.
|
Reconstitution Calculator
Background: FGF basic/FGF2/bFGF
FGF basic is a member of the FGF family, currently comprised of 23 related mitogenic proteins which show 35-60% amino acid conservation. FGF acidic and basic, unlike the other members of the family, lack signal peptides and are apparently secreted by mechanisms other than the classical protein secretion pathway. FGF basic has been isolated from a number of sources, including neural tissue, pituitary, adrenal cortex, corpus luteum and placenta. This factor contains four cysteine residues but reduced FGF basic retains full biological activity, indicating that disulfide bonds are not required for this activity. Several reports indicate that a variety of forms of FGF basic are produced as a result of N-terminal extensions. These extensions apparently affect localization of FGF basic in cellular compartments but do not affect biological activity. Studies indicate that binding of FGF to heparin or cell surface heparan sulfate proteoglycans is necessary for binding of FGF to high affinity FGF receptors. FGF acidic and basic appear to bind to the same high affinity receptors and show a similar range of biological activities.
FGF basic stimulates the proliferation of all cells of mesodermal origin, and many cells of neuroectodermal, ectodermal and endodermal origin. The cells include fibroblasts, endothelial cells, astrocytes, oligodendrocytes, neuroblasts, keratinocytes, osteoblasts, smooth muscle cells, and melanocytes. FGF basic is chemotactic and mitogenic for endothelial cells in vitro. FGF basic induces neuron differentiation, survival and regeneration. FGF basic has also been shown to be crucial in modulating embryonic development and differentiation. These observed in vitro functions of FGF basic 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 participate in the production of a variety of pathological conditions resulting from excessive cell proliferation and excessive angiogenesis (1, 2).
- Coulier, F. et al. (1997) J. Mol. Evol. 44:43.
- Fernig, D. et al. (1994) Prog. Growth Factor Res. 5:353.
Citations for Recombinant Bovine FGF basic/FGF2/bFGF Protein
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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Citations: Showing 1 - 3
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MicroRNA 221 expression in theca and granulosa cells: Hormonal regulation and function
Authors: CL Robinson, L Zhang, LF Schütz, ML Totty, LJ Spicer
J. Anim. Sci., 2018-03-06;0(0):.
Species: Bovine
Sample Types: Whole Cells
Applications: Cell Culture -
miR-17 regulates the proliferation and differentiation of the neural precursor cells during mouse corticogenesis.
Authors: Mao S, Li H, Sun Q, Zen K, Zhang C, Li L
FEBS J, 2014-01-15;281(4):1144-58.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Cross-talk between fibroblast growth factor and bone morphogenetic proteins regulates gap junction-mediated intercellular communication in lens cells.
Authors: Boswell BA, Lein PJ, Musil LS
Mol. Biol. Cell, 2008-04-09;19(6):2631-41.
Species: Chicken
Sample Types: Whole Tissue
Applications: Bioassay
FAQs
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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
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