Detects human FGF basic in direct ELISAs and Western blots. In direct ELISAs, less than 1% cross‑reactivity with recombinant human FGF acidic is observed. Neutralizes the biological activity of recombinant human FGF basic. It will also neutralize the biological effects of bovine FGF basic, but it has no effect on recombinant human or bovine FGF acidic.
Polyclonal Goat IgG
Protein A or G purified
E. coli-derived recombinant human FGF basic
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
<0.10 EU per 1 μg of the antibody by the LAL method.
Recombinant Human FGF basic 157 aa (Catalog # 234-FSE)
Immersion fixed paraffin-embedded sections of human ovarian cancer tissue
Measured by its ability to neutralize FGF basic-induced proliferation in the NR6R‑3T3 mouse fibroblast cell line. Rizzino, A. et al. (1988) Cancer Res. 48:4266. The Neutralization Dose (ND50) is typically 0.5-1.0 µg/mL in the presence of 0.5 ng/mL Recombinant Human FGF basic 146 aa.
Please Note: Optimal dilutions should be determined by each laboratory for each application.
are available in the Technical Information section on our website.
Cell Proliferation Induced by FGF basic and Neutralization by Human FGF basic Antibody.
Recombinant Human FGF basic 146 aa (Catalog # 233-FB) stimulates proliferation in the NR6R‑3T3 mouse fibroblast cell line in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Human FGF basic 146 aa (0.5 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human FGF basic Polyclonal Antibody (Catalog # AB-233-NA). The ND50 is typically 0.5‑1.0 µg/mL.
Preparation and Storage
Reconstitute at 1 mg/mL in sterile PBS.
Reconstitution Buffer Available
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.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: FGF basic
FGF basic is a member of the FGF family of at least 23 related mitogenic proteins which show 35-60% amino acid conservation. FGF acidic and basic, unlike theother members of the family, lack signal peptides and are apparently secreted by mechanisms other than the classical protein secretion pathway. FGF basic hasbeen 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. A variety of forms of FGF basic are producedas a result of Nterminal extensions. These extensions affect localization of FGF basic in cellular compartments but do not affect biological activity. Binding of FGFto 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 thesame high affinity receptors and show a similar range of biological activities. FGF basic stimulates the proliferation of all cells of mesodermal origin and many cellsof neuroectodermal, ectodermal, and endodermal origin. FGF basic induces neuron differentiation, survival, and regeneration. FGF basic also modulates embryonicdevelopment and differentiation. These observed in vitro functions of FGF basic suggest FGF basic may play a role in vivo in the modulation of such normalprocesses 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.
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.
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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Reciprocal cellular cross-talk within the tumor microenvironment promotes oncolytic virus activity.
Authors: Ilkow C, Marguerie M, Batenchuk C, Mayer J, Ben Neriah D, Cousineau S, Falls T, Jennings V, Boileau M, Bellamy D, Bastin D, de Souza C, Alkayyal A, Zhang J, Le Boeuf F, Arulanandam R, Stubbert L, Sampath P, Thorne S, Paramanthan P, Chatterjee A, Strieter R, Burdick M, Addison C, Stojdl D, Atkins H, Auer R, Diallo J, Lichty B, Bell J
Nat Med, 2015;21(5):530-6.
Sample Type: Whole Cells
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