|FGF basic in Human Placenta. FGF basic was detected in immersion fixed paraffin-embedded sections of human placenta using Goat Anti-Human FGF basic Antigen Affinity-purified Polyclonal Antibody (Catalog # AF‑233‑NA) at 10 µg/mL overnight at 4 °C. Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (Catalog # CTS013). Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to trophoblast cells in chorionic villi. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
|Cell Proliferation Induced by FGF basic and Neutralization by Human FGF basic Antibody. Bovine FGF basic (Catalog # 133-FB) stimulates proliferation in the NR6R‑3T3 mouse fibroblast cell line in a dose-dependent manner (orange line). Proliferation elicited by Bovine FGF basic (0.5 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human FGF basic Antigen Affinity-purified Polyclonal Antibody (Catalog # AF-233-NA). The ND50 is typically 0.08‑0.4 µg/mL.|
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 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. 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. 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. FGF basic induces neuron differentiation, survival, and regeneration. FGF basic also modulates 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.
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