|FGF‑5 in Human Placenta. FGF‑5 was detected in immersion fixed paraffin-embedded sections of human placenta using Goat Anti-Human FGF‑5 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF‑237‑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‑5 and Neutralization by Human FGF‑5 Antibody. Recombinant Human FGF‑5 (Catalog # 237-F5) stimulates proliferation in the the NR6R‑3T3 mouse fibroblast cell line in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Human FGF‑5 (20 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human FGF‑5 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF-237-NA). The ND50 is typically 0.2-0.8 µg/mL in the presence of heparin (1 µg/mL).|
The FGF family is comprised of at least seven polypeptides that are potent regulators of cell proliferation, differentiation and function. All FGFs have two conserved cysteine residues and share 30-50% sequence homology at the amino acid level. FGF-5 was originally identified as a transforming gene by the NIH-3T3 focus formation assay using DNA derived from human tumors. FGF-5 cDNA encodes a 267 amino acid residue protein with a putative 22 amino acid residue signal peptide. The murine homologue of FGF-5 was cloned and found to be 84% homologous to the human protein at the amino acid sequence level. Human and murine FGF-5 exhibit cross species activity.
In vitro, recombinant human FGF-5 is a mitogen for Balb/3T3 fibroblasts and bovine heart endothelial cells. FGF-5 was also reported to be a major muscle-derived survival factor for cultured spinal motoneurons. In vivo, FGF-5 is suggested to play important roles in both embryology and neurobiology. Developmentally, FGF-5 mRNA is initially found in the embryoblast followed by the lateral somatic mesoderm, where it may play a role in angiogenesis, plus the myotomes cranial to the tail region, where it may delay terminal myoblast differentiation during cell migration. FGF-5 continues to impact muscle post-natally where it is believed to function as a target-derived neurotrophic factor of skeletal muscle. In the nervous system, FGF-5 has been most often identified in neurons associated with the limbic system, notably in neurons of the olfactory bulb and pyramidal cells of the hippocampus. Hippocampal FGF-5 is suggested to serve as a neurotrophic and differentiative factor for cholinergic and serotonergic neurons projecting to this region.
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