Bovine FGF acidic/FGF1 Antibody Summary
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Cell Proliferation Induced by FGF acidic/FGF1 and Neutral-ization by Bovine FGF acidic/FGF1 Antibody. Bovine FGF acidic/FGF1 (Catalog # 132-FA) stimulates proliferation in the NR6R-3T3 mouse fibroblast cell line in a dose-dependent manner (orange line). Proliferation elicited by Bovine FGF acidic/FGF1 (0.75 ng/mL) is neutralized (green line) by increasing concentrations of Rabbit Anti-Bovine FGF acidic/FGF1 Polyclonal Antibody (Catalog # AB-32-NA). The ND50 is typically 1-3 µg/mL.
Reconstitution Calculator
Preparation and Storage
- 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 acidic/FGF1
FGF acidic, also known as FGF1, ECGF, and HBGF-1, is a 17 kDa nonglycosylated member of the FGF family of mitogenic peptides. FGF acidic, which is produced by multiple cell types, stimulates the proliferation of all cells of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin. It plays a number of roles in development, regeneration, and angiogenesis (1‑3). Bovine FGF acidic shares 53% amino acid sequence identity with FGF basic and 11%‑31% with other bovine FGFs. It shares 92%, 91%, 88%, and 91% aa sequence identity with human, mouse, porcine, and rat FGF acidic, respectively, and exhibits considerable species crossreactivity. During its nonclassical secretion, FGF acidic associates with S100A13, copper ions, and the C2A domain of synaptotagmin 1 (4). It is released extracellularly as a disulfide-linked homodimer and is stored in complex with extracellular heparan sulfate (5). The ability of heparan sulfate to bind FGF acidic is determined by its pattern of sulfation, and alterations in this pattern during embryognesis thereby regulate FGF acidic bioactivity (6). The association of FGF acidic with heparan sulfate is a prerequisite for its subsequent interaction with FGF receptors (7, 8). Ligation triggers receptor dimerization, transphosphorylation, and internalization of receptor/FGF complexes (9). Internalized FGF acidic can translocate to the cytosol with the assistance of Hsp90 and then migrate to the nucleus by means of its two nuclear localization signals (10‑12). The phosphorylation of FGF acidic by nuclear PKC delta triggers its active export to the cytosol where it is dephosphorylated and degraded (13, 14). Intracellular FGF acidic functions as a survival factor by inhibiting p53 activity and proapoptotic signaling (15).
- Gimenez-Gallego, G. et al. (1985) Science 230:1385.
- Galzie, Z. et al. (1997) Biochem. Cell Biol. 75:669.
- Presta, M. et al. (2005) Cytokine Growth Factor Rev. 16:159.
- Rajalingam, D. et al. (2007) Biochemistry 46:9225.
- Guerrini, M. et al. (2007) Curr. Pharm. Des. 13:2045.
- Allen, B.L. and A.C. Rapraeger (2003) J. Cell Biol. 163:637.
- Robinson, C.J. et al. (2005) J. Biol. Chem. 280:42274.
- Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
- Wiedlocha, A. and V. Sorensen (2004) Curr. Top. Microbiol. Immunol. 286:45.
- Wesche, J. et al. (2006) J. Biol. Chem. 281:11405.
- Imamura, T. et al. (1990) Science 249:1567.
- Wesche, J. et al. (2005) Biochemistry 44:6071.
- Wiedlocha, A. et al. (2005) Mol. Biol. Cell 16:794.
- Nilsen, T. et al. (2007) J. Biol. Chem. 282:26245.
- Bouleau, S. et al. (2005) Oncogene 24:7839.
Product Datasheets
Citations for Bovine FGF acidic/FGF1 Antibody
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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FGF1 protects neuroblastoma SH-SY5Y cells from p53-dependent apoptosis through an intracrine pathway regulated by FGF1 phosphorylation
Authors: C Pirou, F Montazer-T, N Jah, E Delmas, C Lasbleiz, B Mignotte, F Renaud
Cell Death Dis, 2017-08-31;8(8):e3023.
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FGF1 C-terminal domain and phosphorylation regulate intracrine FGF1 signaling for its neurotrophic and anti-apoptotic activities
Authors: E Delmas, N Jah, C Pirou, S Bouleau, N Le Floch, J-L Vayssière et al.
Cell Death & Disease
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Human FGF-1 gene transfer promotes the formation of collateral vessels and arterioles in ischemic muscles of hypercholesterolemic hamsters.
Authors: Caron A, Michelet S, Caron A, Sordello S, Ivanov MA, Delaere P, Branellec D, Schwartz B, Emmanuel F
J Gene Med, 2004-09-01;6(9):1033-45.
Species: Hamster
Sample Types: Whole Tissue
Applications: IHC-P
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