Detects human FGF acidic in direct ELISAs and Western blots. In direct ELISAs, approximately 100% cross-reactivity with recombinant mouse FGF-acidic is observed, and less than 1% cross-reactivity with recombinant human (rh) FGF-3, rhFGF-4, rhFGF-5, rhFGF-6, rhFGF-7, rhFGF-8, rhFGF-9, rhFGF-10, rhFGF-11, rhFGF-13, rhFGF-17, rhFGF-18, rhFGF-19, and rhFGF basic is observed.
Neutralizes the biological activity of rhFGF acidic. It will also neutralize the biological activity of rh beta -ECGF and bovine FGF acidic, although 2‑3 times the amount of IgG is required to neutralize bovine FGF acidic biological activity.
Polyclonal Goat IgG
E. coli-derived recombinant human FGF acidic Phe16-Asp155 Accession # P05230
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
<0.10 EU per 1 μg of the antibody by the LAL method.
Measured by its ability to neutralize FGF acidic-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 0.25-0.75 µg/mL in the presence of 0.75 ng/mL Recombinant Human FGF acidic aa 16‑155 and 10 µg/mL heparin.
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 acidic and Neutralization by Human FGF acidic Antibody.
Recombinant Human FGF acidic aa 16‑155 (Catalog # 232-FA) stimulates proliferation in the the NR6R‑3T3 mouse fibroblast cell line in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Human FGF acidic aa 16‑155 (0.75 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human FGF acidic Antigen Affinity-purified Polyclonal Antibody (Catalog # AF232). The ND50 is typically 0.25-0.75 µg/mL in the presence of heparin (10 µg/mL).
FGF acidic in Human Breast.
FGF acidic was detected in immersion fixed paraffin-embedded sections of human breast using Goat Anti-Human FGF acidic Antigen Affinity-purified Polyclonal Antibody (Catalog # AF232) at 15 µg/mL overnight at 4 °C. 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 epithelial cells. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
Detection of Human FGF acidic by Western Blot.
Western blot shows lysates of human brain (hypothalamas) tissue and human heart tissue. PVDF membrane was probed with 0.25 µg/mL of Goat Anti-Human FGF acidic Antigen Affinity-purified Polyclonal Antibody (Catalog # AF232) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for FGF acidic at approximately 16-17 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Detection of Human FGF acidic by Simple WesternTM.
Simple Western lane view shows lysates of human brain (hypothalamus) tissue, loaded at 0.2 mg/mL. A specific band was detected for FGF acidic at approximately 25 kDa (as indicated) using 2.5 µg/mL of Goat Anti-Human FGF acidic Antigen Affinity-purified Polyclonal Antibody (Catalog # AF232) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
Preparation and Storage
Reconstitute at 0.2 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. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
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 acidic
FGF acidic, also known as FGF-1, 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). Human FGF acidic shares 54% amino acid sequence identity with FGF basic and 17%‑33% with other human FGFs. It shares 92%, 96%, 96%, and 96% aa sequence identity with bovine, mouse, porcine, and rat FGF acidic, respectively, and exhibits considerable species crossreactivity. Alternate splicing generates a truncated isoform of human FGF acidic that consists of the N-terminal 40% of the molecule and functions as a receptor antagonist (4). During its nonclassical secretion, FGF acidic associates with S100A13, copper ions, and the C2A domain of synaptotagmin 1 (5). It is released extracellularly as a disulfide-linked homodimer and is stored in complex with extracellular heparan sulfate (6). The ability of heparan sulfate to bind FGF acidic is determined by its pattern of sulfation, and alterations in this pattern during embryogenesis thereby regulate FGF acidic bioactivity (7). The association of FGF acidic with heparan sulfate is a prerequisite for its subsequent interaction with FGF receptors (8, 9). Ligation triggers receptor dimerization, transphosphorylation, and internalization of receptor/FGF complexes (10). 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 (11 - 13). The phosphorylation of FGF acidic by nuclear PKC delta triggers its active export to the cytosol where it is dephosphorylated and degraded (14, 15). Intracellular FGF acidic functions as a survival factor by inhibiting p53 activity and proapoptotic signaling (16).
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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.
Molecular profiling of cervical cancer progression.
Authors: Hagemann T, Bozanovic T, Hooper S, Ljubic A, Slettenaar VI, Wilson JL, Singh N, Gayther SA, Shepherd JH, Van Trappen PO
Br. J. Cancer, 2007;96(2):321-8.
Sample Type: Whole Tissue
Application: IHC Paraffin-embedded
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