Detects IIIc isoforms of mouse FGF R2 in direct ELISAs and Western blots. Does not react with IIIb isoforms of recombinant mouse (rm) FGF R2. In direct ELISAs and Western blots, 100% cross-reactivity with IIIc isoforms of recombinant human (rh) FGF R2 is observed, and no cross-reactivity with IIIb isoforms of rhFGF R2 or any isoforms of rhFGF R1, rmFGF R3, or rhFGF R4 is observed.
Monoclonal Rat IgG2A Clone # 133706
Protein A or G purified from hybridoma culture supernatant
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.
Recombinant Mouse FGF R2 beta (IIIc) Fc Chimera (Catalog # 716-MF) under non-reducing conditions only
Measured by its ability to neutralize FGF R2 beta -mediated inhibition of proliferation in the NR6R‑3T3 mouse fibroblast cell line. The Neutralization Dose (ND50) is typically 0.1-0.4 µg/mL in the presence of 3 ng/mL Recombinant Mouse FGF R2 beta (IIIc) Fc Chimera, 0.3 ng/mL Recombinant Human FGF acidic, and 10 µg/mL heparin.
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.
FGF R2 beta Inhibition of FGF acidic-dependent Cell Proliferation and Neutralization by Rat Anti-Mouse FGF R2 Antibody. Recombinant Mouse FGF R2 beta (IIIc) Fc Chimera (Catalog # 716-MF) inhibits Recombinant Human FGF acidic (Catalog # 232-FA) induced proliferation in the NR6R‑3T3 mouse fibroblast cell line in a dose-dependent manner (orange line). Inhibition of Recombinant Human FGF acidic (0.3 ng/mL) activity elicited by Recombinant Mouse FGF R2 beta (IIIc) Fc Chimera (3 ng/mL) is neutralized (green line) by increasing concentrations of Rat Anti-Mouse FGF R2 (IIIc) Monoclonal Antibody (Catalog # MAB716). The ND50 is typically 0.1-0.4 µg/mL in the presence of heparin (10 µg/mL).
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
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 R2
Fibroblast growth factors (FGFs) comprise a family of at least eighteen structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorigenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGF R1‑4, are known. All four genes for FGF Rs encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid‑box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain. Multiple forms of FGF R1‑3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGF R1 and 2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the beta isoform. Only the alpha isoform has been identified for FGF R3 and FGF R4. Additional splicing events for FGF R1‑3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGF R1. Mutations in FGF R1‑3 have been found in patients with birth defects involving craniosynostosis. The complex patterns of expression of these receptors as well as the specificity of their interactions with the various FGF ligand family members are under investigation.
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