Render Target: SSR
Render Timestamp: 2024-11-14T22:58:11.378Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-09-30 01:54:41.680
Product last modified at: 2024-09-30T08:01:38.444Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

Phospho-FGF Receptor 1 (Tyr766) (1E5) Rabbit mAb #2544

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Transfected Only
    MW (kDa) 120, 145
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-FGF Receptor 1 (Tyr766) (1E5) Rabbit mAb detects transfected levels of FGFR-1 only when phosphorylated at tyrosine 766. The antibody may cross-react with other FGFR family members and some activated protein tyrosine kinases including EGFR and insulin/IGF-I receptors.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr766 of human FGF receptor-1.

    Background

    Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through cell surface receptor tyrosine kinases. There are four members of the FGF receptor family: FGFR1 (flg), FGFR2 (bek, KGFR), FGFR3, and FGFR4. Each receptor contains an extracellular ligand-binding domain, a transmembrane domain, and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR1 can be phosphorylated: Tyr463, 583, 585, 653, 654, 730, and 766. Tyr653 and Tyr654 are important for catalytic activity of activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components, such as Crk and PLCγ (4,5).

    Autophosphorylation of Tyr766 of FGFR1 is critical for phospholipase C (PLC) binding and activation and also plays a role in the negative regulation of FGFR1 activity in vivo (6).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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