Render Target: SSR
Render Timestamp: 2024-11-14T22:58:39.172Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-11-12 23:02:08.265
Product last modified at: 2024-11-13T08:01:24.545Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Phospho-IGF-I Receptor β (Tyr1131)/Insulin Receptor β (Tyr1146) (D6D5L) Rabbit mAb #80732

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 95
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100

    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.

    For a carrier free (BSA and azide free) version of this product see product #40223.

    Protocol

    Specificity / Sensitivity

    Phospho-IGF-I Receptor β (Tyr1131)/Insulin Receptor β (Tyr1146) (D6D5L) Rabbit mAb recognizes endogenous levels of IGF-I receptor β protein only when phosphorylated at Tyr1131 and/or insulin receptor β protein only when phosphorylated at Tyr1146. The antibody cross-reacts with activated ErbB2 and ALK.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Tyr1131 of human IGF-I receptor protein.

    Background

    Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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