Render Target: SSR
Render Timestamp: 2024-10-24T19:49:08.160Z
Commit: 56767fe525c928647c8401233a175d0d607d385d
XML generation date: 2024-09-30 01:57:20.069
Product last modified at: 2024-10-17T11:45:14.752Z
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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-PI3 Kinase p85 (Tyr458)/p55 (Tyr199) (E3U1H) Rabbit mAb #17366

Filter:
  • WB
  • IP
  • F

    Supporting Data

    REACTIVITY M
    SENSITIVITY Endogenous
    MW (kDa) 60, 85
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • F-Flow Cytometry 
    Species Cross-Reactivity Key:
    • M-Mouse 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100
    Flow Cytometry (Fixed/Permeabilized) 1:50 - 1:200

    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-PI3 Kinase p85 (Tyr458)/p55 (Tyr199) (E3U1H) Rabbit mAb recognizes endogenous levels of p85/p55 protein only when phosphorylated at Tyr467/Tyr199 (Tyr458/Tyr199 in mouse).

    Species Reactivity:

    Mouse

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr467 (equivalent to Tyr458 in mouse) of human p85α protein.

    Background

    Phosphoinositide 3-kinase (PI3K) catalyzes the production of phosphatidylinositol-3,4,5-triphosphate by phosphorylating phosphatidylinositol (PI), phosphatidylinositol-4-phosphate (PIP), and phosphatidylinositol-4,5-bisphosphate (PIP2). Growth factors and hormones trigger this phosphorylation event, which in turn coordinates cell growth, cell cycle entry, cell migration, and cell survival (1). PTEN reverses this process, and research studies have shown that the PI3K signaling pathway is constitutively activated in human cancers that have loss of function of PTEN (2). PI3Ks are composed of a catalytic subunit (p110) and a regulatory subunit. Various isoforms of the catalytic subunit (p110α, p110β, p110γ, and p110δ) have been isolated, and the regulatory subunits that associate with p110α, p110β, and p110δ are p85α and p85β (3). In contrast, p110γ associates with a p101 regulatory subunit that is unrelated to p85. Furthermore, p110γ is activated by βγ subunits of heterotrimeric G proteins (4).
    Protein extracts from 3T3-Src cells were profiled by PhosphoScan® to identify phosphotyrosine peptides. Tyr458 of PI3K p85 and Tyr199 of PI3K p55 were among 180 phosphopeptides and 185 phosphotyrosine sites identified (5).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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