Render Target: STATIC
Render Timestamp: 2024-11-05T09:58:28.063Z
Commit: 57f6e368eba1a427377652f2ad915d45d7f340a4
XML generation date: 2024-08-01 15:25:57.094
Product last modified at: 2024-10-15T21:45:07.766Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-GSK-3β (Thr390) Antibody #3548

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 46
    SOURCE Rabbit
    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 and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-GSK-3β (Thr390) Antibody detects endogenous levels of human GSK-3β protein only when phosphorylated at Thr390.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr390 of human GSK-3β. Antibodies are purified by peptide affinity chromatography.

    Background

    Glycogen synthase kinase-3 (GSK-3) was initially identified as an enzyme that regulates glycogen synthesis in response to insulin (1). GSK-3 is a ubiquitously expressed serine/threonine protein kinase that phosphorylates and inactivates glycogen synthase. GSK-3 is a critical downstream element of the PI3K/Akt cell survival pathway whose activity can be inhibited by Akt-mediated phosphorylation at Ser21 of GSK-3α and Ser9 of GSK-3β (2,3). GSK-3 has been implicated in the regulation of cell fate in Dictyostelium and is a component of the Wnt signaling pathway required for Drosophila, Xenopus, and mammalian development (4). GSK-3 has been shown to regulate cyclin D1 proteolysis and subcellular localization (5).
    The phosphorylation of GSK-3β at Thr390 was found to be a possible substrate of p38 MAPK and was reported by several labs using phosphoproteomic analysis on mitotic cell extracts (6-10). Phosphorylation of this site was also identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for modification site discovery (11). Please visit PhosphoSitePlus®, CST's modification site knowledgebase, at www.phosphosite.org for more information.
    For Research Use Only. Not For Use In Diagnostic Procedures.
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