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p- pkc- substrate 2261 antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p- pkc- substrate 2261 antibody
    P Pkc Substrate 2261 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p- pkc- substrate 2261 antibody/product/Cell Signaling Technology Inc
    Average 90 stars, based on 1 article reviews
    p- pkc- substrate 2261 antibody - by Bioz Stars, 2026-03
    90/100 stars

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    PTEN is a protein phosphatase for PKCδ in vitro (A) Purified PTEN proteins were used in a phosphatase assay in vitro using PKCδ as a substrate. The reaction was run for the described time interval. Changes in PKCδ phosphorylation at Y311, T505, and <t>S643</t> were detected by immunoblotting. (B) Western blot showed PKCδ phosphorylation levels in a phosphatase assay in vitro using PKCδ as a substrate following the increased PTEN. The value of western blot band density was quantified by ImageJ analysis. After normalization with the value of PKCδ, the fold changes were presented to compare with 0 time point (0). (C) Western blot showed PKCδ phosphorylation levels in a phosphatase assay in vitro using PKCδ as a substrate following the increased PTEN with/without a phosphatase inhibitor. The value of western blot band density was quantified by ImageJ analysis. After normalization with the value of PKCδ, the fold change was presented to compare with 0 ng PTEN (0).
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    Image Search Results


    PTEN is a protein phosphatase for PKCδ in vitro (A) Purified PTEN proteins were used in a phosphatase assay in vitro using PKCδ as a substrate. The reaction was run for the described time interval. Changes in PKCδ phosphorylation at Y311, T505, and S643 were detected by immunoblotting. (B) Western blot showed PKCδ phosphorylation levels in a phosphatase assay in vitro using PKCδ as a substrate following the increased PTEN. The value of western blot band density was quantified by ImageJ analysis. After normalization with the value of PKCδ, the fold changes were presented to compare with 0 time point (0). (C) Western blot showed PKCδ phosphorylation levels in a phosphatase assay in vitro using PKCδ as a substrate following the increased PTEN with/without a phosphatase inhibitor. The value of western blot band density was quantified by ImageJ analysis. After normalization with the value of PKCδ, the fold change was presented to compare with 0 ng PTEN (0).

    Journal: iScience

    Article Title: PTEN protein phosphatase activity regulates metastasis by targeting PKCδ

    doi: 10.1016/j.isci.2025.112741

    Figure Lengend Snippet: PTEN is a protein phosphatase for PKCδ in vitro (A) Purified PTEN proteins were used in a phosphatase assay in vitro using PKCδ as a substrate. The reaction was run for the described time interval. Changes in PKCδ phosphorylation at Y311, T505, and S643 were detected by immunoblotting. (B) Western blot showed PKCδ phosphorylation levels in a phosphatase assay in vitro using PKCδ as a substrate following the increased PTEN. The value of western blot band density was quantified by ImageJ analysis. After normalization with the value of PKCδ, the fold changes were presented to compare with 0 time point (0). (C) Western blot showed PKCδ phosphorylation levels in a phosphatase assay in vitro using PKCδ as a substrate following the increased PTEN with/without a phosphatase inhibitor. The value of western blot band density was quantified by ImageJ analysis. After normalization with the value of PKCδ, the fold change was presented to compare with 0 ng PTEN (0).

    Article Snippet: anti- p -PKC S643 , Cell Signaling , Cat# 9376, RRID: AB_2168834.

    Techniques: In Vitro, Purification, Phosphatase Assay, Phospho-proteomics, Western Blot