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methyl pp2ac  (Santa Cruz Biotechnology)


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    Structured Review

    Santa Cruz Biotechnology methyl pp2ac
    Methyl Pp2ac, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/methyl+pp2ac/methyl-PP2A-C%CE%B1%2F%CE%B2+Antibody/10__3390_slash_biom15091210-89-8-10
    Average 93 stars, based on 21 article reviews
    methyl pp2ac - by Bioz Stars, 2026-10
    93/100 stars

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    Related Articles

    Methylation:

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Quantitation Assay:

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Liquid Chromatography:

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Mass Spectrometry:

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Western Blot:

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Cell Culture:

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Phospho-proteomics:

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Activity Assay:

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Over Expression:

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Transduction:

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Expressing:

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDSPAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.

    Article Title: Carboxy-Methylation of the Catalytic Subunit of Protein Phosphatase 2A (PP2Ac) Integrates Methionine Availability with Methionine Addicted Cancer Cell Proliferation
    Article Snippet: For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.For Western blot analyses, proteins were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane.. Proteins were detected using the following primary antibodies: methyl PP2Ac (Santa Cruz, CA, USA, sc-81603, demethylated PP2Ac (Santa Cruz, CA, USA, sc-13601), total PP2Ac (Proteintech, Rosemont, IL, USA, 13482-1-AP), PARP (Cell Signaling, Danvers, MA, USA, 9542S) Cleaved Caspase-3 (Cell Signaling, 9661S), pS6 (Cell Signaling, 2317S), S6 (Cell Signaling, 4838S), LC3 A/B (Cell Signaling, 4108S), PME-1 (Millipore, MABC1183), p4EBP1 (Cell Signaling, 9459S), 4EBP1 (Cell Signaling, 9452).. Western blot results shown are representative blots from three experiments.Western blot results shown are representative blots from three experiments.



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    Kettenbach GmbH methylated form of pp2ac
    Chronic hypoxia leads to tau hyperphosphorylation, accompanied by loss of LCMT1-related PP2A activity in the hippocampus of rats. ( a , b ) Immunohistochemistry showed an increase in pS396 positive staining in hypoxic rats compared to control (scale bars = 500 μm and 100 μm). ( c – e ) Hippocampal tissues were homogenized, and phosphor-tau protein levels at pS199, pS262, pS396, and pS404 sites were detected by immunoblotting ( c , d ). Total tau level was measured ( e ) with actin as the loading control. ( f , g ) The levels of the total GSK-3β and the Ser9- phosphorylated GSK-3β (s9-GSK-3β), <t>Leu309-methylated</t> (M-PP2Ac), and total PP2Ac (T-PP2Ac) were measured by Western blotting. ( h ) PP2A activity assay in different groups in rat hippocampus. ( i – k ) The levels of PP2Ac-specific PME-1 and LCMT1 were measured by Western blotting. All data are presented as mean ± SD. n = 3 (rats per group). * p < 0.05, ** p < 0.01 vs. control.
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    Expression of the L309Δ mutant in MDCK cells alters PP2A distribution and complex formation with TJ proteins and Par3. (A) Polarized MDCK monolayers were analyzed by confocal microscopy for the distribution of WTC and L309Δ using anti-HA antibodies. Representative apical x-y and transversal x-z sections are shown; the arrow indicates the monolayer thickness. (B) Representative distribution of PP2A-Bα in MDCK-WTC and MDCK-L309Δ cells 20 h after a Ca 2+ switch. (C) Western blot analysis of <t>HA-PP2Ac</t> and PP2A-Bα in total lysates and NP40-detergent-insoluble fractions prepared from MDCK-WTC and MDCK-L309Δ cells cultured in NC medium. Sodium potassium pump (Na,K-ATPase), membrane marker. (D) Western blot analyses of ZO-1 and occludin in total lysates and HA-immunoprecipitates (IP) prepared from MDCK cells transfected with WTC, L309Δ, or empty vector (EV). (E) Western blot analyses of endogenous Par3 and aPKCζ in total lysates and HA immunoprecipitates (IP) prepared from WTC-, L309Δ- or EV-, transfected MDCK cells. (F) Western blot analyses of myc-Par3 and HA-PP2Ac in total lysates and corresponding myc immunoprecipitates (IP) prepared from MDCK-Par3 cells stably expressing myc-Par3, that were transfected with either WTC, L309Δ, or EV. IgG, immunoglobulin. For (A–F) , similar results were obtained in three separate experiments. Scale bars = 10 μm.
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    Expression of the L309Δ mutant in MDCK cells alters PP2A distribution and complex formation with TJ proteins and Par3. (A) Polarized MDCK monolayers were analyzed by confocal microscopy for the distribution of WTC and L309Δ using anti-HA antibodies. Representative apical x-y and transversal x-z sections are shown; the arrow indicates the monolayer thickness. (B) Representative distribution of PP2A-Bα in MDCK-WTC and MDCK-L309Δ cells 20 h after a Ca 2+ switch. (C) Western blot analysis of <t>HA-PP2Ac</t> and PP2A-Bα in total lysates and NP40-detergent-insoluble fractions prepared from MDCK-WTC and MDCK-L309Δ cells cultured in NC medium. Sodium potassium pump (Na,K-ATPase), membrane marker. (D) Western blot analyses of ZO-1 and occludin in total lysates and HA-immunoprecipitates (IP) prepared from MDCK cells transfected with WTC, L309Δ, or empty vector (EV). (E) Western blot analyses of endogenous Par3 and aPKCζ in total lysates and HA immunoprecipitates (IP) prepared from WTC-, L309Δ- or EV-, transfected MDCK cells. (F) Western blot analyses of myc-Par3 and HA-PP2Ac in total lysates and corresponding myc immunoprecipitates (IP) prepared from MDCK-Par3 cells stably expressing myc-Par3, that were transfected with either WTC, L309Δ, or EV. IgG, immunoglobulin. For (A–F) , similar results were obtained in three separate experiments. Scale bars = 10 μm.
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    Chronic hypoxia leads to tau hyperphosphorylation, accompanied by loss of LCMT1-related PP2A activity in the hippocampus of rats. ( a , b ) Immunohistochemistry showed an increase in pS396 positive staining in hypoxic rats compared to control (scale bars = 500 μm and 100 μm). ( c – e ) Hippocampal tissues were homogenized, and phosphor-tau protein levels at pS199, pS262, pS396, and pS404 sites were detected by immunoblotting ( c , d ). Total tau level was measured ( e ) with actin as the loading control. ( f , g ) The levels of the total GSK-3β and the Ser9- phosphorylated GSK-3β (s9-GSK-3β), Leu309-methylated (M-PP2Ac), and total PP2Ac (T-PP2Ac) were measured by Western blotting. ( h ) PP2A activity assay in different groups in rat hippocampus. ( i – k ) The levels of PP2Ac-specific PME-1 and LCMT1 were measured by Western blotting. All data are presented as mean ± SD. n = 3 (rats per group). * p < 0.05, ** p < 0.01 vs. control.

    Journal: International Journal of Molecular Sciences

    Article Title: HIF-1α Causes LCMT1/PP2A Deficiency and Mediates Tau Hyperphosphorylation and Cognitive Dysfunction during Chronic Hypoxia

    doi: 10.3390/ijms232416140

    Figure Lengend Snippet: Chronic hypoxia leads to tau hyperphosphorylation, accompanied by loss of LCMT1-related PP2A activity in the hippocampus of rats. ( a , b ) Immunohistochemistry showed an increase in pS396 positive staining in hypoxic rats compared to control (scale bars = 500 μm and 100 μm). ( c – e ) Hippocampal tissues were homogenized, and phosphor-tau protein levels at pS199, pS262, pS396, and pS404 sites were detected by immunoblotting ( c , d ). Total tau level was measured ( e ) with actin as the loading control. ( f , g ) The levels of the total GSK-3β and the Ser9- phosphorylated GSK-3β (s9-GSK-3β), Leu309-methylated (M-PP2Ac), and total PP2Ac (T-PP2Ac) were measured by Western blotting. ( h ) PP2A activity assay in different groups in rat hippocampus. ( i – k ) The levels of PP2Ac-specific PME-1 and LCMT1 were measured by Western blotting. All data are presented as mean ± SD. n = 3 (rats per group). * p < 0.05, ** p < 0.01 vs. control.

    Article Snippet: M-PP2Ac , Anti-Methylated PP2Ac at Leu309 , mAb , 1:500 for WB , Millipore (041479).

    Techniques: Activity Assay, Immunohistochemistry, Staining, Control, Western Blot, Methylation

    Primary antibodies.

    Journal: International Journal of Molecular Sciences

    Article Title: HIF-1α Causes LCMT1/PP2A Deficiency and Mediates Tau Hyperphosphorylation and Cognitive Dysfunction during Chronic Hypoxia

    doi: 10.3390/ijms232416140

    Figure Lengend Snippet: Primary antibodies.

    Article Snippet: M-PP2Ac , Anti-Methylated PP2Ac at Leu309 , mAb , 1:500 for WB , Millipore (041479).

    Techniques:

    Expression of the L309Δ mutant in MDCK cells alters PP2A distribution and complex formation with TJ proteins and Par3. (A) Polarized MDCK monolayers were analyzed by confocal microscopy for the distribution of WTC and L309Δ using anti-HA antibodies. Representative apical x-y and transversal x-z sections are shown; the arrow indicates the monolayer thickness. (B) Representative distribution of PP2A-Bα in MDCK-WTC and MDCK-L309Δ cells 20 h after a Ca 2+ switch. (C) Western blot analysis of HA-PP2Ac and PP2A-Bα in total lysates and NP40-detergent-insoluble fractions prepared from MDCK-WTC and MDCK-L309Δ cells cultured in NC medium. Sodium potassium pump (Na,K-ATPase), membrane marker. (D) Western blot analyses of ZO-1 and occludin in total lysates and HA-immunoprecipitates (IP) prepared from MDCK cells transfected with WTC, L309Δ, or empty vector (EV). (E) Western blot analyses of endogenous Par3 and aPKCζ in total lysates and HA immunoprecipitates (IP) prepared from WTC-, L309Δ- or EV-, transfected MDCK cells. (F) Western blot analyses of myc-Par3 and HA-PP2Ac in total lysates and corresponding myc immunoprecipitates (IP) prepared from MDCK-Par3 cells stably expressing myc-Par3, that were transfected with either WTC, L309Δ, or EV. IgG, immunoglobulin. For (A–F) , similar results were obtained in three separate experiments. Scale bars = 10 μm.

    Journal: Frontiers in Cell and Developmental Biology

    Article Title: A Novel Role of PP2A Methylation in the Regulation of Tight Junction Assembly and Integrity

    doi: 10.3389/fcell.2022.911279

    Figure Lengend Snippet: Expression of the L309Δ mutant in MDCK cells alters PP2A distribution and complex formation with TJ proteins and Par3. (A) Polarized MDCK monolayers were analyzed by confocal microscopy for the distribution of WTC and L309Δ using anti-HA antibodies. Representative apical x-y and transversal x-z sections are shown; the arrow indicates the monolayer thickness. (B) Representative distribution of PP2A-Bα in MDCK-WTC and MDCK-L309Δ cells 20 h after a Ca 2+ switch. (C) Western blot analysis of HA-PP2Ac and PP2A-Bα in total lysates and NP40-detergent-insoluble fractions prepared from MDCK-WTC and MDCK-L309Δ cells cultured in NC medium. Sodium potassium pump (Na,K-ATPase), membrane marker. (D) Western blot analyses of ZO-1 and occludin in total lysates and HA-immunoprecipitates (IP) prepared from MDCK cells transfected with WTC, L309Δ, or empty vector (EV). (E) Western blot analyses of endogenous Par3 and aPKCζ in total lysates and HA immunoprecipitates (IP) prepared from WTC-, L309Δ- or EV-, transfected MDCK cells. (F) Western blot analyses of myc-Par3 and HA-PP2Ac in total lysates and corresponding myc immunoprecipitates (IP) prepared from MDCK-Par3 cells stably expressing myc-Par3, that were transfected with either WTC, L309Δ, or EV. IgG, immunoglobulin. For (A–F) , similar results were obtained in three separate experiments. Scale bars = 10 μm.

    Article Snippet: Antibodies used in this study included: Mouse (clone 16B12, Covance) and rabbit (clone C29F4, Cell Signaling Technology) anti-HA; mouse anti-Myc (clone 9B11, Cell Signaling Technology); mouse anti-methyl PP2Ac (clone 2A10, Merck Millipore); mouse anti-demethyl-PP2Ac (clone 1D6; Merck Millipore); mouse anti-PP2Ac (#610556, BD Transduction); mouse anti-LCMT1 clone 4A4 (Merck Millipore); mouse anti-PME-1 ( ); rabbit ( ) and mouse (clone 2G9, Merck Millipore) anti-Bα; rabbit anti-Na + /K + ATPase (#3010, Cell Signaling Technology); mouse anti-occludin (clone OC-3F10; Thermo Fisher Scientific); mouse anti-ZO-1 (clone ZO1-1A12, Thermo Fisher Scientific); rabbit anti-Par3 (#07-330, Merck-Millipore); rabbit anti-aPKCζ (sc-216, Santa Cruz Biotechnology); mouse (clone C4, Merck Millipore) and rabbit (#AAN01, Cytoskeleton Inc.) anti-actin; mouse anti-α-tubulin (clone DM1A; Sigma).

    Techniques: Expressing, Mutagenesis, Confocal Microscopy, Western Blot, Cell Culture, Membrane, Marker, Transfection, Plasmid Preparation, Stable Transfection

    Overexpression of LCMT1 and PME1 in MDCK cells affects the initial redistribution of ZO-1, occludin and Par3 to cell-cell contacts during Ca 2+ -induced TJ reassembly. (A) Total lysates from MDCK-LCMT1 and control MDCK cells were analyzed by Western blot (left) for HA-LCMT1, LCMT1, PP2A-Bα, and total/methylated/demethylated PP2Ac levels. Relative expression levels (right) of PP2A-Bα and methylated PP2Ac were quantified in these cells (mean ± SEM; n = 3; Student’s t -test; *** p < 0.001). (B) Representative immunoblots of myc-PME1, PME1, PP2A-Bα, and total/methylated/demethylated PP2Ac levels in total lysates from MDCK-PME1 and control MDCK cells (left). The relative levels of demethylated PP2Ac (mean ± SEM; n = 3; Student’s t -test; *** p < 0.001) were quantified in these cells (right). (C) Distribution of ZO-1, occludin and Par3 in control MDCK and MDCK-LCMT1 cells 3 h after a Ca 2+ switch. A subset of MDCK-LCMT1 cells was incubated with 100 nM OA (+OA) during the switch. (D) Distribution of ZO-1, occludin and Par3 in control MDCK and MDCK-PME1 cells switched for 2 h from LC to NC medium. For (C–D) , representative images from three separate experiments are shown. Scale bars = 10 μm.

    Journal: Frontiers in Cell and Developmental Biology

    Article Title: A Novel Role of PP2A Methylation in the Regulation of Tight Junction Assembly and Integrity

    doi: 10.3389/fcell.2022.911279

    Figure Lengend Snippet: Overexpression of LCMT1 and PME1 in MDCK cells affects the initial redistribution of ZO-1, occludin and Par3 to cell-cell contacts during Ca 2+ -induced TJ reassembly. (A) Total lysates from MDCK-LCMT1 and control MDCK cells were analyzed by Western blot (left) for HA-LCMT1, LCMT1, PP2A-Bα, and total/methylated/demethylated PP2Ac levels. Relative expression levels (right) of PP2A-Bα and methylated PP2Ac were quantified in these cells (mean ± SEM; n = 3; Student’s t -test; *** p < 0.001). (B) Representative immunoblots of myc-PME1, PME1, PP2A-Bα, and total/methylated/demethylated PP2Ac levels in total lysates from MDCK-PME1 and control MDCK cells (left). The relative levels of demethylated PP2Ac (mean ± SEM; n = 3; Student’s t -test; *** p < 0.001) were quantified in these cells (right). (C) Distribution of ZO-1, occludin and Par3 in control MDCK and MDCK-LCMT1 cells 3 h after a Ca 2+ switch. A subset of MDCK-LCMT1 cells was incubated with 100 nM OA (+OA) during the switch. (D) Distribution of ZO-1, occludin and Par3 in control MDCK and MDCK-PME1 cells switched for 2 h from LC to NC medium. For (C–D) , representative images from three separate experiments are shown. Scale bars = 10 μm.

    Article Snippet: Antibodies used in this study included: Mouse (clone 16B12, Covance) and rabbit (clone C29F4, Cell Signaling Technology) anti-HA; mouse anti-Myc (clone 9B11, Cell Signaling Technology); mouse anti-methyl PP2Ac (clone 2A10, Merck Millipore); mouse anti-demethyl-PP2Ac (clone 1D6; Merck Millipore); mouse anti-PP2Ac (#610556, BD Transduction); mouse anti-LCMT1 clone 4A4 (Merck Millipore); mouse anti-PME-1 ( ); rabbit ( ) and mouse (clone 2G9, Merck Millipore) anti-Bα; rabbit anti-Na + /K + ATPase (#3010, Cell Signaling Technology); mouse anti-occludin (clone OC-3F10; Thermo Fisher Scientific); mouse anti-ZO-1 (clone ZO1-1A12, Thermo Fisher Scientific); rabbit anti-Par3 (#07-330, Merck-Millipore); rabbit anti-aPKCζ (sc-216, Santa Cruz Biotechnology); mouse (clone C4, Merck Millipore) and rabbit (#AAN01, Cytoskeleton Inc.) anti-actin; mouse anti-α-tubulin (clone DM1A; Sigma).

    Techniques: Over Expression, Control, Western Blot, Methylation, Expressing, Incubation

    Endogenous PME1-mediated PP2A demethylation is enhanced during early Ca 2+ -induced TJ formation in MDCK cells. (A) Endogenous demethylated PP2Ac levels were analyzed by immunoblotting (top) and quantified (bottom) in MDCK cells switched for 0, 1 and 4 h from LC to NC medium. Data (mean ± SD) were appraised using one-way ANOVA (F = 168.8; p < 0.0001) with post hoc Dunnett’s multiple comparisons test. **** p < 0.0001. (B) Representative distribution of ZO-1, occludin and Par3 in MDCK cells incubated for 4 h with either 20 μM AMZ-30 or vehicle during a Ca 2+ switch. Similar results were obtained in three separate experiments. Scale bar = 10 μm. (C) Relative levels of demethylated PP2Ac were quantified in these cells (mean ± SEM; n = 3; Student’s t -test; **** p < 0.0001).

    Journal: Frontiers in Cell and Developmental Biology

    Article Title: A Novel Role of PP2A Methylation in the Regulation of Tight Junction Assembly and Integrity

    doi: 10.3389/fcell.2022.911279

    Figure Lengend Snippet: Endogenous PME1-mediated PP2A demethylation is enhanced during early Ca 2+ -induced TJ formation in MDCK cells. (A) Endogenous demethylated PP2Ac levels were analyzed by immunoblotting (top) and quantified (bottom) in MDCK cells switched for 0, 1 and 4 h from LC to NC medium. Data (mean ± SD) were appraised using one-way ANOVA (F = 168.8; p < 0.0001) with post hoc Dunnett’s multiple comparisons test. **** p < 0.0001. (B) Representative distribution of ZO-1, occludin and Par3 in MDCK cells incubated for 4 h with either 20 μM AMZ-30 or vehicle during a Ca 2+ switch. Similar results were obtained in three separate experiments. Scale bar = 10 μm. (C) Relative levels of demethylated PP2Ac were quantified in these cells (mean ± SEM; n = 3; Student’s t -test; **** p < 0.0001).

    Article Snippet: Antibodies used in this study included: Mouse (clone 16B12, Covance) and rabbit (clone C29F4, Cell Signaling Technology) anti-HA; mouse anti-Myc (clone 9B11, Cell Signaling Technology); mouse anti-methyl PP2Ac (clone 2A10, Merck Millipore); mouse anti-demethyl-PP2Ac (clone 1D6; Merck Millipore); mouse anti-PP2Ac (#610556, BD Transduction); mouse anti-LCMT1 clone 4A4 (Merck Millipore); mouse anti-PME-1 ( ); rabbit ( ) and mouse (clone 2G9, Merck Millipore) anti-Bα; rabbit anti-Na + /K + ATPase (#3010, Cell Signaling Technology); mouse anti-occludin (clone OC-3F10; Thermo Fisher Scientific); mouse anti-ZO-1 (clone ZO1-1A12, Thermo Fisher Scientific); rabbit anti-Par3 (#07-330, Merck-Millipore); rabbit anti-aPKCζ (sc-216, Santa Cruz Biotechnology); mouse (clone C4, Merck Millipore) and rabbit (#AAN01, Cytoskeleton Inc.) anti-actin; mouse anti-α-tubulin (clone DM1A; Sigma).

    Techniques: Western Blot, Incubation

    Hcy, HTL and SAM metabolites modulate PP2A methylation state and TJ assembly. (A) Total and demethylated PP2Ac were analyzed by Western blot (top) in total lysates from MDCK cells incubated for 24 h in NC medium in the presence of either 100 μM Hcy, 100 μM HTL, 100 μM SAM, or vehicle. Demethylated PP2Ac levels were quantified in these cells (bottom). Data (mean ± SEM; n = 3) were appraised using one-way ANOVA (F = 150.6; p < 0.0001) with post hoc Dunnett’s test. **** p < 0.0001, *** p < 0.001, versus vehicle-treated controls. (B) Distribution of ZO-1, occludin and Par3 in these cells. Arrows indicate examples of ruffled TJs. (C) Quantification of TJ ruffling in SAM-treated MDCK cells (mean ± SEM; Student’s t -test; **** p < 0.0001). (D) TER values were measured in cells from (B) . Data (mean ± SEM; n = 6 Transwells) were analyzed using one-way ANOVA (F = 42.12; p < 0.0001) with post hoc Dunnett’s multiple comparisons test. **** p < 0.0001, *** p = 0.001, * p < 0.05, versus vehicle-treated control cells. (E) Distribution of ZO-1 and Par3 in MDCK cells switched for 2 h from LC to NC medium in the presence of either 200 μM HTL or vehicle. (F) Distribution of ZO-1 and Par3 in MDCK cells switched for 4 h from LC to NC medium containing either 200 μM Hcy or HTL, together with 20 μM AMZ-30 or vehicle. (G) Distribution of ZO-1 in MDCK-LCMT1 cells switched for 4 h from LC to NC medium in the presence of either 200 μM SAM or vehicle. For (B,E–G) , representative confocal images are shown; similar results were obtained in three separate experiments. Scale bars = 10 μm.

    Journal: Frontiers in Cell and Developmental Biology

    Article Title: A Novel Role of PP2A Methylation in the Regulation of Tight Junction Assembly and Integrity

    doi: 10.3389/fcell.2022.911279

    Figure Lengend Snippet: Hcy, HTL and SAM metabolites modulate PP2A methylation state and TJ assembly. (A) Total and demethylated PP2Ac were analyzed by Western blot (top) in total lysates from MDCK cells incubated for 24 h in NC medium in the presence of either 100 μM Hcy, 100 μM HTL, 100 μM SAM, or vehicle. Demethylated PP2Ac levels were quantified in these cells (bottom). Data (mean ± SEM; n = 3) were appraised using one-way ANOVA (F = 150.6; p < 0.0001) with post hoc Dunnett’s test. **** p < 0.0001, *** p < 0.001, versus vehicle-treated controls. (B) Distribution of ZO-1, occludin and Par3 in these cells. Arrows indicate examples of ruffled TJs. (C) Quantification of TJ ruffling in SAM-treated MDCK cells (mean ± SEM; Student’s t -test; **** p < 0.0001). (D) TER values were measured in cells from (B) . Data (mean ± SEM; n = 6 Transwells) were analyzed using one-way ANOVA (F = 42.12; p < 0.0001) with post hoc Dunnett’s multiple comparisons test. **** p < 0.0001, *** p = 0.001, * p < 0.05, versus vehicle-treated control cells. (E) Distribution of ZO-1 and Par3 in MDCK cells switched for 2 h from LC to NC medium in the presence of either 200 μM HTL or vehicle. (F) Distribution of ZO-1 and Par3 in MDCK cells switched for 4 h from LC to NC medium containing either 200 μM Hcy or HTL, together with 20 μM AMZ-30 or vehicle. (G) Distribution of ZO-1 in MDCK-LCMT1 cells switched for 4 h from LC to NC medium in the presence of either 200 μM SAM or vehicle. For (B,E–G) , representative confocal images are shown; similar results were obtained in three separate experiments. Scale bars = 10 μm.

    Article Snippet: Antibodies used in this study included: Mouse (clone 16B12, Covance) and rabbit (clone C29F4, Cell Signaling Technology) anti-HA; mouse anti-Myc (clone 9B11, Cell Signaling Technology); mouse anti-methyl PP2Ac (clone 2A10, Merck Millipore); mouse anti-demethyl-PP2Ac (clone 1D6; Merck Millipore); mouse anti-PP2Ac (#610556, BD Transduction); mouse anti-LCMT1 clone 4A4 (Merck Millipore); mouse anti-PME-1 ( ); rabbit ( ) and mouse (clone 2G9, Merck Millipore) anti-Bα; rabbit anti-Na + /K + ATPase (#3010, Cell Signaling Technology); mouse anti-occludin (clone OC-3F10; Thermo Fisher Scientific); mouse anti-ZO-1 (clone ZO1-1A12, Thermo Fisher Scientific); rabbit anti-Par3 (#07-330, Merck-Millipore); rabbit anti-aPKCζ (sc-216, Santa Cruz Biotechnology); mouse (clone C4, Merck Millipore) and rabbit (#AAN01, Cytoskeleton Inc.) anti-actin; mouse anti-α-tubulin (clone DM1A; Sigma).

    Techniques: Methylation, Western Blot, Incubation, Control

    Antibodies used in this study

    Journal: Neurotherapeutics

    Article Title: Direct Activation of Protein Phosphatase 2A (PP2A) by Tricyclic Sulfonamides Ameliorates Alzheimer’s Disease Pathogenesis in Cell and Animal Models

    doi: 10.1007/s13311-020-00841-6

    Figure Lengend Snippet: Antibodies used in this study

    Article Snippet: Positive control compound SCR1693, a novel tacrine-dihydropyridine hybrid which has been proved to efficiently reduce tau pathology and amyloidosis [ 34 , 35 ], was synthesized by Simovay (Purity: 99.3%; Jiangsu Simovay Pharmaceutical Co., Ltd. Nanjing, China). table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Antibodies Specific Type Dilution Source pT231 Phosphorylated tau at Thr231 pAb 1:1000 for WB Signalway Antibody (CollegePark, MD, USA) pT205 Phosphorylated tau at Thr205 pAb 1:1000 for WB Signalway Antibody (CollegePark, MD, USA) pS199 Phosphorylated tau at Ser199 pAb 1:1000 for WB Thermo Fisher (NY, USA) pS396 Phosphorylated tau at Ser396 pAb 1:1000 for WB Signalway Antibody (CollegePark, MD, USA) pS404 Phosphorylated tau at Ser404 pAb 1:1000 for WB Signalway Antibody (CollegePark, MD, USA) Tau-5 Total tau mAb 1:1000 for WB Millipore (Temecula, CA, USA) APP C-terminal of APP pAb 1:1000 for WB Proteintech (Chicago, IL, USA) sAPPβ Human sAPPβ pAb 1:500 for WB Immuno-Biological Laboratories (Gunma, Japan) pT668 Phosphorylated APP at Thr688 pAb 1:500 for WB Cell Signaling (Danvers, MA, USA) BACE1 BACE1 pAb 1:500 for WB Proteintech (Chicago, IL, USA) PS1 PS1 pAb 1:500 for WB Proteintech (Chicago, IL, USA) PP2Ac PP2A catalytic subunit pAb 1:1000 for WB Cell Signaling (Danvers, MA, USA) pY307-PP2Ac Phosphorylated PP2Ac at Tyr307 pAb 1:500 for WB Santa Cruz (CA,USA) m-PP2Ac Methylated PP2Ac at Leu309 mAb 1:500 for WB Millipore (Temecula, CA, USA) Dm-PP2Ac Demethylated PP2Ac at Leu309 pAb 1:500 for WB Santa Cruz (CA, USA) PSD95 PSD95 N-terminal pAb 1:1000 for WB Cell Signaling (Danvers, MA, USA) GluA1 N-terminal of GluA1 mAb 1:1000 for WB Santa Cruz (CA, USA) GluA2 GluA2 (aa 175–430) pAb 1:1000 for WB Millipore (Billerica, MA, USA) GluN2B GluN2B pAb 1:500 for WB Millipore (Billerica, MA, USA) Synapsin I Synapsin-I C-terminal pAb 1:1000 for WB Millipore (Billerica, MA, USA) Synaptophysin Synaptophysin (aa 250–350) pAb 1:1000 for WB Proteintech (Chicago, IL, USA) GAPDH GAPDH pAb 1:1000 for WB Proteintech (Chicago, IL, USA) Open in a separate window mAb , monoclonal antibody; pAb , polyclonal antibody; WB , Western blotting Antibodies used in this study Cell Culture and Treatment HEK293/tau (HEK293 cells were stably transfected with human Tau 40) cell line was established in our laboratory.

    Techniques: Methylation