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proteins stat 1  (Cusabio)


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    Cusabio proteins stat 1
    Proteins Stat 1, supplied by Cusabio, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/proteins stat 1/product/Cusabio
    Average 93 stars, based on 6 article reviews
    proteins stat 1 - by Bioz Stars, 2026-03
    93/100 stars

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    Effects of AGS on protein phosphatase 2A (PP2A). Cells were treated with AGS in the presence or absence of the PP2A inhibitor, okadaic acid (OA), and exposed to IFN-α, 1,000 IU for 30 min. A: PP2A-dependent regulation of STAT-1 methylation by Ach. IP, anti-methyl arginine; IB, STAT-1. Lane 1, IFN-α; lane 2, IFN-α + OA; lane 3, AGS + IFN-α; lane 4, AGS + IFN-α + OA; lane 5, tubericidin + IFN-α. B: PP2A-dependent regulation of PIAS-1-pSTAT-1 complex formation. IP, PIAS-1; IB, pSTAT-1. Lanes are designated as lane 1, nontreated (control) cells; lane 2, IFN-α; lane 3, IFN-α + OA; lane 4, AGS + IFN-α; lane 5, AGS + IFN-α + OA; lane 6, tubericidin + IFN-α. Both A and B are representative data from 3 independent experiments with similar results. C–F: effects of Ach on PP2A activation in HCV− (C and D) and HCV+ (E and F) cells. IB, phosphorylated PP2A and total PP2A; <t>β-actin</t> was used as the loading control. Lane 1, control; lane 2, IFN-α; lane 3, IFN-α + betaine; lane 4, AGS + IFN-α; lane 5, AGS + IFN-α + betaine. C and E: representative IB data on PP2A phosphorylation. D and F: quantification of phospho-PP2A/PP2A ratios from 3 independent experiments presented as means ± SE. Bars with different letters are significantly different at P ≤ 0.05.
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    Effects of AGS on protein phosphatase 2A (PP2A). Cells were treated with AGS in the presence or absence of the PP2A inhibitor, okadaic acid (OA), and exposed to IFN-α, 1,000 IU for 30 min. A: PP2A-dependent regulation of STAT-1 methylation by Ach. IP, anti-methyl arginine; IB, STAT-1. Lane 1, IFN-α; lane 2, IFN-α + OA; lane 3, AGS + IFN-α; lane 4, AGS + IFN-α + OA; lane 5, tubericidin + IFN-α. B: PP2A-dependent regulation of PIAS-1-pSTAT-1 complex formation. IP, PIAS-1; IB, pSTAT-1. Lanes are designated as lane 1, nontreated (control) cells; lane 2, IFN-α; lane 3, IFN-α + OA; lane 4, AGS + IFN-α; lane 5, AGS + IFN-α + OA; lane 6, tubericidin + IFN-α. Both A and B are representative data from 3 independent experiments with similar results. C–F: effects of Ach on PP2A activation in HCV− (C and D) and HCV+ (E and F) cells. IB, phosphorylated PP2A and total PP2A; <t>β-actin</t> was used as the loading control. Lane 1, control; lane 2, IFN-α; lane 3, IFN-α + betaine; lane 4, AGS + IFN-α; lane 5, AGS + IFN-α + betaine. C and E: representative IB data on PP2A phosphorylation. D and F: quantification of phospho-PP2A/PP2A ratios from 3 independent experiments presented as means ± SE. Bars with different letters are significantly different at P ≤ 0.05.
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    Effects of AGS on protein phosphatase 2A (PP2A). Cells were treated with AGS in the presence or absence of the PP2A inhibitor, okadaic acid (OA), and exposed to IFN-α, 1,000 IU for 30 min. A: PP2A-dependent regulation of STAT-1 methylation by Ach. IP, anti-methyl arginine; IB, STAT-1. Lane 1, IFN-α; lane 2, IFN-α + OA; lane 3, AGS + IFN-α; lane 4, AGS + IFN-α + OA; lane 5, tubericidin + IFN-α. B: PP2A-dependent regulation of PIAS-1-pSTAT-1 complex formation. IP, PIAS-1; IB, pSTAT-1. Lanes are designated as lane 1, nontreated (control) cells; lane 2, IFN-α; lane 3, IFN-α + OA; lane 4, AGS + IFN-α; lane 5, AGS + IFN-α + OA; lane 6, tubericidin + IFN-α. Both A and B are representative data from 3 independent experiments with similar results. C–F: effects of Ach on PP2A activation in HCV− (C and D) and HCV+ (E and F) cells. IB, phosphorylated PP2A and total PP2A; <t>β-actin</t> was used as the loading control. Lane 1, control; lane 2, IFN-α; lane 3, IFN-α + betaine; lane 4, AGS + IFN-α; lane 5, AGS + IFN-α + betaine. C and E: representative IB data on PP2A phosphorylation. D and F: quantification of phospho-PP2A/PP2A ratios from 3 independent experiments presented as means ± SE. Bars with different letters are significantly different at P ≤ 0.05.
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    Effects of AGS on protein phosphatase 2A (PP2A). Cells were treated with AGS in the presence or absence of the PP2A inhibitor, okadaic acid (OA), and exposed to IFN-α, 1,000 IU for 30 min. A: PP2A-dependent regulation of STAT-1 methylation by Ach. IP, anti-methyl arginine; IB, STAT-1. Lane 1, IFN-α; lane 2, IFN-α + OA; lane 3, AGS + IFN-α; lane 4, AGS + IFN-α + OA; lane 5, tubericidin + IFN-α. B: PP2A-dependent regulation of PIAS-1-pSTAT-1 complex formation. IP, PIAS-1; IB, pSTAT-1. Lanes are designated as lane 1, nontreated (control) cells; lane 2, IFN-α; lane 3, IFN-α + OA; lane 4, AGS + IFN-α; lane 5, AGS + IFN-α + OA; lane 6, tubericidin + IFN-α. Both A and B are representative data from 3 independent experiments with similar results. C–F: effects of Ach on PP2A activation in HCV− (C and D) and HCV+ (E and F) cells. IB, phosphorylated PP2A and total PP2A; <t>β-actin</t> was used as the loading control. Lane 1, control; lane 2, IFN-α; lane 3, IFN-α + betaine; lane 4, AGS + IFN-α; lane 5, AGS + IFN-α + betaine. C and E: representative IB data on PP2A phosphorylation. D and F: quantification of phospho-PP2A/PP2A ratios from 3 independent experiments presented as means ± SE. Bars with different letters are significantly different at P ≤ 0.05.
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    Image Search Results


    Effects of AGS on protein phosphatase 2A (PP2A). Cells were treated with AGS in the presence or absence of the PP2A inhibitor, okadaic acid (OA), and exposed to IFN-α, 1,000 IU for 30 min. A: PP2A-dependent regulation of STAT-1 methylation by Ach. IP, anti-methyl arginine; IB, STAT-1. Lane 1, IFN-α; lane 2, IFN-α + OA; lane 3, AGS + IFN-α; lane 4, AGS + IFN-α + OA; lane 5, tubericidin + IFN-α. B: PP2A-dependent regulation of PIAS-1-pSTAT-1 complex formation. IP, PIAS-1; IB, pSTAT-1. Lanes are designated as lane 1, nontreated (control) cells; lane 2, IFN-α; lane 3, IFN-α + OA; lane 4, AGS + IFN-α; lane 5, AGS + IFN-α + OA; lane 6, tubericidin + IFN-α. Both A and B are representative data from 3 independent experiments with similar results. C–F: effects of Ach on PP2A activation in HCV− (C and D) and HCV+ (E and F) cells. IB, phosphorylated PP2A and total PP2A; β-actin was used as the loading control. Lane 1, control; lane 2, IFN-α; lane 3, IFN-α + betaine; lane 4, AGS + IFN-α; lane 5, AGS + IFN-α + betaine. C and E: representative IB data on PP2A phosphorylation. D and F: quantification of phospho-PP2A/PP2A ratios from 3 independent experiments presented as means ± SE. Bars with different letters are significantly different at P ≤ 0.05.

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Acetaldehyde accelerates HCV-induced impairment of innate immunity by suppressing methylation reactions in liver cells

    doi: 10.1152/ajpgi.00183.2015

    Figure Lengend Snippet: Effects of AGS on protein phosphatase 2A (PP2A). Cells were treated with AGS in the presence or absence of the PP2A inhibitor, okadaic acid (OA), and exposed to IFN-α, 1,000 IU for 30 min. A: PP2A-dependent regulation of STAT-1 methylation by Ach. IP, anti-methyl arginine; IB, STAT-1. Lane 1, IFN-α; lane 2, IFN-α + OA; lane 3, AGS + IFN-α; lane 4, AGS + IFN-α + OA; lane 5, tubericidin + IFN-α. B: PP2A-dependent regulation of PIAS-1-pSTAT-1 complex formation. IP, PIAS-1; IB, pSTAT-1. Lanes are designated as lane 1, nontreated (control) cells; lane 2, IFN-α; lane 3, IFN-α + OA; lane 4, AGS + IFN-α; lane 5, AGS + IFN-α + OA; lane 6, tubericidin + IFN-α. Both A and B are representative data from 3 independent experiments with similar results. C–F: effects of Ach on PP2A activation in HCV− (C and D) and HCV+ (E and F) cells. IB, phosphorylated PP2A and total PP2A; β-actin was used as the loading control. Lane 1, control; lane 2, IFN-α; lane 3, IFN-α + betaine; lane 4, AGS + IFN-α; lane 5, AGS + IFN-α + betaine. C and E: representative IB data on PP2A phosphorylation. D and F: quantification of phospho-PP2A/PP2A ratios from 3 independent experiments presented as means ± SE. Bars with different letters are significantly different at P ≤ 0.05.

    Article Snippet: Antibody to phosphorylated STAT-1 (Tyr 701) was from Cell Signaling (Beverly, MA); antibodies to the STAT-1, protein inhibitor of activated STAT-1 (PIAS-1), and β-actin were from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Methylation, Control, Activation Assay, Phospho-proteomics

    Effects of AGS on HCV infection and apoptosis. HCV-infected RLW cells were treated with AGS for the indicated time. A: HCV RNA in RLW cells. GAPDH mRNA was used to normalize the gene of interest. B: immunostaining of RLW cells treated with AGS for 24 and 48 h. Red, HCV core protein; green, lipid droplets (LDs); yellow, colocalization of core protein and LDs; blue, nuclear staining. C and D: IB, cleaved caspase-3 in both HCV− and HCV+ cells treated with 50 mM ethanol and AGS for 48 h. β-Actin was used as loading control. Lane 1, control (untreated cells); lane 2, EtOH; lane 3, AGS. All data (representative results and quantification) were generated from 3 independent experiments and presented as means ± SE. Bars with different letters are significantly different at P ≤ 0.05.

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Acetaldehyde accelerates HCV-induced impairment of innate immunity by suppressing methylation reactions in liver cells

    doi: 10.1152/ajpgi.00183.2015

    Figure Lengend Snippet: Effects of AGS on HCV infection and apoptosis. HCV-infected RLW cells were treated with AGS for the indicated time. A: HCV RNA in RLW cells. GAPDH mRNA was used to normalize the gene of interest. B: immunostaining of RLW cells treated with AGS for 24 and 48 h. Red, HCV core protein; green, lipid droplets (LDs); yellow, colocalization of core protein and LDs; blue, nuclear staining. C and D: IB, cleaved caspase-3 in both HCV− and HCV+ cells treated with 50 mM ethanol and AGS for 48 h. β-Actin was used as loading control. Lane 1, control (untreated cells); lane 2, EtOH; lane 3, AGS. All data (representative results and quantification) were generated from 3 independent experiments and presented as means ± SE. Bars with different letters are significantly different at P ≤ 0.05.

    Article Snippet: Antibody to phosphorylated STAT-1 (Tyr 701) was from Cell Signaling (Beverly, MA); antibodies to the STAT-1, protein inhibitor of activated STAT-1 (PIAS-1), and β-actin were from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Infection, Immunostaining, Staining, Control, Generated