phospho p38 thr180 thr182 d3f9 rabbit monoclonal  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38 thr180 thr182 d3f9 rabbit monoclonal
    DHA accelerates caspase-1 protein synthesis in a p38MAP-dependent manner (A) Protein synthesis signaling diagram. Inhibitors for signaling components are denoted in red. (B) ES2 and SK-OV3 cells were treated with DHA at IC50 for 16 or 24 h, followed by western blotting to detect <t>phosphor-p38MAPK,</t> p38MAPK, phosphor-Akt, Akt, phosphor-Mnk1, Mnk1, phosphor-Erk, Erk, phosphor-eIF4E, and eIF4E with the respective antibodies. (C) ES2 cells were treated with DHA in the absence or presence of AZD5383, Trametinib, BIRB796, or Rapamycin for 24 h, followed by western blotting to detect caspase-1 and GAPDH with the respective antibodies. (D) ES2 and SK-OV3 cells were cultured in a methionine-free medium for 2 h, and then fed with a medium containing AHA in the absence or presence of BIRB796 for 16 h. Cells were lysed and AHA-incorporated proteins were isolated for western blotting to detect caspase-1 with caspase-1 antibody. Cell lysates before isolating AHA-incorporated proteins were also subjected to western blotting to detect GAPDH to ensure equal loading. (E) ES2, SK-OV3, and OCC1 cells were treated with vehicle or 100 μM DHA in the absence or presence of AZD5363, Trametinib, Rapamycin, BIRB796, or 796 CPG57380 for 24 h followed by MTT assay to analyze cell viability. % of cell viability was calculated as [(Control – Treatment)/Control] x 100. Control: vehicle-treated; Treatment: DHA or DHA + inhibitors. Data are means ± SEM. ∗∗∗, p < 0.001.
    Phospho P38 Thr180 Thr182 D3f9 Rabbit Monoclonal, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "ASC/inflammasome-independent pyroptosis in ovarian cancer cells through translational augmentation of caspase-1"

    Article Title: ASC/inflammasome-independent pyroptosis in ovarian cancer cells through translational augmentation of caspase-1

    Journal: iScience

    doi: 10.1016/j.isci.2023.108408

    DHA accelerates caspase-1 protein synthesis in a p38MAP-dependent manner (A) Protein synthesis signaling diagram. Inhibitors for signaling components are denoted in red. (B) ES2 and SK-OV3 cells were treated with DHA at IC50 for 16 or 24 h, followed by western blotting to detect phosphor-p38MAPK, p38MAPK, phosphor-Akt, Akt, phosphor-Mnk1, Mnk1, phosphor-Erk, Erk, phosphor-eIF4E, and eIF4E with the respective antibodies. (C) ES2 cells were treated with DHA in the absence or presence of AZD5383, Trametinib, BIRB796, or Rapamycin for 24 h, followed by western blotting to detect caspase-1 and GAPDH with the respective antibodies. (D) ES2 and SK-OV3 cells were cultured in a methionine-free medium for 2 h, and then fed with a medium containing AHA in the absence or presence of BIRB796 for 16 h. Cells were lysed and AHA-incorporated proteins were isolated for western blotting to detect caspase-1 with caspase-1 antibody. Cell lysates before isolating AHA-incorporated proteins were also subjected to western blotting to detect GAPDH to ensure equal loading. (E) ES2, SK-OV3, and OCC1 cells were treated with vehicle or 100 μM DHA in the absence or presence of AZD5363, Trametinib, Rapamycin, BIRB796, or 796 CPG57380 for 24 h followed by MTT assay to analyze cell viability. % of cell viability was calculated as [(Control – Treatment)/Control] x 100. Control: vehicle-treated; Treatment: DHA or DHA + inhibitors. Data are means ± SEM. ∗∗∗, p < 0.001.
    Figure Legend Snippet: DHA accelerates caspase-1 protein synthesis in a p38MAP-dependent manner (A) Protein synthesis signaling diagram. Inhibitors for signaling components are denoted in red. (B) ES2 and SK-OV3 cells were treated with DHA at IC50 for 16 or 24 h, followed by western blotting to detect phosphor-p38MAPK, p38MAPK, phosphor-Akt, Akt, phosphor-Mnk1, Mnk1, phosphor-Erk, Erk, phosphor-eIF4E, and eIF4E with the respective antibodies. (C) ES2 cells were treated with DHA in the absence or presence of AZD5383, Trametinib, BIRB796, or Rapamycin for 24 h, followed by western blotting to detect caspase-1 and GAPDH with the respective antibodies. (D) ES2 and SK-OV3 cells were cultured in a methionine-free medium for 2 h, and then fed with a medium containing AHA in the absence or presence of BIRB796 for 16 h. Cells were lysed and AHA-incorporated proteins were isolated for western blotting to detect caspase-1 with caspase-1 antibody. Cell lysates before isolating AHA-incorporated proteins were also subjected to western blotting to detect GAPDH to ensure equal loading. (E) ES2, SK-OV3, and OCC1 cells were treated with vehicle or 100 μM DHA in the absence or presence of AZD5363, Trametinib, Rapamycin, BIRB796, or 796 CPG57380 for 24 h followed by MTT assay to analyze cell viability. % of cell viability was calculated as [(Control – Treatment)/Control] x 100. Control: vehicle-treated; Treatment: DHA or DHA + inhibitors. Data are means ± SEM. ∗∗∗, p < 0.001.

    Techniques Used: Western Blot, Cell Culture, Isolation, MTT Assay


    Figure Legend Snippet:

    Techniques Used: Recombinant, Protease Inhibitor, Pore Size, Western Blot, Bicinchoninic Acid Protein Assay, Flow Cytometry, Colorimetric Assay, Enzyme-linked Immunosorbent Assay, LDH Cytotoxicity Assay, Software

    anti phospho p38 mapk thr180 thr182 rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho p38 mapk thr180 thr182 rabbit mab
    a Western blot analysis after SDS-PAGE of <t>phospho-p38</t> levels in 1-day-old wild-type adults with and without cisplatin treatment for indicated times. Worms were exposed to cisplatin on 300 μg/mL cisplatin-containing plates. The blot was <t>probed</t> <t>with</t> <t>anti:phospho-p38</t> antibody to detect activated PMK-1, anti:PMK-1 antibody was used to estimate total levels of PMK-1 protein, tubulin was used as a loading control. Full uncropped images are available in Supplementary Fig. . b Relative phospho-p38 level quantification from blots presented in Supplementary Fig. . Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. Bars represent mean ± SD. c Western blot analysis after SDS-PAGE of phospho-p38 levels in 1-day-old wild-type adults with (+) and without (−) MitoTempo/cisplatin exposure. The blot was probed with anti:phospho-p38 antibody, tubulin was used as a loading control. Full uncropped images are available in Supplementary Fig. . d Relative phospho-p38 levels quantification from blots presented in Supplementary Fig. . Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. Bars represent mean ± SD. e , h , i Mean survival ± SD of 1-day-old adults with the indicated genotypes after 24 h cisplatin (300 μg/mL) exposure. Statistical significance determined was by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. All data on cisplatin sensitivity trials is available in Supplementary Data . f , g Relative gene expression of four phase II detoxification genes in 1-day-old adult wild-type animals ( f ) without or with (+CP) 6 h or 24 h cisplatin treatment, g without or with (+CP) 6 h cisplatin treatment. Worms were exposed to cisplatin on 300 μg/mL cisplatin-containing plates. Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate for 6 h exposure timepoint and duplicate for 24 h exposure timepoint. F44B9.5 was used as a normalizing control. Bars represent mean ± SEM. Source data are provided as a Source Data file.
    Anti Phospho P38 Mapk Thr180 Thr182 Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Cisplatin toxicity is counteracted by the activation of the p38/ATF-7 signaling pathway in post-mitotic C. elegans"

    Article Title: Cisplatin toxicity is counteracted by the activation of the p38/ATF-7 signaling pathway in post-mitotic C. elegans

    Journal: Nature Communications

    doi: 10.1038/s41467-023-38568-5

    a Western blot analysis after SDS-PAGE of phospho-p38 levels in 1-day-old wild-type adults with and without cisplatin treatment for indicated times. Worms were exposed to cisplatin on 300 μg/mL cisplatin-containing plates. The blot was probed with anti:phospho-p38 antibody to detect activated PMK-1, anti:PMK-1 antibody was used to estimate total levels of PMK-1 protein, tubulin was used as a loading control. Full uncropped images are available in Supplementary Fig. . b Relative phospho-p38 level quantification from blots presented in Supplementary Fig. . Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. Bars represent mean ± SD. c Western blot analysis after SDS-PAGE of phospho-p38 levels in 1-day-old wild-type adults with (+) and without (−) MitoTempo/cisplatin exposure. The blot was probed with anti:phospho-p38 antibody, tubulin was used as a loading control. Full uncropped images are available in Supplementary Fig. . d Relative phospho-p38 levels quantification from blots presented in Supplementary Fig. . Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. Bars represent mean ± SD. e , h , i Mean survival ± SD of 1-day-old adults with the indicated genotypes after 24 h cisplatin (300 μg/mL) exposure. Statistical significance determined was by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. All data on cisplatin sensitivity trials is available in Supplementary Data . f , g Relative gene expression of four phase II detoxification genes in 1-day-old adult wild-type animals ( f ) without or with (+CP) 6 h or 24 h cisplatin treatment, g without or with (+CP) 6 h cisplatin treatment. Worms were exposed to cisplatin on 300 μg/mL cisplatin-containing plates. Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate for 6 h exposure timepoint and duplicate for 24 h exposure timepoint. F44B9.5 was used as a normalizing control. Bars represent mean ± SEM. Source data are provided as a Source Data file.
    Figure Legend Snippet: a Western blot analysis after SDS-PAGE of phospho-p38 levels in 1-day-old wild-type adults with and without cisplatin treatment for indicated times. Worms were exposed to cisplatin on 300 μg/mL cisplatin-containing plates. The blot was probed with anti:phospho-p38 antibody to detect activated PMK-1, anti:PMK-1 antibody was used to estimate total levels of PMK-1 protein, tubulin was used as a loading control. Full uncropped images are available in Supplementary Fig. . b Relative phospho-p38 level quantification from blots presented in Supplementary Fig. . Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. Bars represent mean ± SD. c Western blot analysis after SDS-PAGE of phospho-p38 levels in 1-day-old wild-type adults with (+) and without (−) MitoTempo/cisplatin exposure. The blot was probed with anti:phospho-p38 antibody, tubulin was used as a loading control. Full uncropped images are available in Supplementary Fig. . d Relative phospho-p38 levels quantification from blots presented in Supplementary Fig. . Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. Bars represent mean ± SD. e , h , i Mean survival ± SD of 1-day-old adults with the indicated genotypes after 24 h cisplatin (300 μg/mL) exposure. Statistical significance determined was by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. All data on cisplatin sensitivity trials is available in Supplementary Data . f , g Relative gene expression of four phase II detoxification genes in 1-day-old adult wild-type animals ( f ) without or with (+CP) 6 h or 24 h cisplatin treatment, g without or with (+CP) 6 h cisplatin treatment. Worms were exposed to cisplatin on 300 μg/mL cisplatin-containing plates. Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate for 6 h exposure timepoint and duplicate for 24 h exposure timepoint. F44B9.5 was used as a normalizing control. Bars represent mean ± SEM. Source data are provided as a Source Data file.

    Techniques Used: Western Blot, SDS Page, Expressing

    a Western blot analysis after SDS-PAGE of phospho-p38 levels in 1-day-old adults with (+) and without (–) 1 mM auxin (AUX) treatment. The blot was probed with anti:phospho-p38 antibody and tubulin was used as a loading control. Full uncropped images are available in Supplementary Fig. . b , d Mean survival ± SD of 1-day-old adults with the indicated genotypes after 24 h exposure to 300 μg/mL cisplatin-containing plates without (−AUX) or with (+AUX) 1 mM auxin treatment (see the “Methods” section for details). Statistical significance was determined by the b independent two-sided t -test or d one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. c Western blot analysis after SDS-PAGE of SEK-1 levels in 1-day-old adults with (+) and without (−) 1 mM auxin (AUX) treatment. The blot was probed with anti:Flag antibody and tubulin was used as a loading control. Source data are provided as a Source Data file.
    Figure Legend Snippet: a Western blot analysis after SDS-PAGE of phospho-p38 levels in 1-day-old adults with (+) and without (–) 1 mM auxin (AUX) treatment. The blot was probed with anti:phospho-p38 antibody and tubulin was used as a loading control. Full uncropped images are available in Supplementary Fig. . b , d Mean survival ± SD of 1-day-old adults with the indicated genotypes after 24 h exposure to 300 μg/mL cisplatin-containing plates without (−AUX) or with (+AUX) 1 mM auxin treatment (see the “Methods” section for details). Statistical significance was determined by the b independent two-sided t -test or d one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. c Western blot analysis after SDS-PAGE of SEK-1 levels in 1-day-old adults with (+) and without (−) 1 mM auxin (AUX) treatment. The blot was probed with anti:Flag antibody and tubulin was used as a loading control. Source data are provided as a Source Data file.

    Techniques Used: Western Blot, SDS Page

    phospho p38 mapk thr180 thr182 d3f9 xp rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38 mapk thr180 thr182 d3f9 xp rabbit mab
    Phospho P38 Mapk Thr180 Thr182 D3f9 Xp Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    protein kinase mapk thr180 thr182  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc protein kinase mapk thr180 thr182
    Protein Kinase Mapk Thr180 Thr182, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phospho p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38 mapk
    Phospho P38 Mapk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phospho p38 mapk thr180 thr182  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38 mapk thr180 thr182
    Role of the activation of <t>p38</t> <t>MAPK</t> and ERK1/2 in SS2 and PMA induced NETs formation. (A) Neutrophils were infected with SS2 ZY05719 or treated with PMA for 2 h; <t>p38</t> <t>MAPK</t> and ERK1/2 phosphorylation were determined with western blotting using specific antibody against phospho-p38 MAPK (p-p38), p38 <t>MAPK</t> <t>(p38),</t> phospho-ERK1/2 (p-ERK1/2), and ERK1/2. GAPDH was used as an internal control. (B) Neutrophils were pretreated with inhibitor of p38 MAPK (SB203580) and ERK1/2 (U0126), and then cells were incubated with SS2 ZY05719 or PMA for 3 h. Results were normalized to neutrophils without pretreatment and activation, and are depicted as the mean ±SEM ( n = 3) of three independent experiments; ** p < 0.01; *** p < 0.001. (C) Neutrophils were pretreated with inhibitor of p38 MAPK (SB203580) and ERK1/2 (U0126), and the cells were then incubated with either SS2 ZY05719 or PMA for 3 h. Immunofluorescence was performed using anti-neutrophil elastase (NE) antibody followed by goat anti-rabbit Alexa 568 antibody (red). DNA was stained with DAPI (blue). The results shown are representative of three independent experiments.
    Phospho P38 Mapk Thr180 Thr182, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Streptococcus Suis Serotype 2 Stimulates Neutrophil Extracellular Traps Formation via Activation of p38 MAPK and ERK1/2"

    Article Title: Streptococcus Suis Serotype 2 Stimulates Neutrophil Extracellular Traps Formation via Activation of p38 MAPK and ERK1/2

    Journal: Frontiers in Immunology

    doi: 10.3389/fimmu.2018.02854

    Role of the activation of p38 MAPK and ERK1/2 in SS2 and PMA induced NETs formation. (A) Neutrophils were infected with SS2 ZY05719 or treated with PMA for 2 h; p38 MAPK and ERK1/2 phosphorylation were determined with western blotting using specific antibody against phospho-p38 MAPK (p-p38), p38 MAPK (p38), phospho-ERK1/2 (p-ERK1/2), and ERK1/2. GAPDH was used as an internal control. (B) Neutrophils were pretreated with inhibitor of p38 MAPK (SB203580) and ERK1/2 (U0126), and then cells were incubated with SS2 ZY05719 or PMA for 3 h. Results were normalized to neutrophils without pretreatment and activation, and are depicted as the mean ±SEM ( n = 3) of three independent experiments; ** p < 0.01; *** p < 0.001. (C) Neutrophils were pretreated with inhibitor of p38 MAPK (SB203580) and ERK1/2 (U0126), and the cells were then incubated with either SS2 ZY05719 or PMA for 3 h. Immunofluorescence was performed using anti-neutrophil elastase (NE) antibody followed by goat anti-rabbit Alexa 568 antibody (red). DNA was stained with DAPI (blue). The results shown are representative of three independent experiments.
    Figure Legend Snippet: Role of the activation of p38 MAPK and ERK1/2 in SS2 and PMA induced NETs formation. (A) Neutrophils were infected with SS2 ZY05719 or treated with PMA for 2 h; p38 MAPK and ERK1/2 phosphorylation were determined with western blotting using specific antibody against phospho-p38 MAPK (p-p38), p38 MAPK (p38), phospho-ERK1/2 (p-ERK1/2), and ERK1/2. GAPDH was used as an internal control. (B) Neutrophils were pretreated with inhibitor of p38 MAPK (SB203580) and ERK1/2 (U0126), and then cells were incubated with SS2 ZY05719 or PMA for 3 h. Results were normalized to neutrophils without pretreatment and activation, and are depicted as the mean ±SEM ( n = 3) of three independent experiments; ** p < 0.01; *** p < 0.001. (C) Neutrophils were pretreated with inhibitor of p38 MAPK (SB203580) and ERK1/2 (U0126), and the cells were then incubated with either SS2 ZY05719 or PMA for 3 h. Immunofluorescence was performed using anti-neutrophil elastase (NE) antibody followed by goat anti-rabbit Alexa 568 antibody (red). DNA was stained with DAPI (blue). The results shown are representative of three independent experiments.

    Techniques Used: Activation Assay, Infection, Western Blot, Incubation, Immunofluorescence, Staining

    Western blotting analysis of phosphorylation of p38 MAPK and ERK1/2. (A) Neutrophils were pretreated with inhibitors of TLR4 signaling (TAK-242) and NADPH oxidase (DPI) for 30 min, and the cells were then incubated with SS2 ZY05719 and PMA for 2 h. Phosphorylation of p38 MAPK (p-p38) and ERK1/2 (p-ERK1/2) were determined with western blotting. (B) Neutrophils isolated form wild-type mice and TLR knockout mice were incubated with SS2 ZY05719 and Medium.
    Figure Legend Snippet: Western blotting analysis of phosphorylation of p38 MAPK and ERK1/2. (A) Neutrophils were pretreated with inhibitors of TLR4 signaling (TAK-242) and NADPH oxidase (DPI) for 30 min, and the cells were then incubated with SS2 ZY05719 and PMA for 2 h. Phosphorylation of p38 MAPK (p-p38) and ERK1/2 (p-ERK1/2) were determined with western blotting. (B) Neutrophils isolated form wild-type mice and TLR knockout mice were incubated with SS2 ZY05719 and Medium.

    Techniques Used: Western Blot, Incubation, Isolation, Knock-Out

    phospho p38 mapk thr180 thr182  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38 mapk thr180 thr182
    Phospho P38 Mapk Thr180 Thr182, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti phospho p38 thr180 thr182  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho p38 thr180 thr182
    Anti Phospho P38 Thr180 Thr182, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phospho p38 thr180 thr182 rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38 thr180 thr182 rabbit mab
    Phospho P38 Thr180 Thr182 Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc phospho p38 map kinase thr180 thr182
    PI3K and JAK2 signaling pathways are involved in the production and activation of xanthine oxidase (XO). (A) Representative western blot of XO and tubulin expression in cardiac microvascular endothelial cells (CMECs) following hypoxia/reoxygenation (H/R). LY294002 and AG490 significantly decreased the increase in the XO protein level induced by H/R. (B) Summary data (n=3 biological replicates) of western blot analysis of XO and tubulin expression in CMECs following H/R. LY294002, SB203580 and AG490 treatment group compared with H/R group. * p<0.05 vs. H/R group. PI3K and JAK2 signaling pathways are involved in the production and activation of xanthine oxidase (XO). (C) Representative western blots of phosphorylated (p-)PI3K, total (t-)PI3K, p-JAK2, t-JAK2, <t>p-p38</t> <t>MAPK</t> and t-p38 MAPK expression in cardiac microvascular endothelial cells (CMECs) following hypoxia/reoxygenation (H/R). H/R activates the PI3K and JAK2 signaling pathways but not the <t>p38</t> <t>MAPK</t> signaling pathway. (D) Summary data (n=3 biological replicates) of western blot analysis of p-PI3K, t-PI3K, p-JAK2, t-JAK2, p-p38 MAPK and t-p38 MAPK expression in CMECs. ** p<0.01 vs. control group. (E) Representative data for flow cytometric analysis of DCFH-DA-stained CMECs following H/R. LY294002, SB203580 and AG490 treatment groups compared with H/R group. (F) Summary data (n=3 biological replicates) of flow cytometric analysis of DCFH-DA-stained CMECs following H/R. LY294002 (1 µ M), SB203580 (30 µ M) and AG490 (30 µ M) treatment groups compared with H/R group. * p<0.05 vs. H/R group; ** p<0.01 vs. H/R group.
    Phospho P38 Map Kinase Thr180 Thr182, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Hepatocyte growth factor inhibits hypoxia/reoxygenation-induced activation of xanthine oxidase in endothelial cells through the JAK2 signaling pathway"

    Article Title: Hepatocyte growth factor inhibits hypoxia/reoxygenation-induced activation of xanthine oxidase in endothelial cells through the JAK2 signaling pathway

    Journal: International Journal of Molecular Medicine

    doi: 10.3892/ijmm.2016.2708

    PI3K and JAK2 signaling pathways are involved in the production and activation of xanthine oxidase (XO). (A) Representative western blot of XO and tubulin expression in cardiac microvascular endothelial cells (CMECs) following hypoxia/reoxygenation (H/R). LY294002 and AG490 significantly decreased the increase in the XO protein level induced by H/R. (B) Summary data (n=3 biological replicates) of western blot analysis of XO and tubulin expression in CMECs following H/R. LY294002, SB203580 and AG490 treatment group compared with H/R group. * p<0.05 vs. H/R group. PI3K and JAK2 signaling pathways are involved in the production and activation of xanthine oxidase (XO). (C) Representative western blots of phosphorylated (p-)PI3K, total (t-)PI3K, p-JAK2, t-JAK2, p-p38 MAPK and t-p38 MAPK expression in cardiac microvascular endothelial cells (CMECs) following hypoxia/reoxygenation (H/R). H/R activates the PI3K and JAK2 signaling pathways but not the p38 MAPK signaling pathway. (D) Summary data (n=3 biological replicates) of western blot analysis of p-PI3K, t-PI3K, p-JAK2, t-JAK2, p-p38 MAPK and t-p38 MAPK expression in CMECs. ** p<0.01 vs. control group. (E) Representative data for flow cytometric analysis of DCFH-DA-stained CMECs following H/R. LY294002, SB203580 and AG490 treatment groups compared with H/R group. (F) Summary data (n=3 biological replicates) of flow cytometric analysis of DCFH-DA-stained CMECs following H/R. LY294002 (1 µ M), SB203580 (30 µ M) and AG490 (30 µ M) treatment groups compared with H/R group. * p<0.05 vs. H/R group; ** p<0.01 vs. H/R group.
    Figure Legend Snippet: PI3K and JAK2 signaling pathways are involved in the production and activation of xanthine oxidase (XO). (A) Representative western blot of XO and tubulin expression in cardiac microvascular endothelial cells (CMECs) following hypoxia/reoxygenation (H/R). LY294002 and AG490 significantly decreased the increase in the XO protein level induced by H/R. (B) Summary data (n=3 biological replicates) of western blot analysis of XO and tubulin expression in CMECs following H/R. LY294002, SB203580 and AG490 treatment group compared with H/R group. * p<0.05 vs. H/R group. PI3K and JAK2 signaling pathways are involved in the production and activation of xanthine oxidase (XO). (C) Representative western blots of phosphorylated (p-)PI3K, total (t-)PI3K, p-JAK2, t-JAK2, p-p38 MAPK and t-p38 MAPK expression in cardiac microvascular endothelial cells (CMECs) following hypoxia/reoxygenation (H/R). H/R activates the PI3K and JAK2 signaling pathways but not the p38 MAPK signaling pathway. (D) Summary data (n=3 biological replicates) of western blot analysis of p-PI3K, t-PI3K, p-JAK2, t-JAK2, p-p38 MAPK and t-p38 MAPK expression in CMECs. ** p<0.01 vs. control group. (E) Representative data for flow cytometric analysis of DCFH-DA-stained CMECs following H/R. LY294002, SB203580 and AG490 treatment groups compared with H/R group. (F) Summary data (n=3 biological replicates) of flow cytometric analysis of DCFH-DA-stained CMECs following H/R. LY294002 (1 µ M), SB203580 (30 µ M) and AG490 (30 µ M) treatment groups compared with H/R group. * p<0.05 vs. H/R group; ** p<0.01 vs. H/R group.

    Techniques Used: Activation Assay, Western Blot, Expressing, Staining

    PI3K siRNA and JAK2 siRNA downregulate the production and activation of xanthine oxidase (XO). (A) Representative western blots of p38 MAPK, PI3K, JAK2 and tubulin expression in cardiac microvascular endothelial cells (CMECs). (B) Representative western blot of XO and tubulin expression in CMECs following hypoxia/reoxygenation (H/R). PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- and negative control siRNA-transfected groups compared with H/R group. (C) Summary data (n=3 biological replicates) for western blot analysis of XO and tubulin expression in CMECs following H/R. PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- or negative control siRNA-transfected groups compared with H/R group. ** p<0.01 vs. H/R group. (D) Representative flow cytometric analysis of DCFH-DA-stained CMECs after H/R. PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- or negative control siRNA-transfected groups compared with H/R group. (E) Summary data (n=3 biological replicates) for flow cytometric analysis of DCFH-DA-stained CMECs after H/R. PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- or negative control siRNA-transfected groups compared with H/R group. ** p<0.01 vs. H/R group.
    Figure Legend Snippet: PI3K siRNA and JAK2 siRNA downregulate the production and activation of xanthine oxidase (XO). (A) Representative western blots of p38 MAPK, PI3K, JAK2 and tubulin expression in cardiac microvascular endothelial cells (CMECs). (B) Representative western blot of XO and tubulin expression in CMECs following hypoxia/reoxygenation (H/R). PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- and negative control siRNA-transfected groups compared with H/R group. (C) Summary data (n=3 biological replicates) for western blot analysis of XO and tubulin expression in CMECs following H/R. PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- or negative control siRNA-transfected groups compared with H/R group. ** p<0.01 vs. H/R group. (D) Representative flow cytometric analysis of DCFH-DA-stained CMECs after H/R. PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- or negative control siRNA-transfected groups compared with H/R group. (E) Summary data (n=3 biological replicates) for flow cytometric analysis of DCFH-DA-stained CMECs after H/R. PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- or negative control siRNA-transfected groups compared with H/R group. ** p<0.01 vs. H/R group.

    Techniques Used: Activation Assay, Western Blot, Expressing, Negative Control, Transfection, Staining

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    Cell Signaling Technology Inc phospho p38 thr180 thr182 d3f9 rabbit monoclonal
    DHA accelerates caspase-1 protein synthesis in a p38MAP-dependent manner (A) Protein synthesis signaling diagram. Inhibitors for signaling components are denoted in red. (B) ES2 and SK-OV3 cells were treated with DHA at IC50 for 16 or 24 h, followed by western blotting to detect <t>phosphor-p38MAPK,</t> p38MAPK, phosphor-Akt, Akt, phosphor-Mnk1, Mnk1, phosphor-Erk, Erk, phosphor-eIF4E, and eIF4E with the respective antibodies. (C) ES2 cells were treated with DHA in the absence or presence of AZD5383, Trametinib, BIRB796, or Rapamycin for 24 h, followed by western blotting to detect caspase-1 and GAPDH with the respective antibodies. (D) ES2 and SK-OV3 cells were cultured in a methionine-free medium for 2 h, and then fed with a medium containing AHA in the absence or presence of BIRB796 for 16 h. Cells were lysed and AHA-incorporated proteins were isolated for western blotting to detect caspase-1 with caspase-1 antibody. Cell lysates before isolating AHA-incorporated proteins were also subjected to western blotting to detect GAPDH to ensure equal loading. (E) ES2, SK-OV3, and OCC1 cells were treated with vehicle or 100 μM DHA in the absence or presence of AZD5363, Trametinib, Rapamycin, BIRB796, or 796 CPG57380 for 24 h followed by MTT assay to analyze cell viability. % of cell viability was calculated as [(Control – Treatment)/Control] x 100. Control: vehicle-treated; Treatment: DHA or DHA + inhibitors. Data are means ± SEM. ∗∗∗, p < 0.001.
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    DHA accelerates caspase-1 protein synthesis in a p38MAP-dependent manner (A) Protein synthesis signaling diagram. Inhibitors for signaling components are denoted in red. (B) ES2 and SK-OV3 cells were treated with DHA at IC50 for 16 or 24 h, followed by western blotting to detect phosphor-p38MAPK, p38MAPK, phosphor-Akt, Akt, phosphor-Mnk1, Mnk1, phosphor-Erk, Erk, phosphor-eIF4E, and eIF4E with the respective antibodies. (C) ES2 cells were treated with DHA in the absence or presence of AZD5383, Trametinib, BIRB796, or Rapamycin for 24 h, followed by western blotting to detect caspase-1 and GAPDH with the respective antibodies. (D) ES2 and SK-OV3 cells were cultured in a methionine-free medium for 2 h, and then fed with a medium containing AHA in the absence or presence of BIRB796 for 16 h. Cells were lysed and AHA-incorporated proteins were isolated for western blotting to detect caspase-1 with caspase-1 antibody. Cell lysates before isolating AHA-incorporated proteins were also subjected to western blotting to detect GAPDH to ensure equal loading. (E) ES2, SK-OV3, and OCC1 cells were treated with vehicle or 100 μM DHA in the absence or presence of AZD5363, Trametinib, Rapamycin, BIRB796, or 796 CPG57380 for 24 h followed by MTT assay to analyze cell viability. % of cell viability was calculated as [(Control – Treatment)/Control] x 100. Control: vehicle-treated; Treatment: DHA or DHA + inhibitors. Data are means ± SEM. ∗∗∗, p < 0.001.

    Journal: iScience

    Article Title: ASC/inflammasome-independent pyroptosis in ovarian cancer cells through translational augmentation of caspase-1

    doi: 10.1016/j.isci.2023.108408

    Figure Lengend Snippet: DHA accelerates caspase-1 protein synthesis in a p38MAP-dependent manner (A) Protein synthesis signaling diagram. Inhibitors for signaling components are denoted in red. (B) ES2 and SK-OV3 cells were treated with DHA at IC50 for 16 or 24 h, followed by western blotting to detect phosphor-p38MAPK, p38MAPK, phosphor-Akt, Akt, phosphor-Mnk1, Mnk1, phosphor-Erk, Erk, phosphor-eIF4E, and eIF4E with the respective antibodies. (C) ES2 cells were treated with DHA in the absence or presence of AZD5383, Trametinib, BIRB796, or Rapamycin for 24 h, followed by western blotting to detect caspase-1 and GAPDH with the respective antibodies. (D) ES2 and SK-OV3 cells were cultured in a methionine-free medium for 2 h, and then fed with a medium containing AHA in the absence or presence of BIRB796 for 16 h. Cells were lysed and AHA-incorporated proteins were isolated for western blotting to detect caspase-1 with caspase-1 antibody. Cell lysates before isolating AHA-incorporated proteins were also subjected to western blotting to detect GAPDH to ensure equal loading. (E) ES2, SK-OV3, and OCC1 cells were treated with vehicle or 100 μM DHA in the absence or presence of AZD5363, Trametinib, Rapamycin, BIRB796, or 796 CPG57380 for 24 h followed by MTT assay to analyze cell viability. % of cell viability was calculated as [(Control – Treatment)/Control] x 100. Control: vehicle-treated; Treatment: DHA or DHA + inhibitors. Data are means ± SEM. ∗∗∗, p < 0.001.

    Article Snippet: Phospho–p38 (Thr180/Thr182) (D3F9) Rabbit monoclonal , Cell Signaling , #4511S.

    Techniques: Western Blot, Cell Culture, Isolation, MTT Assay

    Journal: iScience

    Article Title: ASC/inflammasome-independent pyroptosis in ovarian cancer cells through translational augmentation of caspase-1

    doi: 10.1016/j.isci.2023.108408

    Figure Lengend Snippet:

    Article Snippet: Phospho–p38 (Thr180/Thr182) (D3F9) Rabbit monoclonal , Cell Signaling , #4511S.

    Techniques: Recombinant, Protease Inhibitor, Pore Size, Western Blot, Bicinchoninic Acid Protein Assay, Flow Cytometry, Colorimetric Assay, Enzyme-linked Immunosorbent Assay, LDH Cytotoxicity Assay, Software

    a Western blot analysis after SDS-PAGE of phospho-p38 levels in 1-day-old wild-type adults with and without cisplatin treatment for indicated times. Worms were exposed to cisplatin on 300 μg/mL cisplatin-containing plates. The blot was probed with anti:phospho-p38 antibody to detect activated PMK-1, anti:PMK-1 antibody was used to estimate total levels of PMK-1 protein, tubulin was used as a loading control. Full uncropped images are available in Supplementary Fig. . b Relative phospho-p38 level quantification from blots presented in Supplementary Fig. . Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. Bars represent mean ± SD. c Western blot analysis after SDS-PAGE of phospho-p38 levels in 1-day-old wild-type adults with (+) and without (−) MitoTempo/cisplatin exposure. The blot was probed with anti:phospho-p38 antibody, tubulin was used as a loading control. Full uncropped images are available in Supplementary Fig. . d Relative phospho-p38 levels quantification from blots presented in Supplementary Fig. . Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. Bars represent mean ± SD. e , h , i Mean survival ± SD of 1-day-old adults with the indicated genotypes after 24 h cisplatin (300 μg/mL) exposure. Statistical significance determined was by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. All data on cisplatin sensitivity trials is available in Supplementary Data . f , g Relative gene expression of four phase II detoxification genes in 1-day-old adult wild-type animals ( f ) without or with (+CP) 6 h or 24 h cisplatin treatment, g without or with (+CP) 6 h cisplatin treatment. Worms were exposed to cisplatin on 300 μg/mL cisplatin-containing plates. Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate for 6 h exposure timepoint and duplicate for 24 h exposure timepoint. F44B9.5 was used as a normalizing control. Bars represent mean ± SEM. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Cisplatin toxicity is counteracted by the activation of the p38/ATF-7 signaling pathway in post-mitotic C. elegans

    doi: 10.1038/s41467-023-38568-5

    Figure Lengend Snippet: a Western blot analysis after SDS-PAGE of phospho-p38 levels in 1-day-old wild-type adults with and without cisplatin treatment for indicated times. Worms were exposed to cisplatin on 300 μg/mL cisplatin-containing plates. The blot was probed with anti:phospho-p38 antibody to detect activated PMK-1, anti:PMK-1 antibody was used to estimate total levels of PMK-1 protein, tubulin was used as a loading control. Full uncropped images are available in Supplementary Fig. . b Relative phospho-p38 level quantification from blots presented in Supplementary Fig. . Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. Bars represent mean ± SD. c Western blot analysis after SDS-PAGE of phospho-p38 levels in 1-day-old wild-type adults with (+) and without (−) MitoTempo/cisplatin exposure. The blot was probed with anti:phospho-p38 antibody, tubulin was used as a loading control. Full uncropped images are available in Supplementary Fig. . d Relative phospho-p38 levels quantification from blots presented in Supplementary Fig. . Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. Bars represent mean ± SD. e , h , i Mean survival ± SD of 1-day-old adults with the indicated genotypes after 24 h cisplatin (300 μg/mL) exposure. Statistical significance determined was by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. All data on cisplatin sensitivity trials is available in Supplementary Data . f , g Relative gene expression of four phase II detoxification genes in 1-day-old adult wild-type animals ( f ) without or with (+CP) 6 h or 24 h cisplatin treatment, g without or with (+CP) 6 h cisplatin treatment. Worms were exposed to cisplatin on 300 μg/mL cisplatin-containing plates. Statistical significance was determined by one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate for 6 h exposure timepoint and duplicate for 24 h exposure timepoint. F44B9.5 was used as a normalizing control. Bars represent mean ± SEM. Source data are provided as a Source Data file.

    Article Snippet: Primary antibodies were: anti:phospho-p38 MAPK (Thr180/Thr182) Rabbit mAb (D3F9, Cell Signaling) 1:1000, anti:total PMK-1 MAPK Rabbit pAb 1:1000 from the Pukkila-Worley lab , anti:tubulin (T5168, Sigma) 1:5000, anti:Flag (M2, Sigma) 1:1000.

    Techniques: Western Blot, SDS Page, Expressing

    a Western blot analysis after SDS-PAGE of phospho-p38 levels in 1-day-old adults with (+) and without (–) 1 mM auxin (AUX) treatment. The blot was probed with anti:phospho-p38 antibody and tubulin was used as a loading control. Full uncropped images are available in Supplementary Fig. . b , d Mean survival ± SD of 1-day-old adults with the indicated genotypes after 24 h exposure to 300 μg/mL cisplatin-containing plates without (−AUX) or with (+AUX) 1 mM auxin treatment (see the “Methods” section for details). Statistical significance was determined by the b independent two-sided t -test or d one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. c Western blot analysis after SDS-PAGE of SEK-1 levels in 1-day-old adults with (+) and without (−) 1 mM auxin (AUX) treatment. The blot was probed with anti:Flag antibody and tubulin was used as a loading control. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Cisplatin toxicity is counteracted by the activation of the p38/ATF-7 signaling pathway in post-mitotic C. elegans

    doi: 10.1038/s41467-023-38568-5

    Figure Lengend Snippet: a Western blot analysis after SDS-PAGE of phospho-p38 levels in 1-day-old adults with (+) and without (–) 1 mM auxin (AUX) treatment. The blot was probed with anti:phospho-p38 antibody and tubulin was used as a loading control. Full uncropped images are available in Supplementary Fig. . b , d Mean survival ± SD of 1-day-old adults with the indicated genotypes after 24 h exposure to 300 μg/mL cisplatin-containing plates without (−AUX) or with (+AUX) 1 mM auxin treatment (see the “Methods” section for details). Statistical significance was determined by the b independent two-sided t -test or d one-way ANOVA followed by Bonferroni post hoc correction. The experiment was performed in triplicate. c Western blot analysis after SDS-PAGE of SEK-1 levels in 1-day-old adults with (+) and without (−) 1 mM auxin (AUX) treatment. The blot was probed with anti:Flag antibody and tubulin was used as a loading control. Source data are provided as a Source Data file.

    Article Snippet: Primary antibodies were: anti:phospho-p38 MAPK (Thr180/Thr182) Rabbit mAb (D3F9, Cell Signaling) 1:1000, anti:total PMK-1 MAPK Rabbit pAb 1:1000 from the Pukkila-Worley lab , anti:tubulin (T5168, Sigma) 1:5000, anti:Flag (M2, Sigma) 1:1000.

    Techniques: Western Blot, SDS Page

    Role of the activation of p38 MAPK and ERK1/2 in SS2 and PMA induced NETs formation. (A) Neutrophils were infected with SS2 ZY05719 or treated with PMA for 2 h; p38 MAPK and ERK1/2 phosphorylation were determined with western blotting using specific antibody against phospho-p38 MAPK (p-p38), p38 MAPK (p38), phospho-ERK1/2 (p-ERK1/2), and ERK1/2. GAPDH was used as an internal control. (B) Neutrophils were pretreated with inhibitor of p38 MAPK (SB203580) and ERK1/2 (U0126), and then cells were incubated with SS2 ZY05719 or PMA for 3 h. Results were normalized to neutrophils without pretreatment and activation, and are depicted as the mean ±SEM ( n = 3) of three independent experiments; ** p < 0.01; *** p < 0.001. (C) Neutrophils were pretreated with inhibitor of p38 MAPK (SB203580) and ERK1/2 (U0126), and the cells were then incubated with either SS2 ZY05719 or PMA for 3 h. Immunofluorescence was performed using anti-neutrophil elastase (NE) antibody followed by goat anti-rabbit Alexa 568 antibody (red). DNA was stained with DAPI (blue). The results shown are representative of three independent experiments.

    Journal: Frontiers in Immunology

    Article Title: Streptococcus Suis Serotype 2 Stimulates Neutrophil Extracellular Traps Formation via Activation of p38 MAPK and ERK1/2

    doi: 10.3389/fimmu.2018.02854

    Figure Lengend Snippet: Role of the activation of p38 MAPK and ERK1/2 in SS2 and PMA induced NETs formation. (A) Neutrophils were infected with SS2 ZY05719 or treated with PMA for 2 h; p38 MAPK and ERK1/2 phosphorylation were determined with western blotting using specific antibody against phospho-p38 MAPK (p-p38), p38 MAPK (p38), phospho-ERK1/2 (p-ERK1/2), and ERK1/2. GAPDH was used as an internal control. (B) Neutrophils were pretreated with inhibitor of p38 MAPK (SB203580) and ERK1/2 (U0126), and then cells were incubated with SS2 ZY05719 or PMA for 3 h. Results were normalized to neutrophils without pretreatment and activation, and are depicted as the mean ±SEM ( n = 3) of three independent experiments; ** p < 0.01; *** p < 0.001. (C) Neutrophils were pretreated with inhibitor of p38 MAPK (SB203580) and ERK1/2 (U0126), and the cells were then incubated with either SS2 ZY05719 or PMA for 3 h. Immunofluorescence was performed using anti-neutrophil elastase (NE) antibody followed by goat anti-rabbit Alexa 568 antibody (red). DNA was stained with DAPI (blue). The results shown are representative of three independent experiments.

    Article Snippet: Thereafter, the membranes were incubated with Phospho-p38 MAPK (Thr180/Thr182) (D3F9) XP ® Rabbit mAb, p38 MAPK (D13E1) XP® Rabbit mAb, Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E)XP ® Rabbit mAb, p44/42 MAPK (Erk1/2)(137F5) Rabbit mAb, Phospho-SAPK/JNK (Thr183/Tyr185) (81E11) Rabbit mAb (1:1000, Cell Signaling Technology, Danvers, MA, USA), or anti-GAPDH Rabbit pAb (1:5000, CMCTAG, Milwaukee, WI, USA) at 4°C overnight.

    Techniques: Activation Assay, Infection, Western Blot, Incubation, Immunofluorescence, Staining

    Western blotting analysis of phosphorylation of p38 MAPK and ERK1/2. (A) Neutrophils were pretreated with inhibitors of TLR4 signaling (TAK-242) and NADPH oxidase (DPI) for 30 min, and the cells were then incubated with SS2 ZY05719 and PMA for 2 h. Phosphorylation of p38 MAPK (p-p38) and ERK1/2 (p-ERK1/2) were determined with western blotting. (B) Neutrophils isolated form wild-type mice and TLR knockout mice were incubated with SS2 ZY05719 and Medium.

    Journal: Frontiers in Immunology

    Article Title: Streptococcus Suis Serotype 2 Stimulates Neutrophil Extracellular Traps Formation via Activation of p38 MAPK and ERK1/2

    doi: 10.3389/fimmu.2018.02854

    Figure Lengend Snippet: Western blotting analysis of phosphorylation of p38 MAPK and ERK1/2. (A) Neutrophils were pretreated with inhibitors of TLR4 signaling (TAK-242) and NADPH oxidase (DPI) for 30 min, and the cells were then incubated with SS2 ZY05719 and PMA for 2 h. Phosphorylation of p38 MAPK (p-p38) and ERK1/2 (p-ERK1/2) were determined with western blotting. (B) Neutrophils isolated form wild-type mice and TLR knockout mice were incubated with SS2 ZY05719 and Medium.

    Article Snippet: Thereafter, the membranes were incubated with Phospho-p38 MAPK (Thr180/Thr182) (D3F9) XP ® Rabbit mAb, p38 MAPK (D13E1) XP® Rabbit mAb, Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E)XP ® Rabbit mAb, p44/42 MAPK (Erk1/2)(137F5) Rabbit mAb, Phospho-SAPK/JNK (Thr183/Tyr185) (81E11) Rabbit mAb (1:1000, Cell Signaling Technology, Danvers, MA, USA), or anti-GAPDH Rabbit pAb (1:5000, CMCTAG, Milwaukee, WI, USA) at 4°C overnight.

    Techniques: Western Blot, Incubation, Isolation, Knock-Out

    PI3K and JAK2 signaling pathways are involved in the production and activation of xanthine oxidase (XO). (A) Representative western blot of XO and tubulin expression in cardiac microvascular endothelial cells (CMECs) following hypoxia/reoxygenation (H/R). LY294002 and AG490 significantly decreased the increase in the XO protein level induced by H/R. (B) Summary data (n=3 biological replicates) of western blot analysis of XO and tubulin expression in CMECs following H/R. LY294002, SB203580 and AG490 treatment group compared with H/R group. * p<0.05 vs. H/R group. PI3K and JAK2 signaling pathways are involved in the production and activation of xanthine oxidase (XO). (C) Representative western blots of phosphorylated (p-)PI3K, total (t-)PI3K, p-JAK2, t-JAK2, p-p38 MAPK and t-p38 MAPK expression in cardiac microvascular endothelial cells (CMECs) following hypoxia/reoxygenation (H/R). H/R activates the PI3K and JAK2 signaling pathways but not the p38 MAPK signaling pathway. (D) Summary data (n=3 biological replicates) of western blot analysis of p-PI3K, t-PI3K, p-JAK2, t-JAK2, p-p38 MAPK and t-p38 MAPK expression in CMECs. ** p<0.01 vs. control group. (E) Representative data for flow cytometric analysis of DCFH-DA-stained CMECs following H/R. LY294002, SB203580 and AG490 treatment groups compared with H/R group. (F) Summary data (n=3 biological replicates) of flow cytometric analysis of DCFH-DA-stained CMECs following H/R. LY294002 (1 µ M), SB203580 (30 µ M) and AG490 (30 µ M) treatment groups compared with H/R group. * p<0.05 vs. H/R group; ** p<0.01 vs. H/R group.

    Journal: International Journal of Molecular Medicine

    Article Title: Hepatocyte growth factor inhibits hypoxia/reoxygenation-induced activation of xanthine oxidase in endothelial cells through the JAK2 signaling pathway

    doi: 10.3892/ijmm.2016.2708

    Figure Lengend Snippet: PI3K and JAK2 signaling pathways are involved in the production and activation of xanthine oxidase (XO). (A) Representative western blot of XO and tubulin expression in cardiac microvascular endothelial cells (CMECs) following hypoxia/reoxygenation (H/R). LY294002 and AG490 significantly decreased the increase in the XO protein level induced by H/R. (B) Summary data (n=3 biological replicates) of western blot analysis of XO and tubulin expression in CMECs following H/R. LY294002, SB203580 and AG490 treatment group compared with H/R group. * p<0.05 vs. H/R group. PI3K and JAK2 signaling pathways are involved in the production and activation of xanthine oxidase (XO). (C) Representative western blots of phosphorylated (p-)PI3K, total (t-)PI3K, p-JAK2, t-JAK2, p-p38 MAPK and t-p38 MAPK expression in cardiac microvascular endothelial cells (CMECs) following hypoxia/reoxygenation (H/R). H/R activates the PI3K and JAK2 signaling pathways but not the p38 MAPK signaling pathway. (D) Summary data (n=3 biological replicates) of western blot analysis of p-PI3K, t-PI3K, p-JAK2, t-JAK2, p-p38 MAPK and t-p38 MAPK expression in CMECs. ** p<0.01 vs. control group. (E) Representative data for flow cytometric analysis of DCFH-DA-stained CMECs following H/R. LY294002, SB203580 and AG490 treatment groups compared with H/R group. (F) Summary data (n=3 biological replicates) of flow cytometric analysis of DCFH-DA-stained CMECs following H/R. LY294002 (1 µ M), SB203580 (30 µ M) and AG490 (30 µ M) treatment groups compared with H/R group. * p<0.05 vs. H/R group; ** p<0.01 vs. H/R group.

    Article Snippet: Forty micrograms of protein was separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), transferred to polyvinylidene difluoride (PVDF) membranes, and then probed with antibodies for XO (#ab109235; Abcam), phospho-PI3 kinase p85 (Tyr458)/p55 (Tyr199) (#4228), PI3 kinase p85 (19H8) (#4257), phospho-p38 MAP kinase (Thr180/Thr182) (#4631), p38 MAPK (D13E1) (#8690), JAK2 (D2E12) (#3230) and phospho-JAK2 (Tyr1007/1008) (C80C3) (#3776) (all from Cell Signaling Technology, Beverly, MA, USA).

    Techniques: Activation Assay, Western Blot, Expressing, Staining

    PI3K siRNA and JAK2 siRNA downregulate the production and activation of xanthine oxidase (XO). (A) Representative western blots of p38 MAPK, PI3K, JAK2 and tubulin expression in cardiac microvascular endothelial cells (CMECs). (B) Representative western blot of XO and tubulin expression in CMECs following hypoxia/reoxygenation (H/R). PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- and negative control siRNA-transfected groups compared with H/R group. (C) Summary data (n=3 biological replicates) for western blot analysis of XO and tubulin expression in CMECs following H/R. PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- or negative control siRNA-transfected groups compared with H/R group. ** p<0.01 vs. H/R group. (D) Representative flow cytometric analysis of DCFH-DA-stained CMECs after H/R. PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- or negative control siRNA-transfected groups compared with H/R group. (E) Summary data (n=3 biological replicates) for flow cytometric analysis of DCFH-DA-stained CMECs after H/R. PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- or negative control siRNA-transfected groups compared with H/R group. ** p<0.01 vs. H/R group.

    Journal: International Journal of Molecular Medicine

    Article Title: Hepatocyte growth factor inhibits hypoxia/reoxygenation-induced activation of xanthine oxidase in endothelial cells through the JAK2 signaling pathway

    doi: 10.3892/ijmm.2016.2708

    Figure Lengend Snippet: PI3K siRNA and JAK2 siRNA downregulate the production and activation of xanthine oxidase (XO). (A) Representative western blots of p38 MAPK, PI3K, JAK2 and tubulin expression in cardiac microvascular endothelial cells (CMECs). (B) Representative western blot of XO and tubulin expression in CMECs following hypoxia/reoxygenation (H/R). PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- and negative control siRNA-transfected groups compared with H/R group. (C) Summary data (n=3 biological replicates) for western blot analysis of XO and tubulin expression in CMECs following H/R. PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- or negative control siRNA-transfected groups compared with H/R group. ** p<0.01 vs. H/R group. (D) Representative flow cytometric analysis of DCFH-DA-stained CMECs after H/R. PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- or negative control siRNA-transfected groups compared with H/R group. (E) Summary data (n=3 biological replicates) for flow cytometric analysis of DCFH-DA-stained CMECs after H/R. PI3K siRNA-, p38 MAPK siRNA-, JAK2 siRNA- or negative control siRNA-transfected groups compared with H/R group. ** p<0.01 vs. H/R group.

    Article Snippet: Forty micrograms of protein was separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), transferred to polyvinylidene difluoride (PVDF) membranes, and then probed with antibodies for XO (#ab109235; Abcam), phospho-PI3 kinase p85 (Tyr458)/p55 (Tyr199) (#4228), PI3 kinase p85 (19H8) (#4257), phospho-p38 MAP kinase (Thr180/Thr182) (#4631), p38 MAPK (D13E1) (#8690), JAK2 (D2E12) (#3230) and phospho-JAK2 (Tyr1007/1008) (C80C3) (#3776) (all from Cell Signaling Technology, Beverly, MA, USA).

    Techniques: Activation Assay, Western Blot, Expressing, Negative Control, Transfection, Staining