jnk  (Cell Signaling Technology Inc)


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    ( A ) A549 cells were treated with 15 µM embelin for 4 and 8h. Total as well as <t>phosphorylated</t> <t>ERK</t> 1/2, p38, <t>JNK</t> 1/2 and tubulin (loading control) levels were measured by Western blot as described in the “Materials and Methods” section. ( B ) Normalized values of the band intensities obtained by densitometric analysis of the data from ( A ). ( C ) Caspase-3 activity in cells pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Control values are normalized to 1 and the data indicated are the mean ± SD of three separate experiments. * indicates p<0.05 as compared with control and # indicates p<0.05 as compared with embelin treated cells.
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    1) Product Images from "Activation of p38/JNK Pathway Is Responsible for Embelin Induced Apoptosis in Lung Cancer Cells: Transitional Role of Reactive Oxygen Species"

    Article Title: Activation of p38/JNK Pathway Is Responsible for Embelin Induced Apoptosis in Lung Cancer Cells: Transitional Role of Reactive Oxygen Species

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0087050

    ( A ) A549 cells were treated with 15 µM embelin for 4 and 8h. Total as well as phosphorylated ERK 1/2, p38, JNK 1/2 and tubulin (loading control) levels were measured by Western blot as described in the “Materials and Methods” section. ( B ) Normalized values of the band intensities obtained by densitometric analysis of the data from ( A ). ( C ) Caspase-3 activity in cells pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Control values are normalized to 1 and the data indicated are the mean ± SD of three separate experiments. * indicates p<0.05 as compared with control and # indicates p<0.05 as compared with embelin treated cells.
    Figure Legend Snippet: ( A ) A549 cells were treated with 15 µM embelin for 4 and 8h. Total as well as phosphorylated ERK 1/2, p38, JNK 1/2 and tubulin (loading control) levels were measured by Western blot as described in the “Materials and Methods” section. ( B ) Normalized values of the band intensities obtained by densitometric analysis of the data from ( A ). ( C ) Caspase-3 activity in cells pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Control values are normalized to 1 and the data indicated are the mean ± SD of three separate experiments. * indicates p<0.05 as compared with control and # indicates p<0.05 as compared with embelin treated cells.

    Techniques Used: Western Blot, Activity Assay

    A549 cells were pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Total and phosphorylated levels of ERK 1/2, p38, JNK 1/2 and tubulin (loading control) were detected by Western blotting as described in the “Materials and Methods” section.
    Figure Legend Snippet: A549 cells were pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Total and phosphorylated levels of ERK 1/2, p38, JNK 1/2 and tubulin (loading control) were detected by Western blotting as described in the “Materials and Methods” section.

    Techniques Used: Western Blot

    A549 cells were pre-treated with or without the antioxidant FeTMPyP (10 µM) for 1h followed by embelin (15 µM) treatment for 4h. ( A ) Cellular levels of total and phosphorylated ERK 1/2, p38, JNK 1/2 and tubulin were detected by Western blot followed by chemiluminescence detection as described under “Materials and Methods” section. ( B ) Under similar experimental conditions as ( A ), cellular caspase-3 activity was measured as described under “Materials and Methods” section. Data presented are the mean ± SD of three separate experiments. * indicates p<0.01 as compared to control and # indicates p<0.05 as compared to embelin treated cells.
    Figure Legend Snippet: A549 cells were pre-treated with or without the antioxidant FeTMPyP (10 µM) for 1h followed by embelin (15 µM) treatment for 4h. ( A ) Cellular levels of total and phosphorylated ERK 1/2, p38, JNK 1/2 and tubulin were detected by Western blot followed by chemiluminescence detection as described under “Materials and Methods” section. ( B ) Under similar experimental conditions as ( A ), cellular caspase-3 activity was measured as described under “Materials and Methods” section. Data presented are the mean ± SD of three separate experiments. * indicates p<0.01 as compared to control and # indicates p<0.05 as compared to embelin treated cells.

    Techniques Used: Western Blot, Activity Assay

    jnk  (Cell Signaling Technology Inc)


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    ( A ) A549 cells were treated with 15 µM embelin for 4 and 8h. Total as well as <t>phosphorylated</t> <t>ERK</t> 1/2, p38, <t>JNK</t> 1/2 and tubulin (loading control) levels were measured by Western blot as described in the “Materials and Methods” section. ( B ) Normalized values of the band intensities obtained by densitometric analysis of the data from ( A ). ( C ) Caspase-3 activity in cells pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Control values are normalized to 1 and the data indicated are the mean ± SD of three separate experiments. * indicates p<0.05 as compared with control and # indicates p<0.05 as compared with embelin treated cells.
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    1) Product Images from "Activation of p38/JNK Pathway Is Responsible for Embelin Induced Apoptosis in Lung Cancer Cells: Transitional Role of Reactive Oxygen Species"

    Article Title: Activation of p38/JNK Pathway Is Responsible for Embelin Induced Apoptosis in Lung Cancer Cells: Transitional Role of Reactive Oxygen Species

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0087050

    ( A ) A549 cells were treated with 15 µM embelin for 4 and 8h. Total as well as phosphorylated ERK 1/2, p38, JNK 1/2 and tubulin (loading control) levels were measured by Western blot as described in the “Materials and Methods” section. ( B ) Normalized values of the band intensities obtained by densitometric analysis of the data from ( A ). ( C ) Caspase-3 activity in cells pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Control values are normalized to 1 and the data indicated are the mean ± SD of three separate experiments. * indicates p<0.05 as compared with control and # indicates p<0.05 as compared with embelin treated cells.
    Figure Legend Snippet: ( A ) A549 cells were treated with 15 µM embelin for 4 and 8h. Total as well as phosphorylated ERK 1/2, p38, JNK 1/2 and tubulin (loading control) levels were measured by Western blot as described in the “Materials and Methods” section. ( B ) Normalized values of the band intensities obtained by densitometric analysis of the data from ( A ). ( C ) Caspase-3 activity in cells pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Control values are normalized to 1 and the data indicated are the mean ± SD of three separate experiments. * indicates p<0.05 as compared with control and # indicates p<0.05 as compared with embelin treated cells.

    Techniques Used: Western Blot, Activity Assay

    A549 cells were pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Total and phosphorylated levels of ERK 1/2, p38, JNK 1/2 and tubulin (loading control) were detected by Western blotting as described in the “Materials and Methods” section.
    Figure Legend Snippet: A549 cells were pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Total and phosphorylated levels of ERK 1/2, p38, JNK 1/2 and tubulin (loading control) were detected by Western blotting as described in the “Materials and Methods” section.

    Techniques Used: Western Blot

    A549 cells were pre-treated with or without the antioxidant FeTMPyP (10 µM) for 1h followed by embelin (15 µM) treatment for 4h. ( A ) Cellular levels of total and phosphorylated ERK 1/2, p38, JNK 1/2 and tubulin were detected by Western blot followed by chemiluminescence detection as described under “Materials and Methods” section. ( B ) Under similar experimental conditions as ( A ), cellular caspase-3 activity was measured as described under “Materials and Methods” section. Data presented are the mean ± SD of three separate experiments. * indicates p<0.01 as compared to control and # indicates p<0.05 as compared to embelin treated cells.
    Figure Legend Snippet: A549 cells were pre-treated with or without the antioxidant FeTMPyP (10 µM) for 1h followed by embelin (15 µM) treatment for 4h. ( A ) Cellular levels of total and phosphorylated ERK 1/2, p38, JNK 1/2 and tubulin were detected by Western blot followed by chemiluminescence detection as described under “Materials and Methods” section. ( B ) Under similar experimental conditions as ( A ), cellular caspase-3 activity was measured as described under “Materials and Methods” section. Data presented are the mean ± SD of three separate experiments. * indicates p<0.01 as compared to control and # indicates p<0.05 as compared to embelin treated cells.

    Techniques Used: Western Blot, Activity Assay

    jnk  (Cell Signaling Technology Inc)


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    Effects of AgNPs and F on MAPK phosphorylation. ( A ) Representative Western blotting. Normalized densitometric values of <t>phosphorylated</t> <t>p38</t> MAPK ( B ) p42/p44 MAPK ( C ), and <t>JNK</t> MAPK ( D ). Notes: F was only able to induce p42/44 phosphorylation (* P <0.05 vs control). However, when AgNPs were also added, phosphorylation of p42/44 MAPK was enhanced (* P <0.05 vs F; ** P <0.01 vs control). Abbreviations: AgNPs, silver nanoparticles; F, fluoride; MAPK, mitogen-activated protein kinases; vs, versus.
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    1) Product Images from "Pharmacological and toxicological effects of co-exposure of human gingival fibroblasts to silver nanoparticles and sodium fluoride"

    Article Title: Pharmacological and toxicological effects of co-exposure of human gingival fibroblasts to silver nanoparticles and sodium fluoride

    Journal: International Journal of Nanomedicine

    doi: 10.2147/IJN.S59172

    Effects of AgNPs and F on MAPK phosphorylation. ( A ) Representative Western blotting. Normalized densitometric values of phosphorylated p38 MAPK ( B ) p42/p44 MAPK ( C ), and JNK MAPK ( D ). Notes: F was only able to induce p42/44 phosphorylation (* P <0.05 vs control). However, when AgNPs were also added, phosphorylation of p42/44 MAPK was enhanced (* P <0.05 vs F; ** P <0.01 vs control). Abbreviations: AgNPs, silver nanoparticles; F, fluoride; MAPK, mitogen-activated protein kinases; vs, versus.
    Figure Legend Snippet: Effects of AgNPs and F on MAPK phosphorylation. ( A ) Representative Western blotting. Normalized densitometric values of phosphorylated p38 MAPK ( B ) p42/p44 MAPK ( C ), and JNK MAPK ( D ). Notes: F was only able to induce p42/44 phosphorylation (* P <0.05 vs control). However, when AgNPs were also added, phosphorylation of p42/44 MAPK was enhanced (* P <0.05 vs F; ** P <0.01 vs control). Abbreviations: AgNPs, silver nanoparticles; F, fluoride; MAPK, mitogen-activated protein kinases; vs, versus.

    Techniques Used: Western Blot

    p sapk jnk  (Cell Signaling Technology Inc)


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    P Sapk Jnk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Inhibiting Cx43 on HUVECs could attenuate U937-HUVEC adhesion via modulating the MAPK signaling pathway. (a) Effects of two kinds of Cx43-siRNAs on the activation of MAPKs <t>(p-ERK/ERK,</t> <t>p-p38/p38,</t> and <t>p-JNK/JNK)</t> ( n = 4, ∗ P < 0.05 vs. control). Control group means lipofectamine 2000 pretreatment group; NC: negative control (negative control has random base sequence that differs from Cx43-siRNA1 and Cx43-siRNA1). (b–d) The contents of MCP-1, sICAM-1, and sVCAM-1 when HUVECs were pretreated with U0126 (inhibiting p-ERK1/2, 10 μ M, 24 hours), SB202190 (inhibiting p38, 10 μ M, 24 hours), and SP600125 (inhibiting p-JNK1/2, 10 μ M, 24 hours) ( n = 5, ∗ P < 0.05 vs. control). (e) The changes of U937-HUVEC adhesion when HUVECs were pretreated with U0126, SB202190, and SP600125 ( n = 5, ∗ P < 0.05 vs. control). The solvents of U0126, SB202190, and SP600125 were DMSO, which had no effects on the above results. (b–e) The control group is just DMSO pretreatment. In all experiments, HUVECs were all pretreated with TNF- α (10 ng/ml, 12 h). Effects of TNF- α are showed in Supplemental .
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    1) Product Images from "Dexmedetomidine Attenuates Monocyte-Endothelial Adherence via Inhibiting Connexin43 on Vascular Endothelial Cells"

    Article Title: Dexmedetomidine Attenuates Monocyte-Endothelial Adherence via Inhibiting Connexin43 on Vascular Endothelial Cells

    Journal: Mediators of Inflammation

    doi: 10.1155/2020/7039854

    Inhibiting Cx43 on HUVECs could attenuate U937-HUVEC adhesion via modulating the MAPK signaling pathway. (a) Effects of two kinds of Cx43-siRNAs on the activation of MAPKs (p-ERK/ERK, p-p38/p38, and p-JNK/JNK) ( n = 4, ∗ P < 0.05 vs. control). Control group means lipofectamine 2000 pretreatment group; NC: negative control (negative control has random base sequence that differs from Cx43-siRNA1 and Cx43-siRNA1). (b–d) The contents of MCP-1, sICAM-1, and sVCAM-1 when HUVECs were pretreated with U0126 (inhibiting p-ERK1/2, 10 μ M, 24 hours), SB202190 (inhibiting p38, 10 μ M, 24 hours), and SP600125 (inhibiting p-JNK1/2, 10 μ M, 24 hours) ( n = 5, ∗ P < 0.05 vs. control). (e) The changes of U937-HUVEC adhesion when HUVECs were pretreated with U0126, SB202190, and SP600125 ( n = 5, ∗ P < 0.05 vs. control). The solvents of U0126, SB202190, and SP600125 were DMSO, which had no effects on the above results. (b–e) The control group is just DMSO pretreatment. In all experiments, HUVECs were all pretreated with TNF- α (10 ng/ml, 12 h). Effects of TNF- α are showed in Supplemental .
    Figure Legend Snippet: Inhibiting Cx43 on HUVECs could attenuate U937-HUVEC adhesion via modulating the MAPK signaling pathway. (a) Effects of two kinds of Cx43-siRNAs on the activation of MAPKs (p-ERK/ERK, p-p38/p38, and p-JNK/JNK) ( n = 4, ∗ P < 0.05 vs. control). Control group means lipofectamine 2000 pretreatment group; NC: negative control (negative control has random base sequence that differs from Cx43-siRNA1 and Cx43-siRNA1). (b–d) The contents of MCP-1, sICAM-1, and sVCAM-1 when HUVECs were pretreated with U0126 (inhibiting p-ERK1/2, 10 μ M, 24 hours), SB202190 (inhibiting p38, 10 μ M, 24 hours), and SP600125 (inhibiting p-JNK1/2, 10 μ M, 24 hours) ( n = 5, ∗ P < 0.05 vs. control). (e) The changes of U937-HUVEC adhesion when HUVECs were pretreated with U0126, SB202190, and SP600125 ( n = 5, ∗ P < 0.05 vs. control). The solvents of U0126, SB202190, and SP600125 were DMSO, which had no effects on the above results. (b–e) The control group is just DMSO pretreatment. In all experiments, HUVECs were all pretreated with TNF- α (10 ng/ml, 12 h). Effects of TNF- α are showed in Supplemental .

    Techniques Used: Activation Assay, Negative Control, Sequencing

    Dexmedetomidine attenuated U937-HUVEC adhesion, as well as the contents of MCP-1, sICAM-1, and sVCAM-1. (a) Effects of dexmedetomidine (Dexm: 0.1 nM and 1 nM, 24 hours) on the activation of MAPKs (p-ERK/ERK, p-p38/p38, and p-JNK/JNK) ( n = 4, ∗ P < 0.05 vs. control). (b–d) The contents of MCP-1, sICAM-1, and sVCAM-1 when HUVECs were pretreated with dexmedetomidine (Dexm: 0.1 nM and 1 nM, 24 hours) ( n = 4, ∗ P < 0.05 vs. control; # P < 0.05 vs. 0.1 nM group). (e) The changes of U937-HUVEC adhesion when HUVECs were pretreated with dexmedetomidine (Dexm: 0.1 nM and 1 nM, 24 hours) ( n = 4, ∗ P < 0.05 vs. control; # P < 0.05 vs. 0.1 nM group). In all experiments, HUVECs were all pretreated with TNF- α (10 ng/ml, 12 h). Effects of TNF- α are showed in Supplemental .
    Figure Legend Snippet: Dexmedetomidine attenuated U937-HUVEC adhesion, as well as the contents of MCP-1, sICAM-1, and sVCAM-1. (a) Effects of dexmedetomidine (Dexm: 0.1 nM and 1 nM, 24 hours) on the activation of MAPKs (p-ERK/ERK, p-p38/p38, and p-JNK/JNK) ( n = 4, ∗ P < 0.05 vs. control). (b–d) The contents of MCP-1, sICAM-1, and sVCAM-1 when HUVECs were pretreated with dexmedetomidine (Dexm: 0.1 nM and 1 nM, 24 hours) ( n = 4, ∗ P < 0.05 vs. control; # P < 0.05 vs. 0.1 nM group). (e) The changes of U937-HUVEC adhesion when HUVECs were pretreated with dexmedetomidine (Dexm: 0.1 nM and 1 nM, 24 hours) ( n = 4, ∗ P < 0.05 vs. control; # P < 0.05 vs. 0.1 nM group). In all experiments, HUVECs were all pretreated with TNF- α (10 ng/ml, 12 h). Effects of TNF- α are showed in Supplemental .

    Techniques Used: Activation Assay

    total jnk  (Cell Signaling Technology Inc)


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    C57 mice were injected intravenously with AAV 2/8 LSP.dnMstat and after one week the animals were sacrificed. Immunoblotting for total and phosphorylated <t>Smad2/3,</t> <t>Akt</t> and <t>JNK</t> was performed on protein homogenates of quadriceps muscle using beta-actin as a loading control. In dnMstat treated C57 quadriceps there was a (a) 41% decrease in phosphorylated Smad 2/3, (b) 59% increase in phosphorylated Akt and (c) 31% decrease in phosphorylated JNK. Data represent mean±SD. * Statistically significant compared to control, p<0.05.
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    1) Product Images from "Systemic Myostatin Inhibition via Liver-Targeted Gene Transfer in Normal and Dystrophic Mice"

    Article Title: Systemic Myostatin Inhibition via Liver-Targeted Gene Transfer in Normal and Dystrophic Mice

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0009176

    C57 mice were injected intravenously with AAV 2/8 LSP.dnMstat and after one week the animals were sacrificed. Immunoblotting for total and phosphorylated Smad2/3, Akt and JNK was performed on protein homogenates of quadriceps muscle using beta-actin as a loading control. In dnMstat treated C57 quadriceps there was a (a) 41% decrease in phosphorylated Smad 2/3, (b) 59% increase in phosphorylated Akt and (c) 31% decrease in phosphorylated JNK. Data represent mean±SD. * Statistically significant compared to control, p<0.05.
    Figure Legend Snippet: C57 mice were injected intravenously with AAV 2/8 LSP.dnMstat and after one week the animals were sacrificed. Immunoblotting for total and phosphorylated Smad2/3, Akt and JNK was performed on protein homogenates of quadriceps muscle using beta-actin as a loading control. In dnMstat treated C57 quadriceps there was a (a) 41% decrease in phosphorylated Smad 2/3, (b) 59% increase in phosphorylated Akt and (c) 31% decrease in phosphorylated JNK. Data represent mean±SD. * Statistically significant compared to control, p<0.05.

    Techniques Used: Injection, Western Blot

    jnk  (Cell Signaling Technology Inc)


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    A–B. MIN6 cells pretreated with 30 µM PD98059 (PD) or 50 µM SP600125 (SP) for 2 h were stimulated with 11.6 nM MCP-1 for 5 <t>min.</t> <t>ERK1/2</t> or <t>JNK</t> phosphorylation was examined by Western blot. The experiments were performed at least three times and representative results are shown. C. MIN6 cells were incubated with control medium (CM), 30 µM PD98059 (PD) or 50 µM SP600125 (SP) for 1 h, then stimulated with 11.6 nM MCP-1 for 9 h and examined for amylin expression by real-time PCR. * p <0.05 vs cells cultured with CM. # p <0.05 compared with cells treated with MCP-1 alone. Mean±SD of three independent experiments.
    Jnk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "MCP-1 Upregulates Amylin Expression in Murine Pancreatic β Cells through ERK/JNK-AP1 and NF-κB Related Signaling Pathways Independent of CCR2"

    Article Title: MCP-1 Upregulates Amylin Expression in Murine Pancreatic β Cells through ERK/JNK-AP1 and NF-κB Related Signaling Pathways Independent of CCR2

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0019559

    A–B. MIN6 cells pretreated with 30 µM PD98059 (PD) or 50 µM SP600125 (SP) for 2 h were stimulated with 11.6 nM MCP-1 for 5 min. ERK1/2 or JNK phosphorylation was examined by Western blot. The experiments were performed at least three times and representative results are shown. C. MIN6 cells were incubated with control medium (CM), 30 µM PD98059 (PD) or 50 µM SP600125 (SP) for 1 h, then stimulated with 11.6 nM MCP-1 for 9 h and examined for amylin expression by real-time PCR. * p <0.05 vs cells cultured with CM. # p <0.05 compared with cells treated with MCP-1 alone. Mean±SD of three independent experiments.
    Figure Legend Snippet: A–B. MIN6 cells pretreated with 30 µM PD98059 (PD) or 50 µM SP600125 (SP) for 2 h were stimulated with 11.6 nM MCP-1 for 5 min. ERK1/2 or JNK phosphorylation was examined by Western blot. The experiments were performed at least three times and representative results are shown. C. MIN6 cells were incubated with control medium (CM), 30 µM PD98059 (PD) or 50 µM SP600125 (SP) for 1 h, then stimulated with 11.6 nM MCP-1 for 9 h and examined for amylin expression by real-time PCR. * p <0.05 vs cells cultured with CM. # p <0.05 compared with cells treated with MCP-1 alone. Mean±SD of three independent experiments.

    Techniques Used: Western Blot, Incubation, Expressing, Real-time Polymerase Chain Reaction, Cell Culture

    phospho sapk jnk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho sapk jnk
    ( A ) MIA PaCa-2 control and FOXM1 knockdown pancreatic cancer cells were γ-irradiated with the indicated doses. Seventy-two hours following irradiation cells were harvested and immunoblotting was carried out with antibodies specific for <t>Phospho/Total-SAPK/JNK</t> and cleaved caspase-3. β-actin was used as the loading control. ( B ) MIA PaCa-2 FOXM1 knockdown pancreatic cancer cells were preincubated for 1 hour with 10 µM of JNK inhibitor, SP600125 and then were γ-irradiated as indicated. Forty-eight hours following irradiation cells were harvested and immunoblotting was performed for cleaved caspase-3 and β-actin as the loading control. ( C ) The graphs show mean values ± SEM of four independent experiments. ( D ) MDA-MB-231 FOXM1 knockdown breast cancer cells were preincubated for 1 hour with 10 µM of JNK inhibitor, SP600125 and then were subjected to γ-irradiation with the indicated doses. Seventy-two hours after irradiation cells were harvested and immunoblotting was performed with cleaved caspase-3 and β-actin antibodies. ( E ) The graphs show mean values ± SEM of two independent experiments. ( F ) Pancreatic MIA PaCa-2 control and FOXM1 knockdown cancer cells were subjected to ionizing radiation with the indicated doses. Thirty-six hours following irradiation cells were harvested and immunoblotting was carried out with antibodies specific for Bcl-2 and Bcl-xL. β-actin was used as the loading control. ( G ) Breast MDA-MB-231 control and FOXM1 knockdown cancer cells were γ-irradiated as indicated. Seventy-two hours following irradiation cells were harvested and immunoblotting was performed for Bcl-2. β-actin was used as the loading control. ( H ) MIA PaCa-2 control and FOXM1 knockdown pancreatic cancer cells were harvested for RNA extraction. Quantitative RT-PCR was carried out with Bcl-2 and cyclophilin primers. The graph demonstrates mean values ±SEM of three independent experiments. ( I ) To extract RNA MDA-MB-231 control and FOXM1 knockdown breast cancer cells were harvested. Using Bcl-2 and cyclophlin primers qRT-PCR was performed. The graph shows mean values ±SEM of three independent experiments.
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    Images

    1) Product Images from "Suppression of FOXM1 Sensitizes Human Cancer Cells to Cell Death Induced by DNA-Damage"

    Article Title: Suppression of FOXM1 Sensitizes Human Cancer Cells to Cell Death Induced by DNA-Damage

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0031761

    ( A ) MIA PaCa-2 control and FOXM1 knockdown pancreatic cancer cells were γ-irradiated with the indicated doses. Seventy-two hours following irradiation cells were harvested and immunoblotting was carried out with antibodies specific for Phospho/Total-SAPK/JNK and cleaved caspase-3. β-actin was used as the loading control. ( B ) MIA PaCa-2 FOXM1 knockdown pancreatic cancer cells were preincubated for 1 hour with 10 µM of JNK inhibitor, SP600125 and then were γ-irradiated as indicated. Forty-eight hours following irradiation cells were harvested and immunoblotting was performed for cleaved caspase-3 and β-actin as the loading control. ( C ) The graphs show mean values ± SEM of four independent experiments. ( D ) MDA-MB-231 FOXM1 knockdown breast cancer cells were preincubated for 1 hour with 10 µM of JNK inhibitor, SP600125 and then were subjected to γ-irradiation with the indicated doses. Seventy-two hours after irradiation cells were harvested and immunoblotting was performed with cleaved caspase-3 and β-actin antibodies. ( E ) The graphs show mean values ± SEM of two independent experiments. ( F ) Pancreatic MIA PaCa-2 control and FOXM1 knockdown cancer cells were subjected to ionizing radiation with the indicated doses. Thirty-six hours following irradiation cells were harvested and immunoblotting was carried out with antibodies specific for Bcl-2 and Bcl-xL. β-actin was used as the loading control. ( G ) Breast MDA-MB-231 control and FOXM1 knockdown cancer cells were γ-irradiated as indicated. Seventy-two hours following irradiation cells were harvested and immunoblotting was performed for Bcl-2. β-actin was used as the loading control. ( H ) MIA PaCa-2 control and FOXM1 knockdown pancreatic cancer cells were harvested for RNA extraction. Quantitative RT-PCR was carried out with Bcl-2 and cyclophilin primers. The graph demonstrates mean values ±SEM of three independent experiments. ( I ) To extract RNA MDA-MB-231 control and FOXM1 knockdown breast cancer cells were harvested. Using Bcl-2 and cyclophlin primers qRT-PCR was performed. The graph shows mean values ±SEM of three independent experiments.
    Figure Legend Snippet: ( A ) MIA PaCa-2 control and FOXM1 knockdown pancreatic cancer cells were γ-irradiated with the indicated doses. Seventy-two hours following irradiation cells were harvested and immunoblotting was carried out with antibodies specific for Phospho/Total-SAPK/JNK and cleaved caspase-3. β-actin was used as the loading control. ( B ) MIA PaCa-2 FOXM1 knockdown pancreatic cancer cells were preincubated for 1 hour with 10 µM of JNK inhibitor, SP600125 and then were γ-irradiated as indicated. Forty-eight hours following irradiation cells were harvested and immunoblotting was performed for cleaved caspase-3 and β-actin as the loading control. ( C ) The graphs show mean values ± SEM of four independent experiments. ( D ) MDA-MB-231 FOXM1 knockdown breast cancer cells were preincubated for 1 hour with 10 µM of JNK inhibitor, SP600125 and then were subjected to γ-irradiation with the indicated doses. Seventy-two hours after irradiation cells were harvested and immunoblotting was performed with cleaved caspase-3 and β-actin antibodies. ( E ) The graphs show mean values ± SEM of two independent experiments. ( F ) Pancreatic MIA PaCa-2 control and FOXM1 knockdown cancer cells were subjected to ionizing radiation with the indicated doses. Thirty-six hours following irradiation cells were harvested and immunoblotting was carried out with antibodies specific for Bcl-2 and Bcl-xL. β-actin was used as the loading control. ( G ) Breast MDA-MB-231 control and FOXM1 knockdown cancer cells were γ-irradiated as indicated. Seventy-two hours following irradiation cells were harvested and immunoblotting was performed for Bcl-2. β-actin was used as the loading control. ( H ) MIA PaCa-2 control and FOXM1 knockdown pancreatic cancer cells were harvested for RNA extraction. Quantitative RT-PCR was carried out with Bcl-2 and cyclophilin primers. The graph demonstrates mean values ±SEM of three independent experiments. ( I ) To extract RNA MDA-MB-231 control and FOXM1 knockdown breast cancer cells were harvested. Using Bcl-2 and cyclophlin primers qRT-PCR was performed. The graph shows mean values ±SEM of three independent experiments.

    Techniques Used: Irradiation, Western Blot, RNA Extraction, Quantitative RT-PCR

    sapk jnk kinase assay  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc sapk jnk kinase assay
    Sapk Jnk Kinase Assay, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    p jnk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p jnk
    Methimazole attenuated the increased expression of <t>phosphorylated</t> <t>JNK</t> and ERK proteins (30 minutes). (a) Methimazole prevented the increased expression of p-ERK in scratched astrocytes. (b) Methimazole prevented the increased expression of <t>p-JNK</t> in scratched astrocytes. All values were expressed as mean ± SEM, n = 5. ∗ p < 0.05 vs. control; # p < 0.05 vs. scratch.
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    1) Product Images from "Methimazole Inhibits the Expression of GFAP and the Migration of Astrocyte in Scratched Wound Model In Vitro"

    Article Title: Methimazole Inhibits the Expression of GFAP and the Migration of Astrocyte in Scratched Wound Model In Vitro

    Journal: Mediators of Inflammation

    doi: 10.1155/2020/4027470

    Methimazole attenuated the increased expression of phosphorylated JNK and ERK proteins (30 minutes). (a) Methimazole prevented the increased expression of p-ERK in scratched astrocytes. (b) Methimazole prevented the increased expression of p-JNK in scratched astrocytes. All values were expressed as mean ± SEM, n = 5. ∗ p < 0.05 vs. control; # p < 0.05 vs. scratch.
    Figure Legend Snippet: Methimazole attenuated the increased expression of phosphorylated JNK and ERK proteins (30 minutes). (a) Methimazole prevented the increased expression of p-ERK in scratched astrocytes. (b) Methimazole prevented the increased expression of p-JNK in scratched astrocytes. All values were expressed as mean ± SEM, n = 5. ∗ p < 0.05 vs. control; # p < 0.05 vs. scratch.

    Techniques Used: Expressing

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    Cell Signaling Technology Inc jnk
    ( A ) A549 cells were treated with 15 µM embelin for 4 and 8h. Total as well as <t>phosphorylated</t> <t>ERK</t> 1/2, p38, <t>JNK</t> 1/2 and tubulin (loading control) levels were measured by Western blot as described in the “Materials and Methods” section. ( B ) Normalized values of the band intensities obtained by densitometric analysis of the data from ( A ). ( C ) Caspase-3 activity in cells pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Control values are normalized to 1 and the data indicated are the mean ± SD of three separate experiments. * indicates p<0.05 as compared with control and # indicates p<0.05 as compared with embelin treated cells.
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    Cell Signaling Technology Inc p sapk jnk
    ( A ) A549 cells were treated with 15 µM embelin for 4 and 8h. Total as well as <t>phosphorylated</t> <t>ERK</t> 1/2, p38, <t>JNK</t> 1/2 and tubulin (loading control) levels were measured by Western blot as described in the “Materials and Methods” section. ( B ) Normalized values of the band intensities obtained by densitometric analysis of the data from ( A ). ( C ) Caspase-3 activity in cells pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Control values are normalized to 1 and the data indicated are the mean ± SD of three separate experiments. * indicates p<0.05 as compared with control and # indicates p<0.05 as compared with embelin treated cells.
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    Cell Signaling Technology Inc sapk jnk
    ( A ) A549 cells were treated with 15 µM embelin for 4 and 8h. Total as well as <t>phosphorylated</t> <t>ERK</t> 1/2, p38, <t>JNK</t> 1/2 and tubulin (loading control) levels were measured by Western blot as described in the “Materials and Methods” section. ( B ) Normalized values of the band intensities obtained by densitometric analysis of the data from ( A ). ( C ) Caspase-3 activity in cells pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Control values are normalized to 1 and the data indicated are the mean ± SD of three separate experiments. * indicates p<0.05 as compared with control and # indicates p<0.05 as compared with embelin treated cells.
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    Cell Signaling Technology Inc total jnk
    C57 mice were injected intravenously with AAV 2/8 LSP.dnMstat and after one week the animals were sacrificed. Immunoblotting for total and phosphorylated <t>Smad2/3,</t> <t>Akt</t> and <t>JNK</t> was performed on protein homogenates of quadriceps muscle using beta-actin as a loading control. In dnMstat treated C57 quadriceps there was a (a) 41% decrease in phosphorylated Smad 2/3, (b) 59% increase in phosphorylated Akt and (c) 31% decrease in phosphorylated JNK. Data represent mean±SD. * Statistically significant compared to control, p<0.05.
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    Cell Signaling Technology Inc phospho sapk jnk
    ( A ) MIA PaCa-2 control and FOXM1 knockdown pancreatic cancer cells were γ-irradiated with the indicated doses. Seventy-two hours following irradiation cells were harvested and immunoblotting was carried out with antibodies specific for <t>Phospho/Total-SAPK/JNK</t> and cleaved caspase-3. β-actin was used as the loading control. ( B ) MIA PaCa-2 FOXM1 knockdown pancreatic cancer cells were preincubated for 1 hour with 10 µM of JNK inhibitor, SP600125 and then were γ-irradiated as indicated. Forty-eight hours following irradiation cells were harvested and immunoblotting was performed for cleaved caspase-3 and β-actin as the loading control. ( C ) The graphs show mean values ± SEM of four independent experiments. ( D ) MDA-MB-231 FOXM1 knockdown breast cancer cells were preincubated for 1 hour with 10 µM of JNK inhibitor, SP600125 and then were subjected to γ-irradiation with the indicated doses. Seventy-two hours after irradiation cells were harvested and immunoblotting was performed with cleaved caspase-3 and β-actin antibodies. ( E ) The graphs show mean values ± SEM of two independent experiments. ( F ) Pancreatic MIA PaCa-2 control and FOXM1 knockdown cancer cells were subjected to ionizing radiation with the indicated doses. Thirty-six hours following irradiation cells were harvested and immunoblotting was carried out with antibodies specific for Bcl-2 and Bcl-xL. β-actin was used as the loading control. ( G ) Breast MDA-MB-231 control and FOXM1 knockdown cancer cells were γ-irradiated as indicated. Seventy-two hours following irradiation cells were harvested and immunoblotting was performed for Bcl-2. β-actin was used as the loading control. ( H ) MIA PaCa-2 control and FOXM1 knockdown pancreatic cancer cells were harvested for RNA extraction. Quantitative RT-PCR was carried out with Bcl-2 and cyclophilin primers. The graph demonstrates mean values ±SEM of three independent experiments. ( I ) To extract RNA MDA-MB-231 control and FOXM1 knockdown breast cancer cells were harvested. Using Bcl-2 and cyclophlin primers qRT-PCR was performed. The graph shows mean values ±SEM of three independent experiments.
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    ( A ) MIA PaCa-2 control and FOXM1 knockdown pancreatic cancer cells were γ-irradiated with the indicated doses. Seventy-two hours following irradiation cells were harvested and immunoblotting was carried out with antibodies specific for <t>Phospho/Total-SAPK/JNK</t> and cleaved caspase-3. β-actin was used as the loading control. ( B ) MIA PaCa-2 FOXM1 knockdown pancreatic cancer cells were preincubated for 1 hour with 10 µM of JNK inhibitor, SP600125 and then were γ-irradiated as indicated. Forty-eight hours following irradiation cells were harvested and immunoblotting was performed for cleaved caspase-3 and β-actin as the loading control. ( C ) The graphs show mean values ± SEM of four independent experiments. ( D ) MDA-MB-231 FOXM1 knockdown breast cancer cells were preincubated for 1 hour with 10 µM of JNK inhibitor, SP600125 and then were subjected to γ-irradiation with the indicated doses. Seventy-two hours after irradiation cells were harvested and immunoblotting was performed with cleaved caspase-3 and β-actin antibodies. ( E ) The graphs show mean values ± SEM of two independent experiments. ( F ) Pancreatic MIA PaCa-2 control and FOXM1 knockdown cancer cells were subjected to ionizing radiation with the indicated doses. Thirty-six hours following irradiation cells were harvested and immunoblotting was carried out with antibodies specific for Bcl-2 and Bcl-xL. β-actin was used as the loading control. ( G ) Breast MDA-MB-231 control and FOXM1 knockdown cancer cells were γ-irradiated as indicated. Seventy-two hours following irradiation cells were harvested and immunoblotting was performed for Bcl-2. β-actin was used as the loading control. ( H ) MIA PaCa-2 control and FOXM1 knockdown pancreatic cancer cells were harvested for RNA extraction. Quantitative RT-PCR was carried out with Bcl-2 and cyclophilin primers. The graph demonstrates mean values ±SEM of three independent experiments. ( I ) To extract RNA MDA-MB-231 control and FOXM1 knockdown breast cancer cells were harvested. Using Bcl-2 and cyclophlin primers qRT-PCR was performed. The graph shows mean values ±SEM of three independent experiments.
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    Methimazole attenuated the increased expression of <t>phosphorylated</t> <t>JNK</t> and ERK proteins (30 minutes). (a) Methimazole prevented the increased expression of p-ERK in scratched astrocytes. (b) Methimazole prevented the increased expression of <t>p-JNK</t> in scratched astrocytes. All values were expressed as mean ± SEM, n = 5. ∗ p < 0.05 vs. control; # p < 0.05 vs. scratch.
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    ( A ) A549 cells were treated with 15 µM embelin for 4 and 8h. Total as well as phosphorylated ERK 1/2, p38, JNK 1/2 and tubulin (loading control) levels were measured by Western blot as described in the “Materials and Methods” section. ( B ) Normalized values of the band intensities obtained by densitometric analysis of the data from ( A ). ( C ) Caspase-3 activity in cells pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Control values are normalized to 1 and the data indicated are the mean ± SD of three separate experiments. * indicates p<0.05 as compared with control and # indicates p<0.05 as compared with embelin treated cells.

    Journal: PLoS ONE

    Article Title: Activation of p38/JNK Pathway Is Responsible for Embelin Induced Apoptosis in Lung Cancer Cells: Transitional Role of Reactive Oxygen Species

    doi: 10.1371/journal.pone.0087050

    Figure Lengend Snippet: ( A ) A549 cells were treated with 15 µM embelin for 4 and 8h. Total as well as phosphorylated ERK 1/2, p38, JNK 1/2 and tubulin (loading control) levels were measured by Western blot as described in the “Materials and Methods” section. ( B ) Normalized values of the band intensities obtained by densitometric analysis of the data from ( A ). ( C ) Caspase-3 activity in cells pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Control values are normalized to 1 and the data indicated are the mean ± SD of three separate experiments. * indicates p<0.05 as compared with control and # indicates p<0.05 as compared with embelin treated cells.

    Article Snippet: Blots were probed with monoclonal antibodies raised against total and phospho specific antibodies for ERK 1/2, p38, JNK (Cell Signaling Technology); and tubulin (Sigma-Aldrich).

    Techniques: Western Blot, Activity Assay

    A549 cells were pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Total and phosphorylated levels of ERK 1/2, p38, JNK 1/2 and tubulin (loading control) were detected by Western blotting as described in the “Materials and Methods” section.

    Journal: PLoS ONE

    Article Title: Activation of p38/JNK Pathway Is Responsible for Embelin Induced Apoptosis in Lung Cancer Cells: Transitional Role of Reactive Oxygen Species

    doi: 10.1371/journal.pone.0087050

    Figure Lengend Snippet: A549 cells were pre-treated with or without U0126 (5 µM), PD169316 (5 µM), SP600125 (5 µM) for 1h followed by embelin (15 µM) for 4h. Total and phosphorylated levels of ERK 1/2, p38, JNK 1/2 and tubulin (loading control) were detected by Western blotting as described in the “Materials and Methods” section.

    Article Snippet: Blots were probed with monoclonal antibodies raised against total and phospho specific antibodies for ERK 1/2, p38, JNK (Cell Signaling Technology); and tubulin (Sigma-Aldrich).

    Techniques: Western Blot

    A549 cells were pre-treated with or without the antioxidant FeTMPyP (10 µM) for 1h followed by embelin (15 µM) treatment for 4h. ( A ) Cellular levels of total and phosphorylated ERK 1/2, p38, JNK 1/2 and tubulin were detected by Western blot followed by chemiluminescence detection as described under “Materials and Methods” section. ( B ) Under similar experimental conditions as ( A ), cellular caspase-3 activity was measured as described under “Materials and Methods” section. Data presented are the mean ± SD of three separate experiments. * indicates p<0.01 as compared to control and # indicates p<0.05 as compared to embelin treated cells.

    Journal: PLoS ONE

    Article Title: Activation of p38/JNK Pathway Is Responsible for Embelin Induced Apoptosis in Lung Cancer Cells: Transitional Role of Reactive Oxygen Species

    doi: 10.1371/journal.pone.0087050

    Figure Lengend Snippet: A549 cells were pre-treated with or without the antioxidant FeTMPyP (10 µM) for 1h followed by embelin (15 µM) treatment for 4h. ( A ) Cellular levels of total and phosphorylated ERK 1/2, p38, JNK 1/2 and tubulin were detected by Western blot followed by chemiluminescence detection as described under “Materials and Methods” section. ( B ) Under similar experimental conditions as ( A ), cellular caspase-3 activity was measured as described under “Materials and Methods” section. Data presented are the mean ± SD of three separate experiments. * indicates p<0.01 as compared to control and # indicates p<0.05 as compared to embelin treated cells.

    Article Snippet: Blots were probed with monoclonal antibodies raised against total and phospho specific antibodies for ERK 1/2, p38, JNK (Cell Signaling Technology); and tubulin (Sigma-Aldrich).

    Techniques: Western Blot, Activity Assay

    C57 mice were injected intravenously with AAV 2/8 LSP.dnMstat and after one week the animals were sacrificed. Immunoblotting for total and phosphorylated Smad2/3, Akt and JNK was performed on protein homogenates of quadriceps muscle using beta-actin as a loading control. In dnMstat treated C57 quadriceps there was a (a) 41% decrease in phosphorylated Smad 2/3, (b) 59% increase in phosphorylated Akt and (c) 31% decrease in phosphorylated JNK. Data represent mean±SD. * Statistically significant compared to control, p<0.05.

    Journal: PLoS ONE

    Article Title: Systemic Myostatin Inhibition via Liver-Targeted Gene Transfer in Normal and Dystrophic Mice

    doi: 10.1371/journal.pone.0009176

    Figure Lengend Snippet: C57 mice were injected intravenously with AAV 2/8 LSP.dnMstat and after one week the animals were sacrificed. Immunoblotting for total and phosphorylated Smad2/3, Akt and JNK was performed on protein homogenates of quadriceps muscle using beta-actin as a loading control. In dnMstat treated C57 quadriceps there was a (a) 41% decrease in phosphorylated Smad 2/3, (b) 59% increase in phosphorylated Akt and (c) 31% decrease in phosphorylated JNK. Data represent mean±SD. * Statistically significant compared to control, p<0.05.

    Article Snippet: Se Jin Lee), phospho-Smad 2/3 (1∶500, Millipore, Temecula, CA), Smad 2/3 (1∶1000, Cell Signaling Technology, Danvers, MA), activin IIB receptor (1∶500, Sigma, St. Louis, MO), phospho-Akt and total Akt (1∶1000, Cell Signaling Technology, Danvers, MA), phospho-JNK and total JNK (1∶1000, Cell Signaling Technology, Danvers, MA), and actin (1∶2000, Sigma, St. Louis, MO).

    Techniques: Injection, Western Blot

    ( A ) MIA PaCa-2 control and FOXM1 knockdown pancreatic cancer cells were γ-irradiated with the indicated doses. Seventy-two hours following irradiation cells were harvested and immunoblotting was carried out with antibodies specific for Phospho/Total-SAPK/JNK and cleaved caspase-3. β-actin was used as the loading control. ( B ) MIA PaCa-2 FOXM1 knockdown pancreatic cancer cells were preincubated for 1 hour with 10 µM of JNK inhibitor, SP600125 and then were γ-irradiated as indicated. Forty-eight hours following irradiation cells were harvested and immunoblotting was performed for cleaved caspase-3 and β-actin as the loading control. ( C ) The graphs show mean values ± SEM of four independent experiments. ( D ) MDA-MB-231 FOXM1 knockdown breast cancer cells were preincubated for 1 hour with 10 µM of JNK inhibitor, SP600125 and then were subjected to γ-irradiation with the indicated doses. Seventy-two hours after irradiation cells were harvested and immunoblotting was performed with cleaved caspase-3 and β-actin antibodies. ( E ) The graphs show mean values ± SEM of two independent experiments. ( F ) Pancreatic MIA PaCa-2 control and FOXM1 knockdown cancer cells were subjected to ionizing radiation with the indicated doses. Thirty-six hours following irradiation cells were harvested and immunoblotting was carried out with antibodies specific for Bcl-2 and Bcl-xL. β-actin was used as the loading control. ( G ) Breast MDA-MB-231 control and FOXM1 knockdown cancer cells were γ-irradiated as indicated. Seventy-two hours following irradiation cells were harvested and immunoblotting was performed for Bcl-2. β-actin was used as the loading control. ( H ) MIA PaCa-2 control and FOXM1 knockdown pancreatic cancer cells were harvested for RNA extraction. Quantitative RT-PCR was carried out with Bcl-2 and cyclophilin primers. The graph demonstrates mean values ±SEM of three independent experiments. ( I ) To extract RNA MDA-MB-231 control and FOXM1 knockdown breast cancer cells were harvested. Using Bcl-2 and cyclophlin primers qRT-PCR was performed. The graph shows mean values ±SEM of three independent experiments.

    Journal: PLoS ONE

    Article Title: Suppression of FOXM1 Sensitizes Human Cancer Cells to Cell Death Induced by DNA-Damage

    doi: 10.1371/journal.pone.0031761

    Figure Lengend Snippet: ( A ) MIA PaCa-2 control and FOXM1 knockdown pancreatic cancer cells were γ-irradiated with the indicated doses. Seventy-two hours following irradiation cells were harvested and immunoblotting was carried out with antibodies specific for Phospho/Total-SAPK/JNK and cleaved caspase-3. β-actin was used as the loading control. ( B ) MIA PaCa-2 FOXM1 knockdown pancreatic cancer cells were preincubated for 1 hour with 10 µM of JNK inhibitor, SP600125 and then were γ-irradiated as indicated. Forty-eight hours following irradiation cells were harvested and immunoblotting was performed for cleaved caspase-3 and β-actin as the loading control. ( C ) The graphs show mean values ± SEM of four independent experiments. ( D ) MDA-MB-231 FOXM1 knockdown breast cancer cells were preincubated for 1 hour with 10 µM of JNK inhibitor, SP600125 and then were subjected to γ-irradiation with the indicated doses. Seventy-two hours after irradiation cells were harvested and immunoblotting was performed with cleaved caspase-3 and β-actin antibodies. ( E ) The graphs show mean values ± SEM of two independent experiments. ( F ) Pancreatic MIA PaCa-2 control and FOXM1 knockdown cancer cells were subjected to ionizing radiation with the indicated doses. Thirty-six hours following irradiation cells were harvested and immunoblotting was carried out with antibodies specific for Bcl-2 and Bcl-xL. β-actin was used as the loading control. ( G ) Breast MDA-MB-231 control and FOXM1 knockdown cancer cells were γ-irradiated as indicated. Seventy-two hours following irradiation cells were harvested and immunoblotting was performed for Bcl-2. β-actin was used as the loading control. ( H ) MIA PaCa-2 control and FOXM1 knockdown pancreatic cancer cells were harvested for RNA extraction. Quantitative RT-PCR was carried out with Bcl-2 and cyclophilin primers. The graph demonstrates mean values ±SEM of three independent experiments. ( I ) To extract RNA MDA-MB-231 control and FOXM1 knockdown breast cancer cells were harvested. Using Bcl-2 and cyclophlin primers qRT-PCR was performed. The graph shows mean values ±SEM of three independent experiments.

    Article Snippet: Treated cells were harvested and processed for immunoblotting as described in ref. with antibodies specific for FOXM1 (the rabbit polyclonal antibody against FOXM1 was described previously ), p53 (Santa Cruz), cleaved caspase-3 (Cell signaling), PARP-1/2 (Santa Cruz), Total and Phospho-SAPK/JNK (Cell signaling), Bcl-2 (Santa Cruz), Bcl-xL (Cell signaling) and β-actin (Sigma).

    Techniques: Irradiation, Western Blot, RNA Extraction, Quantitative RT-PCR

    Methimazole attenuated the increased expression of phosphorylated JNK and ERK proteins (30 minutes). (a) Methimazole prevented the increased expression of p-ERK in scratched astrocytes. (b) Methimazole prevented the increased expression of p-JNK in scratched astrocytes. All values were expressed as mean ± SEM, n = 5. ∗ p < 0.05 vs. control; # p < 0.05 vs. scratch.

    Journal: Mediators of Inflammation

    Article Title: Methimazole Inhibits the Expression of GFAP and the Migration of Astrocyte in Scratched Wound Model In Vitro

    doi: 10.1155/2020/4027470

    Figure Lengend Snippet: Methimazole attenuated the increased expression of phosphorylated JNK and ERK proteins (30 minutes). (a) Methimazole prevented the increased expression of p-ERK in scratched astrocytes. (b) Methimazole prevented the increased expression of p-JNK in scratched astrocytes. All values were expressed as mean ± SEM, n = 5. ∗ p < 0.05 vs. control; # p < 0.05 vs. scratch.

    Article Snippet: Primary antibodies of GFAP (1 : 1000, Santa Cruz), p-ERK (1 : 1000, Cell Signaling), ERK (1 : 1000, Cell Signaling), p-JNK (1 : 1000, Cell Signaling), and JNK (1 : 1000, Cell Signaling) and the corresponding secondary antibodies were used here. β -Actin (Santa Cruz) was used as an internal control.

    Techniques: Expressing