Structured Review

Millipore ampk inhibitors
AMP-activated protein kinase <t>(AMPK)</t> is involved in resistin-induced matrix metalloproteinase (MMP-2) expression and cell migration JJ012 and SW1353 cells were pre-treated with Ara A (0.5 mM) and compound C (10 μM) for 30 min or pre-transfected with control, AMPKα1, or AMPKα2 siRNA for 24 h, and subsequently stimulated with resistin (3 ng/ml) for 24 h. In vitro migration, MMP-2 protein expression (JJ012 cells), and MMP-2 mRNA expression were measured by (A) Transwell assays, (B) enzyme-linked immunosorbent assay (ELISA), and (C) real-time quantitative polymerase chain reaction (RT-qPCR), respectively. Next, the JJ012 and SW1353 cells were pre-treated with SB203580 (10 μM) for 30 min or pre-transfected with control or <t>p38</t> siRNA for 24 h, and subsequently stimulated with resistin (3 ng/ml) for 24 h. In vitro migration, MMP-2 protein expression (JJ012 cells), and MMP-2 mRNA expression were measured by (D) Transwell assays, (E) ELISA, and (F) RT-qPCR, respectively. (G) The JJ012 cells were incubated with resistin for the indicated time intervals, and the p-AMPK and p38 expression were examined by western blot. (H) The JJ012 cells were pre-treated for 30 min with Ara A and compound C, or SB203580 followed by stimulation with resistin. The p-p38 and p-AMPK expression were measured by western blot. The results are expressed as mean ± SEM. *, P
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1) Product Images from "Resistin promotes tumor metastasis by down-regulation of miR-519d through the AMPK/p38 signaling pathway in human chondrosarcoma cells"

Article Title: Resistin promotes tumor metastasis by down-regulation of miR-519d through the AMPK/p38 signaling pathway in human chondrosarcoma cells

Journal: Oncotarget

doi:

AMP-activated protein kinase (AMPK) is involved in resistin-induced matrix metalloproteinase (MMP-2) expression and cell migration JJ012 and SW1353 cells were pre-treated with Ara A (0.5 mM) and compound C (10 μM) for 30 min or pre-transfected with control, AMPKα1, or AMPKα2 siRNA for 24 h, and subsequently stimulated with resistin (3 ng/ml) for 24 h. In vitro migration, MMP-2 protein expression (JJ012 cells), and MMP-2 mRNA expression were measured by (A) Transwell assays, (B) enzyme-linked immunosorbent assay (ELISA), and (C) real-time quantitative polymerase chain reaction (RT-qPCR), respectively. Next, the JJ012 and SW1353 cells were pre-treated with SB203580 (10 μM) for 30 min or pre-transfected with control or p38 siRNA for 24 h, and subsequently stimulated with resistin (3 ng/ml) for 24 h. In vitro migration, MMP-2 protein expression (JJ012 cells), and MMP-2 mRNA expression were measured by (D) Transwell assays, (E) ELISA, and (F) RT-qPCR, respectively. (G) The JJ012 cells were incubated with resistin for the indicated time intervals, and the p-AMPK and p38 expression were examined by western blot. (H) The JJ012 cells were pre-treated for 30 min with Ara A and compound C, or SB203580 followed by stimulation with resistin. The p-p38 and p-AMPK expression were measured by western blot. The results are expressed as mean ± SEM. *, P
Figure Legend Snippet: AMP-activated protein kinase (AMPK) is involved in resistin-induced matrix metalloproteinase (MMP-2) expression and cell migration JJ012 and SW1353 cells were pre-treated with Ara A (0.5 mM) and compound C (10 μM) for 30 min or pre-transfected with control, AMPKα1, or AMPKα2 siRNA for 24 h, and subsequently stimulated with resistin (3 ng/ml) for 24 h. In vitro migration, MMP-2 protein expression (JJ012 cells), and MMP-2 mRNA expression were measured by (A) Transwell assays, (B) enzyme-linked immunosorbent assay (ELISA), and (C) real-time quantitative polymerase chain reaction (RT-qPCR), respectively. Next, the JJ012 and SW1353 cells were pre-treated with SB203580 (10 μM) for 30 min or pre-transfected with control or p38 siRNA for 24 h, and subsequently stimulated with resistin (3 ng/ml) for 24 h. In vitro migration, MMP-2 protein expression (JJ012 cells), and MMP-2 mRNA expression were measured by (D) Transwell assays, (E) ELISA, and (F) RT-qPCR, respectively. (G) The JJ012 cells were incubated with resistin for the indicated time intervals, and the p-AMPK and p38 expression were examined by western blot. (H) The JJ012 cells were pre-treated for 30 min with Ara A and compound C, or SB203580 followed by stimulation with resistin. The p-p38 and p-AMPK expression were measured by western blot. The results are expressed as mean ± SEM. *, P

Techniques Used: Expressing, Migration, Acetylene Reduction Assay, Transfection, In Vitro, Enzyme-linked Immunosorbent Assay, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, Incubation, Western Blot

Resistin promotes cell migration and matrix metalloproteinase (MMP-2) expression by down-regulating microRNA (miR)-519d expression (A) The JJ012 and SW1353 cells were transfected with miR-519d mimic or inhibitor for 24 h, and cell migration ability was examined by Transwell assay. (B) The JJ012 cells were transfected with an miR-519d mimic or inhibitor for 24 h, and MMP-2 expression was examined by western blot (upper panel), and enzyme-linked immunosorbent assay (lower panel). (C) The JJ012 and SW1353 cells were incubated with resistin (0.3–3 ng/ml) for 24 h, and miR-519d expression was detected by real-time quantitative polymerase chain reaction. (D) Sequences of miR-519d and the potential miR-519d binding site at the MMP-2 3′ untranslated region (3′ UTR; WT-MMP-2 3′ UTR). Also shown are the nucleotides mutated in the MMP-2 3′UTR mutant (MUT-MMP2 3′ UTR). (E) The JJ012 and SW1353 cells were transfected with a wild-type or mutant MMP-2 3′ UTR luciferase plasmid for 24 h followed by stimulation with resistin (0.3-3 ng/ml) for 24 h, and the relative luciferase activity was measured. The JJ012 cells were pre-treated with AMPK and p38 inhibitors for 30 min or pre-transfected with specific siRNAs for 24 h followed by stimulation with resistin (3 ng/ml) for 24 h; and the (F, G) miR-519d expression and (H) MMP-2 3′ UTR activity were examined. The results are expressed as mean ± SEM. *, P
Figure Legend Snippet: Resistin promotes cell migration and matrix metalloproteinase (MMP-2) expression by down-regulating microRNA (miR)-519d expression (A) The JJ012 and SW1353 cells were transfected with miR-519d mimic or inhibitor for 24 h, and cell migration ability was examined by Transwell assay. (B) The JJ012 cells were transfected with an miR-519d mimic or inhibitor for 24 h, and MMP-2 expression was examined by western blot (upper panel), and enzyme-linked immunosorbent assay (lower panel). (C) The JJ012 and SW1353 cells were incubated with resistin (0.3–3 ng/ml) for 24 h, and miR-519d expression was detected by real-time quantitative polymerase chain reaction. (D) Sequences of miR-519d and the potential miR-519d binding site at the MMP-2 3′ untranslated region (3′ UTR; WT-MMP-2 3′ UTR). Also shown are the nucleotides mutated in the MMP-2 3′UTR mutant (MUT-MMP2 3′ UTR). (E) The JJ012 and SW1353 cells were transfected with a wild-type or mutant MMP-2 3′ UTR luciferase plasmid for 24 h followed by stimulation with resistin (0.3-3 ng/ml) for 24 h, and the relative luciferase activity was measured. The JJ012 cells were pre-treated with AMPK and p38 inhibitors for 30 min or pre-transfected with specific siRNAs for 24 h followed by stimulation with resistin (3 ng/ml) for 24 h; and the (F, G) miR-519d expression and (H) MMP-2 3′ UTR activity were examined. The results are expressed as mean ± SEM. *, P

Techniques Used: Migration, Expressing, Transfection, Transwell Assay, Western Blot, Enzyme-linked Immunosorbent Assay, Incubation, Real-time Polymerase Chain Reaction, Binding Assay, Mutagenesis, Luciferase, Plasmid Preparation, Activity Assay

2) Product Images from "Enhanced Expression of WD Repeat-Containing Protein 35 via CaMKK/AMPK Activation in Bupivacaine-Treated Neuro2a Cells"

Article Title: Enhanced Expression of WD Repeat-Containing Protein 35 via CaMKK/AMPK Activation in Bupivacaine-Treated Neuro2a Cells

Journal: PLoS ONE

doi: 10.1371/journal.pone.0098185

Effect of iodotubercidin on bupivacaine-induced AMPK and p38 MAPK activity. Neuro2a cells were treated with AMPK inhibitor iodotubercidin (1 µM) for 1 h, followed by bupivacaine (2 mM) for 9 h. (A) Expression of phospho-AMPKα (P-AMPKα), AMPK, phospho-p38 (P-p38) and p38 was measured by Western blotting (n = 3 per group). The bar diagram shows the ratio of phospho-AMPKα to AMPK (B) and the ratio of P-p38 to p38 (C). * P
Figure Legend Snippet: Effect of iodotubercidin on bupivacaine-induced AMPK and p38 MAPK activity. Neuro2a cells were treated with AMPK inhibitor iodotubercidin (1 µM) for 1 h, followed by bupivacaine (2 mM) for 9 h. (A) Expression of phospho-AMPKα (P-AMPKα), AMPK, phospho-p38 (P-p38) and p38 was measured by Western blotting (n = 3 per group). The bar diagram shows the ratio of phospho-AMPKα to AMPK (B) and the ratio of P-p38 to p38 (C). * P

Techniques Used: Activity Assay, Expressing, Western Blot

Effect of compound C on bupivacaine-induced AMPK and p38 MAPK activity. Neuro2a cells were treated with AMPK inhibitor compound C (10 µM) for 1 h, followed by bupivacaine (2 mM) for 9 h. (A) Expression of phospho-AMPKα (P-AMPKα), AMPK, phospho-p38 (P-p38) and p38 was measured by Western blotting (n = 3 per group). The bar diagram shows the ratio of phospho-AMPKα to AMPK (B) and the ratio of P-p38 to p38 (C). * P
Figure Legend Snippet: Effect of compound C on bupivacaine-induced AMPK and p38 MAPK activity. Neuro2a cells were treated with AMPK inhibitor compound C (10 µM) for 1 h, followed by bupivacaine (2 mM) for 9 h. (A) Expression of phospho-AMPKα (P-AMPKα), AMPK, phospho-p38 (P-p38) and p38 was measured by Western blotting (n = 3 per group). The bar diagram shows the ratio of phospho-AMPKα to AMPK (B) and the ratio of P-p38 to p38 (C). * P

Techniques Used: Activity Assay, Expressing, Western Blot

Effect of bupivacaine on intracellular ATP levels and AMPK activation. Neuro2a cells were treated with 2(A) Intracellular levels of ATP were measured with a luminescence assay (n = 4 per group). (B) Expression of phospho-AMPKα (P-AMPKα) and AMPK following cell exposure to bupivacaine was measured by Western blotting (n = 3 per group). *** P
Figure Legend Snippet: Effect of bupivacaine on intracellular ATP levels and AMPK activation. Neuro2a cells were treated with 2(A) Intracellular levels of ATP were measured with a luminescence assay (n = 4 per group). (B) Expression of phospho-AMPKα (P-AMPKα) and AMPK following cell exposure to bupivacaine was measured by Western blotting (n = 3 per group). *** P

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

Effect of STO-609 on bupivacaine-induced AMPK and p38 MAPK activity. Neuro2a cells were treated with CaMKK inhibitor STO-609 (50 µM) for 1 h, followed by bupivacaine (2 mM) for 9 h. (A) Expression of phospho-AMPKα (P-AMPKα), AMPK, phospho-p38 (P-p38) and p38 was measured by Western blotting (n = 3 per group). The bar diagram shows the ratio of phospho-AMPKα to AMPK (B) and the ratio of P-p38 to p38 (C). ** P
Figure Legend Snippet: Effect of STO-609 on bupivacaine-induced AMPK and p38 MAPK activity. Neuro2a cells were treated with CaMKK inhibitor STO-609 (50 µM) for 1 h, followed by bupivacaine (2 mM) for 9 h. (A) Expression of phospho-AMPKα (P-AMPKα), AMPK, phospho-p38 (P-p38) and p38 was measured by Western blotting (n = 3 per group). The bar diagram shows the ratio of phospho-AMPKα to AMPK (B) and the ratio of P-p38 to p38 (C). ** P

Techniques Used: Activity Assay, Expressing, Western Blot

3) Product Images from "AMP-activated protein kinase activation mediates CCL3-induced cell migration and matrix metalloproteinase-2 expression in human chondrosarcoma"

Article Title: AMP-activated protein kinase activation mediates CCL3-induced cell migration and matrix metalloproteinase-2 expression in human chondrosarcoma

Journal: Cell Communication and Signaling : CCS

doi: 10.1186/1478-811X-11-68

AMPK-dependent p38 pathway is involved CCL3-induced migration and MMP-2 expression. (A-E): Cells were pretreated for 30 min with SB203580 (10 μM) or transfected with p38 mutant for 24 h. Subsequently, they were stimulated with CCL3 (30 ng/ml) for 24 h, and in vitro migration (A B) , invasion (C) , and MMP-2 (D E) expression were measured with the Transwell assay, wound healing assay, qPCR, and western blotting. (F): JJ012 cells were incubated with CCL3 for indicated time intervals, and p-AMPK expression was examined by western blotting. (G H): Cells were pretreated for 30 min with Ara A, compound C, or SB203580 followed by stimulation with CCL3. The p-p38 (G) and p-AMPK (H) expression was measured by western blotting. Results are expressed as the mean ± SE. * P
Figure Legend Snippet: AMPK-dependent p38 pathway is involved CCL3-induced migration and MMP-2 expression. (A-E): Cells were pretreated for 30 min with SB203580 (10 μM) or transfected with p38 mutant for 24 h. Subsequently, they were stimulated with CCL3 (30 ng/ml) for 24 h, and in vitro migration (A B) , invasion (C) , and MMP-2 (D E) expression were measured with the Transwell assay, wound healing assay, qPCR, and western blotting. (F): JJ012 cells were incubated with CCL3 for indicated time intervals, and p-AMPK expression was examined by western blotting. (G H): Cells were pretreated for 30 min with Ara A, compound C, or SB203580 followed by stimulation with CCL3. The p-p38 (G) and p-AMPK (H) expression was measured by western blotting. Results are expressed as the mean ± SE. * P

Techniques Used: Migration, Expressing, Transfection, Mutagenesis, In Vitro, Transwell Assay, Wound Healing Assay, Real-time Polymerase Chain Reaction, Western Blot, Incubation, Acetylene Reduction Assay

The CCR5/AMPK/p38 pathway is involved in CCL3-mediated NF-κB activation. (A): JJ012 cells were pre-treated with CCR5 mAb, Ara A, SB203580, or PDTC followed by stimulation with CCL3 for 120 min and analyses using the chromatin immunoprecipitation assay. Chromatin was immunoprecipitated with anti-p65 antibody. One percentage of the precipitated chromatin was assayed to verify equal loading (input). (B): JJ012 cells were pretreated with Met-RANTES, Ara A, compound C, or SB203580 followed by stimulation with CCL3 for 120 min, and p65 immunofluorescence staining was performed. * P
Figure Legend Snippet: The CCR5/AMPK/p38 pathway is involved in CCL3-mediated NF-κB activation. (A): JJ012 cells were pre-treated with CCR5 mAb, Ara A, SB203580, or PDTC followed by stimulation with CCL3 for 120 min and analyses using the chromatin immunoprecipitation assay. Chromatin was immunoprecipitated with anti-p65 antibody. One percentage of the precipitated chromatin was assayed to verify equal loading (input). (B): JJ012 cells were pretreated with Met-RANTES, Ara A, compound C, or SB203580 followed by stimulation with CCL3 for 120 min, and p65 immunofluorescence staining was performed. * P

Techniques Used: Activation Assay, Acetylene Reduction Assay, Chromatin Immunoprecipitation, Immunoprecipitation, Immunofluorescence, Staining

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Article Snippet: AMPK Inhibitor and Agonist Treatment β TC6 cells were pretreated with 10 μ mol/L AMPK inhibitor (compound C; Sigma-Aldrich, USA) [ ] for 4 h before being exposed to 0.5 mmol/L PA+DMEM (25 mmol/L glucose)+100 μ mol/L MF for 72 h. Cells exposed to compound C or complete medium alone were used as controls. β TC6 cells were pretreated with 0.5 mmol/L PA+DMEM (25 mmol/L glucose) for 24 h. Consequently, cells were treated with 1 mmol/L of AMPK agonist AICAR (dissolved in 0.1% DMSO (v /v ); Henan DaKen Chemical CO., LTD.) [ ] for additional 72 h. PA-induced cells+DMEM (25 mmol/L glucose) without AICAR and uninduced cells exposed to AICAR served as controls.

Article Title: Quercetin-induced apoptosis ameliorates vascular smooth muscle cell senescence through AMP-activated protein kinase signaling pathway
Article Snippet: Compound C, an AMPK inhibitor, was provided by Calbiochem (La Jolla, CA, USA).

Activation Assay:

Article Title: Anabolic SIRT4 Exerts Retrograde Control over TORC1 Signaling by Glutamine Sparing in the Mitochondria
Article Snippet: .. For AMPK activation, 0.5 mM AICAR (Sigma, catalog no. A9978) was used as a high dose, and 0.03 mM was used as a low dose for 1 h. For AMPK inhibition, compound C (dorsomorphin; Sigma, catalog no. A5499) was used at a 20 μM dose for 1 h. For increasing anaplerotic flux, 10 mM dimethyl α-ketoglutarate (DMKG; Sigma, catalog no. 349631) was added to cells for 1 h. For Arf1 inhibition, 10 μM brefeldin A was added in low-glucose conditions for 1 h. For inhibition of autophagy flux, the cells were kept in either low (5 mM)- or high (25 mM)-glucose medium with or without 100 μM leupeptin (Sigma, catalog no. L2884) for 12 h. For the qPCR and luciferase assays, the cells were kept in the indicated medium conditions for 6 h. ..

Inhibition:

Article Title: Anabolic SIRT4 Exerts Retrograde Control over TORC1 Signaling by Glutamine Sparing in the Mitochondria
Article Snippet: .. For AMPK activation, 0.5 mM AICAR (Sigma, catalog no. A9978) was used as a high dose, and 0.03 mM was used as a low dose for 1 h. For AMPK inhibition, compound C (dorsomorphin; Sigma, catalog no. A5499) was used at a 20 μM dose for 1 h. For increasing anaplerotic flux, 10 mM dimethyl α-ketoglutarate (DMKG; Sigma, catalog no. 349631) was added to cells for 1 h. For Arf1 inhibition, 10 μM brefeldin A was added in low-glucose conditions for 1 h. For inhibition of autophagy flux, the cells were kept in either low (5 mM)- or high (25 mM)-glucose medium with or without 100 μM leupeptin (Sigma, catalog no. L2884) for 12 h. For the qPCR and luciferase assays, the cells were kept in the indicated medium conditions for 6 h. ..

Real-time Polymerase Chain Reaction:

Article Title: Anabolic SIRT4 Exerts Retrograde Control over TORC1 Signaling by Glutamine Sparing in the Mitochondria
Article Snippet: .. For AMPK activation, 0.5 mM AICAR (Sigma, catalog no. A9978) was used as a high dose, and 0.03 mM was used as a low dose for 1 h. For AMPK inhibition, compound C (dorsomorphin; Sigma, catalog no. A5499) was used at a 20 μM dose for 1 h. For increasing anaplerotic flux, 10 mM dimethyl α-ketoglutarate (DMKG; Sigma, catalog no. 349631) was added to cells for 1 h. For Arf1 inhibition, 10 μM brefeldin A was added in low-glucose conditions for 1 h. For inhibition of autophagy flux, the cells were kept in either low (5 mM)- or high (25 mM)-glucose medium with or without 100 μM leupeptin (Sigma, catalog no. L2884) for 12 h. For the qPCR and luciferase assays, the cells were kept in the indicated medium conditions for 6 h. ..

Luciferase:

Article Title: Anabolic SIRT4 Exerts Retrograde Control over TORC1 Signaling by Glutamine Sparing in the Mitochondria
Article Snippet: .. For AMPK activation, 0.5 mM AICAR (Sigma, catalog no. A9978) was used as a high dose, and 0.03 mM was used as a low dose for 1 h. For AMPK inhibition, compound C (dorsomorphin; Sigma, catalog no. A5499) was used at a 20 μM dose for 1 h. For increasing anaplerotic flux, 10 mM dimethyl α-ketoglutarate (DMKG; Sigma, catalog no. 349631) was added to cells for 1 h. For Arf1 inhibition, 10 μM brefeldin A was added in low-glucose conditions for 1 h. For inhibition of autophagy flux, the cells were kept in either low (5 mM)- or high (25 mM)-glucose medium with or without 100 μM leupeptin (Sigma, catalog no. L2884) for 12 h. For the qPCR and luciferase assays, the cells were kept in the indicated medium conditions for 6 h. ..

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    Millipore compound c
    Ginsenoside Mc1 inhibited hydrogen peroxide (H 2 O 2 )–mediated reactive oxygen species (ROS) production by increasing the expression of antioxidant proteins in H9c2 cells. (A) Cells were stimulated with various doses (0, 10, 25, or 50 μg/mL) of ginsenoside Mc1 for 30 min. (B) H9c2 cells were incubated with ginsenoside Mc1 (50 μg/mL) for the indicated times (0, 15, 30, or 60 min). The extent of AMPK phosphorylation was determined by Western blotting. (C) Cells were incubated with several doses (0, 25, or 50 μg/mL) of ginsenoside Mc1 for 24 h. (D) H9c2 cells were stimulated with ginsenoside Mc1 (50 μg/mL) or ginsenoside Mc1 plus <t>compound</t> C (2 or 5 μM) for 24 h. Catalase and SOD2 levels were determined by Western blotting. (E) Cells were pretreated with ginsenoside Mc1 (25 or 50 μg/mL) for 24 h and then stimulated with H 2 O 2 (600 μM) for 2 h. (F) H9c2 cells were preincubated with ginsenoside Mc1 (50 μg/mL) or ginsenoside Mc1 plus compound C (2 or 5 μM) for 24 h and then stimulated with H 2 O 2 (600 μM) for 2 h. The stimulated cells were stained with dihydroethidium (DHE) solution to assess the prevalence of intracellular ROS. The mean ± standard deviation was obtained from 3 separate experiments [*, p
    Compound C, supplied by Millipore, 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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    Millipore dorsomorphin
    Effects of <t>dorsomorphin</t> on Salmonella -induced changes in hepcidin expression and serum iron levels.
    Dorsomorphin, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore ampk inhibitors
    AMP-activated protein kinase <t>(AMPK)</t> is involved in resistin-induced matrix metalloproteinase (MMP-2) expression and cell migration JJ012 and SW1353 cells were pre-treated with Ara A (0.5 mM) and compound C (10 μM) for 30 min or pre-transfected with control, AMPKα1, or AMPKα2 siRNA for 24 h, and subsequently stimulated with resistin (3 ng/ml) for 24 h. In vitro migration, MMP-2 protein expression (JJ012 cells), and MMP-2 mRNA expression were measured by (A) Transwell assays, (B) enzyme-linked immunosorbent assay (ELISA), and (C) real-time quantitative polymerase chain reaction (RT-qPCR), respectively. Next, the JJ012 and SW1353 cells were pre-treated with SB203580 (10 μM) for 30 min or pre-transfected with control or <t>p38</t> siRNA for 24 h, and subsequently stimulated with resistin (3 ng/ml) for 24 h. In vitro migration, MMP-2 protein expression (JJ012 cells), and MMP-2 mRNA expression were measured by (D) Transwell assays, (E) ELISA, and (F) RT-qPCR, respectively. (G) The JJ012 cells were incubated with resistin for the indicated time intervals, and the p-AMPK and p38 expression were examined by western blot. (H) The JJ012 cells were pre-treated for 30 min with Ara A and compound C, or SB203580 followed by stimulation with resistin. The p-p38 and p-AMPK expression were measured by western blot. The results are expressed as mean ± SEM. *, P
    Ampk Inhibitors, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ampk inhibitors/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ampk inhibitors - by Bioz Stars, 2021-09
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    Ginsenoside Mc1 inhibited hydrogen peroxide (H 2 O 2 )–mediated reactive oxygen species (ROS) production by increasing the expression of antioxidant proteins in H9c2 cells. (A) Cells were stimulated with various doses (0, 10, 25, or 50 μg/mL) of ginsenoside Mc1 for 30 min. (B) H9c2 cells were incubated with ginsenoside Mc1 (50 μg/mL) for the indicated times (0, 15, 30, or 60 min). The extent of AMPK phosphorylation was determined by Western blotting. (C) Cells were incubated with several doses (0, 25, or 50 μg/mL) of ginsenoside Mc1 for 24 h. (D) H9c2 cells were stimulated with ginsenoside Mc1 (50 μg/mL) or ginsenoside Mc1 plus compound C (2 or 5 μM) for 24 h. Catalase and SOD2 levels were determined by Western blotting. (E) Cells were pretreated with ginsenoside Mc1 (25 or 50 μg/mL) for 24 h and then stimulated with H 2 O 2 (600 μM) for 2 h. (F) H9c2 cells were preincubated with ginsenoside Mc1 (50 μg/mL) or ginsenoside Mc1 plus compound C (2 or 5 μM) for 24 h and then stimulated with H 2 O 2 (600 μM) for 2 h. The stimulated cells were stained with dihydroethidium (DHE) solution to assess the prevalence of intracellular ROS. The mean ± standard deviation was obtained from 3 separate experiments [*, p

    Journal: Journal of Ginseng Research

    Article Title: Ginsenoside compound-Mc1 attenuates oxidative stress and apoptosis in cardiomyocytes through an AMP-activated protein kinase–dependent mechanism

    doi: 10.1016/j.jgr.2019.08.006

    Figure Lengend Snippet: Ginsenoside Mc1 inhibited hydrogen peroxide (H 2 O 2 )–mediated reactive oxygen species (ROS) production by increasing the expression of antioxidant proteins in H9c2 cells. (A) Cells were stimulated with various doses (0, 10, 25, or 50 μg/mL) of ginsenoside Mc1 for 30 min. (B) H9c2 cells were incubated with ginsenoside Mc1 (50 μg/mL) for the indicated times (0, 15, 30, or 60 min). The extent of AMPK phosphorylation was determined by Western blotting. (C) Cells were incubated with several doses (0, 25, or 50 μg/mL) of ginsenoside Mc1 for 24 h. (D) H9c2 cells were stimulated with ginsenoside Mc1 (50 μg/mL) or ginsenoside Mc1 plus compound C (2 or 5 μM) for 24 h. Catalase and SOD2 levels were determined by Western blotting. (E) Cells were pretreated with ginsenoside Mc1 (25 or 50 μg/mL) for 24 h and then stimulated with H 2 O 2 (600 μM) for 2 h. (F) H9c2 cells were preincubated with ginsenoside Mc1 (50 μg/mL) or ginsenoside Mc1 plus compound C (2 or 5 μM) for 24 h and then stimulated with H 2 O 2 (600 μM) for 2 h. The stimulated cells were stained with dihydroethidium (DHE) solution to assess the prevalence of intracellular ROS. The mean ± standard deviation was obtained from 3 separate experiments [*, p

    Article Snippet: Ginsenoside Mc1, compound C (AMPK inhibitor; Sigma-Aldrich), and N-acetylcysteine (NAC; Cayman Chemical, MI, USA) were dissolved in dimethyl sulfoxide (Sigma-Aldrich).

    Techniques: Expressing, Incubation, Western Blot, Staining, Standard Deviation

    Ginsenoside Mc1 exhibited a protective effect after the treatment of H9c2 cells with hydrogen peroxide (H 2 O 2 ). (A and B) Cells were preincubated with ginsenoside Mc1 (25 or 50 μg/mL) or ginsenoside Mc1 plus compound C (2 μM) for 24 h and then stimulated with H 2 O 2 (600 μM) for 2 h. Bax and Bcl2 levels were determined by Western blotting. (C and D) H9c2 cells were pretreated with ginsenoside Mc1 or ginsenoside Mc1 plus compound C for 24 h and then stimulated with H 2 O 2 for 4 h. Cell viability was measured using an EZ-CYTOX kit. The mean ± standard deviation was obtained from 3 separate experiments [*, p

    Journal: Journal of Ginseng Research

    Article Title: Ginsenoside compound-Mc1 attenuates oxidative stress and apoptosis in cardiomyocytes through an AMP-activated protein kinase–dependent mechanism

    doi: 10.1016/j.jgr.2019.08.006

    Figure Lengend Snippet: Ginsenoside Mc1 exhibited a protective effect after the treatment of H9c2 cells with hydrogen peroxide (H 2 O 2 ). (A and B) Cells were preincubated with ginsenoside Mc1 (25 or 50 μg/mL) or ginsenoside Mc1 plus compound C (2 μM) for 24 h and then stimulated with H 2 O 2 (600 μM) for 2 h. Bax and Bcl2 levels were determined by Western blotting. (C and D) H9c2 cells were pretreated with ginsenoside Mc1 or ginsenoside Mc1 plus compound C for 24 h and then stimulated with H 2 O 2 for 4 h. Cell viability was measured using an EZ-CYTOX kit. The mean ± standard deviation was obtained from 3 separate experiments [*, p

    Article Snippet: Ginsenoside Mc1, compound C (AMPK inhibitor; Sigma-Aldrich), and N-acetylcysteine (NAC; Cayman Chemical, MI, USA) were dissolved in dimethyl sulfoxide (Sigma-Aldrich).

    Techniques: Western Blot, Standard Deviation

    Ginsenoside Mc1 inhibited hydrogen peroxide (H 2 O 2 )– induced apoptotic events in H9c2 cells. (A) Cells were preincubated with ginsenoside Mc1 (50 μg/mL) or ginsenoside Mc1 plus compound C (2 μM) for 24 h and then stimulated with H 2 O 2 (600 μM) for 2 h. The shape of the nucleus was determined by Hoechst staining. White arrows indicate DNA-damaged cells. (B) H9c2 cells were pretreated with ginsenoside Mc1 or ginsenoside Mc1 plus compound C for 24 h and then stimulated with H 2 O 2 for 4 h. The rate of apoptosis was determined using annexin V/propidium iodide (PI) double staining and flow cytometry. The mean ± standard deviation was obtained from 3 separate experiments [***, p

    Journal: Journal of Ginseng Research

    Article Title: Ginsenoside compound-Mc1 attenuates oxidative stress and apoptosis in cardiomyocytes through an AMP-activated protein kinase–dependent mechanism

    doi: 10.1016/j.jgr.2019.08.006

    Figure Lengend Snippet: Ginsenoside Mc1 inhibited hydrogen peroxide (H 2 O 2 )– induced apoptotic events in H9c2 cells. (A) Cells were preincubated with ginsenoside Mc1 (50 μg/mL) or ginsenoside Mc1 plus compound C (2 μM) for 24 h and then stimulated with H 2 O 2 (600 μM) for 2 h. The shape of the nucleus was determined by Hoechst staining. White arrows indicate DNA-damaged cells. (B) H9c2 cells were pretreated with ginsenoside Mc1 or ginsenoside Mc1 plus compound C for 24 h and then stimulated with H 2 O 2 for 4 h. The rate of apoptosis was determined using annexin V/propidium iodide (PI) double staining and flow cytometry. The mean ± standard deviation was obtained from 3 separate experiments [***, p

    Article Snippet: Ginsenoside Mc1, compound C (AMPK inhibitor; Sigma-Aldrich), and N-acetylcysteine (NAC; Cayman Chemical, MI, USA) were dissolved in dimethyl sulfoxide (Sigma-Aldrich).

    Techniques: Staining, Double Staining, Flow Cytometry, Standard Deviation

    Effects of dorsomorphin on Salmonella -induced changes in hepcidin expression and serum iron levels.

    Journal: The Journal of Clinical Investigation

    Article Title: Selective modulation of TLR4-activated inflammatory responses by altered iron homeostasis in mice

    doi: 10.1172/JCI39939

    Figure Lengend Snippet: Effects of dorsomorphin on Salmonella -induced changes in hepcidin expression and serum iron levels.

    Article Snippet: Treatment with dorsomorphin (12.5 μg/g BW i.p.; Calbiochem) or an equivalent volume of the vehicle DMSO was started at the same time as the streptomycin was administered and was continued twice daily for the duration of the experiment.

    Techniques: Expressing

    Effects of dorsomorphin treatment on Salmonella -induced intestinal inflammation in WT mice.

    Journal: The Journal of Clinical Investigation

    Article Title: Selective modulation of TLR4-activated inflammatory responses by altered iron homeostasis in mice

    doi: 10.1172/JCI39939

    Figure Lengend Snippet: Effects of dorsomorphin treatment on Salmonella -induced intestinal inflammation in WT mice.

    Article Snippet: Treatment with dorsomorphin (12.5 μg/g BW i.p.; Calbiochem) or an equivalent volume of the vehicle DMSO was started at the same time as the streptomycin was administered and was continued twice daily for the duration of the experiment.

    Techniques: Mouse Assay

    Structure of the ALK2-FKBP12 complex. A , secondary structure elements are labeled and shown as ribbons . Disordered parts of the L45 loop and A loop are indicated by a thin dashed line . Dorsomorphin is shown in gray stick representation, and Mg 2+ ion ( cyan ) and sulfate molecules ( purple ) are displayed as spheres. Inset box shows the specific interactions of dorsomorphin ( yellow sticks ) with the ATP pocket in ALK2. Hydrogen bonds ( blue dashed lines ) are formed with the hinge amide of His-286 and via a water molecule to Glu-248 (α C ). The planarity of the phenyl ring is restricted by the close packing of Val-214 and Gly-289 ( dashed gray lines). B , FKBP12 binding is dominated by insertion of the αGS2 helix into the central FK506-binding pocket of FKBP12. Here, the ALK5 residues Leu-195–Leu-196 are replaced by ALK2 Phe-198–Leu-199 resulting in a subtle shift in the complex interface. The hydrophobic contact surface in FKBP12 is colored yellow. C , | F o | − | F c | omit map contoured at 3σ ( green mesh ) for the bound dorsomorphin ligand ( yellow sticks ).

    Journal: The Journal of Biological Chemistry

    Article Title: Structure of the Bone Morphogenetic Protein Receptor ALK2 and Implications for Fibrodysplasia Ossificans Progressiva *

    doi: 10.1074/jbc.M112.365932

    Figure Lengend Snippet: Structure of the ALK2-FKBP12 complex. A , secondary structure elements are labeled and shown as ribbons . Disordered parts of the L45 loop and A loop are indicated by a thin dashed line . Dorsomorphin is shown in gray stick representation, and Mg 2+ ion ( cyan ) and sulfate molecules ( purple ) are displayed as spheres. Inset box shows the specific interactions of dorsomorphin ( yellow sticks ) with the ATP pocket in ALK2. Hydrogen bonds ( blue dashed lines ) are formed with the hinge amide of His-286 and via a water molecule to Glu-248 (α C ). The planarity of the phenyl ring is restricted by the close packing of Val-214 and Gly-289 ( dashed gray lines). B , FKBP12 binding is dominated by insertion of the αGS2 helix into the central FK506-binding pocket of FKBP12. Here, the ALK5 residues Leu-195–Leu-196 are replaced by ALK2 Phe-198–Leu-199 resulting in a subtle shift in the complex interface. The hydrophobic contact surface in FKBP12 is colored yellow. C , | F o | − | F c | omit map contoured at 3σ ( green mesh ) for the bound dorsomorphin ligand ( yellow sticks ).

    Article Snippet: The ALK2-FKBP12 complex was preincubated with 1 mm dorsomorphin (Calbiochem) at a protein concentration of 10 mg/ml and crystallized using a precipitant containing 30% PEG3350, 0.25 m ammonium sulfate, and 0.1 m BisTris, pH 6.0.

    Techniques: Labeling, Binding Assay

    AMP-activated protein kinase (AMPK) is involved in resistin-induced matrix metalloproteinase (MMP-2) expression and cell migration JJ012 and SW1353 cells were pre-treated with Ara A (0.5 mM) and compound C (10 μM) for 30 min or pre-transfected with control, AMPKα1, or AMPKα2 siRNA for 24 h, and subsequently stimulated with resistin (3 ng/ml) for 24 h. In vitro migration, MMP-2 protein expression (JJ012 cells), and MMP-2 mRNA expression were measured by (A) Transwell assays, (B) enzyme-linked immunosorbent assay (ELISA), and (C) real-time quantitative polymerase chain reaction (RT-qPCR), respectively. Next, the JJ012 and SW1353 cells were pre-treated with SB203580 (10 μM) for 30 min or pre-transfected with control or p38 siRNA for 24 h, and subsequently stimulated with resistin (3 ng/ml) for 24 h. In vitro migration, MMP-2 protein expression (JJ012 cells), and MMP-2 mRNA expression were measured by (D) Transwell assays, (E) ELISA, and (F) RT-qPCR, respectively. (G) The JJ012 cells were incubated with resistin for the indicated time intervals, and the p-AMPK and p38 expression were examined by western blot. (H) The JJ012 cells were pre-treated for 30 min with Ara A and compound C, or SB203580 followed by stimulation with resistin. The p-p38 and p-AMPK expression were measured by western blot. The results are expressed as mean ± SEM. *, P

    Journal: Oncotarget

    Article Title: Resistin promotes tumor metastasis by down-regulation of miR-519d through the AMPK/p38 signaling pathway in human chondrosarcoma cells

    doi:

    Figure Lengend Snippet: AMP-activated protein kinase (AMPK) is involved in resistin-induced matrix metalloproteinase (MMP-2) expression and cell migration JJ012 and SW1353 cells were pre-treated with Ara A (0.5 mM) and compound C (10 μM) for 30 min or pre-transfected with control, AMPKα1, or AMPKα2 siRNA for 24 h, and subsequently stimulated with resistin (3 ng/ml) for 24 h. In vitro migration, MMP-2 protein expression (JJ012 cells), and MMP-2 mRNA expression were measured by (A) Transwell assays, (B) enzyme-linked immunosorbent assay (ELISA), and (C) real-time quantitative polymerase chain reaction (RT-qPCR), respectively. Next, the JJ012 and SW1353 cells were pre-treated with SB203580 (10 μM) for 30 min or pre-transfected with control or p38 siRNA for 24 h, and subsequently stimulated with resistin (3 ng/ml) for 24 h. In vitro migration, MMP-2 protein expression (JJ012 cells), and MMP-2 mRNA expression were measured by (D) Transwell assays, (E) ELISA, and (F) RT-qPCR, respectively. (G) The JJ012 cells were incubated with resistin for the indicated time intervals, and the p-AMPK and p38 expression were examined by western blot. (H) The JJ012 cells were pre-treated for 30 min with Ara A and compound C, or SB203580 followed by stimulation with resistin. The p-p38 and p-AMPK expression were measured by western blot. The results are expressed as mean ± SEM. *, P

    Article Snippet: AMPK inhibitors (Ara A and compound C), p38 inhibitor (SB203580), MMP-2 inhibitor, and human MMP-2 ELISA kits were purchased from Calbiochem (San Diego, CA).

    Techniques: Expressing, Migration, Acetylene Reduction Assay, Transfection, In Vitro, Enzyme-linked Immunosorbent Assay, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, Incubation, Western Blot

    Resistin promotes cell migration and matrix metalloproteinase (MMP-2) expression by down-regulating microRNA (miR)-519d expression (A) The JJ012 and SW1353 cells were transfected with miR-519d mimic or inhibitor for 24 h, and cell migration ability was examined by Transwell assay. (B) The JJ012 cells were transfected with an miR-519d mimic or inhibitor for 24 h, and MMP-2 expression was examined by western blot (upper panel), and enzyme-linked immunosorbent assay (lower panel). (C) The JJ012 and SW1353 cells were incubated with resistin (0.3–3 ng/ml) for 24 h, and miR-519d expression was detected by real-time quantitative polymerase chain reaction. (D) Sequences of miR-519d and the potential miR-519d binding site at the MMP-2 3′ untranslated region (3′ UTR; WT-MMP-2 3′ UTR). Also shown are the nucleotides mutated in the MMP-2 3′UTR mutant (MUT-MMP2 3′ UTR). (E) The JJ012 and SW1353 cells were transfected with a wild-type or mutant MMP-2 3′ UTR luciferase plasmid for 24 h followed by stimulation with resistin (0.3-3 ng/ml) for 24 h, and the relative luciferase activity was measured. The JJ012 cells were pre-treated with AMPK and p38 inhibitors for 30 min or pre-transfected with specific siRNAs for 24 h followed by stimulation with resistin (3 ng/ml) for 24 h; and the (F, G) miR-519d expression and (H) MMP-2 3′ UTR activity were examined. The results are expressed as mean ± SEM. *, P

    Journal: Oncotarget

    Article Title: Resistin promotes tumor metastasis by down-regulation of miR-519d through the AMPK/p38 signaling pathway in human chondrosarcoma cells

    doi:

    Figure Lengend Snippet: Resistin promotes cell migration and matrix metalloproteinase (MMP-2) expression by down-regulating microRNA (miR)-519d expression (A) The JJ012 and SW1353 cells were transfected with miR-519d mimic or inhibitor for 24 h, and cell migration ability was examined by Transwell assay. (B) The JJ012 cells were transfected with an miR-519d mimic or inhibitor for 24 h, and MMP-2 expression was examined by western blot (upper panel), and enzyme-linked immunosorbent assay (lower panel). (C) The JJ012 and SW1353 cells were incubated with resistin (0.3–3 ng/ml) for 24 h, and miR-519d expression was detected by real-time quantitative polymerase chain reaction. (D) Sequences of miR-519d and the potential miR-519d binding site at the MMP-2 3′ untranslated region (3′ UTR; WT-MMP-2 3′ UTR). Also shown are the nucleotides mutated in the MMP-2 3′UTR mutant (MUT-MMP2 3′ UTR). (E) The JJ012 and SW1353 cells were transfected with a wild-type or mutant MMP-2 3′ UTR luciferase plasmid for 24 h followed by stimulation with resistin (0.3-3 ng/ml) for 24 h, and the relative luciferase activity was measured. The JJ012 cells were pre-treated with AMPK and p38 inhibitors for 30 min or pre-transfected with specific siRNAs for 24 h followed by stimulation with resistin (3 ng/ml) for 24 h; and the (F, G) miR-519d expression and (H) MMP-2 3′ UTR activity were examined. The results are expressed as mean ± SEM. *, P

    Article Snippet: AMPK inhibitors (Ara A and compound C), p38 inhibitor (SB203580), MMP-2 inhibitor, and human MMP-2 ELISA kits were purchased from Calbiochem (San Diego, CA).

    Techniques: Migration, Expressing, Transfection, Transwell Assay, Western Blot, Enzyme-linked Immunosorbent Assay, Incubation, Real-time Polymerase Chain Reaction, Binding Assay, Mutagenesis, Luciferase, Plasmid Preparation, Activity Assay