ampk2 protein Search Results


93
MedChemExpress gpx4
Figure 6. Western blotting analysis on the effects of irisin on the expression level of ferroptosis-associated proteins. (a) Representative western blotting images for the expression of ACSL4, COX-2, <t>GPX4,</t> p-AMPK, and t-AMPK in lung tissues. GAPDH was selected as the loading control protein. (b) Quantification analysis of the related bands of ACSL4, COX-2, GPX4, p-AMPK, and t-AMPK in lung tissues. Lung tissues were harvested on day 3 post-CLP. Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-hoc test. n ¼ 6 per group. Data are presented as means SEM. *p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001.
Gpx4, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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MedChemExpress phospho ampk hy p80791 medchemexpress
Figure 6. Western blotting analysis on the effects of irisin on the expression level of ferroptosis-associated proteins. (a) Representative western blotting images for the expression of ACSL4, COX-2, <t>GPX4,</t> p-AMPK, and t-AMPK in lung tissues. GAPDH was selected as the loading control protein. (b) Quantification analysis of the related bands of ACSL4, COX-2, GPX4, p-AMPK, and t-AMPK in lung tissues. Lung tissues were harvested on day 3 post-CLP. Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-hoc test. n ¼ 6 per group. Data are presented as means SEM. *p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001.
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MedChemExpress rabbit anti ampk
Figure 6. Western blotting analysis on the effects of irisin on the expression level of ferroptosis-associated proteins. (a) Representative western blotting images for the expression of ACSL4, COX-2, <t>GPX4,</t> p-AMPK, and t-AMPK in lung tissues. GAPDH was selected as the loading control protein. (b) Quantification analysis of the related bands of ACSL4, COX-2, GPX4, p-AMPK, and t-AMPK in lung tissues. Lung tissues were harvested on day 3 post-CLP. Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-hoc test. n ¼ 6 per group. Data are presented as means SEM. *p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001.
Rabbit Anti Ampk, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Boster Bio ampk phosphorylated monoclonal antibody p ampk
Figure 4. The cellular <t>AMPK</t> expression and phosphorylation level. AMPK protein expressions and phosphorylation in HeLa and KO HeLa cells with or without viral infection were detected with Western blotting. (A) The expression and phosphorylation of AMPK protein on KO HeLa cells compared with HeLa cells. (B) The expression and phosphorylation of AMPK protein on HeLa cells after viral infection. (C) The expression and phosphorylation of AMPK protein on KO HeLa cells after viral infection.
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Boster Bio anti prkaa2
Figure 4. The cellular <t>AMPK</t> expression and phosphorylation level. AMPK protein expressions and phosphorylation in HeLa and KO HeLa cells with or without viral infection were detected with Western blotting. (A) The expression and phosphorylation of AMPK protein on KO HeLa cells compared with HeLa cells. (B) The expression and phosphorylation of AMPK protein on HeLa cells after viral infection. (C) The expression and phosphorylation of AMPK protein on KO HeLa cells after viral infection.
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Boster Bio anti rabbit ampk
Figure 4. The cellular <t>AMPK</t> expression and phosphorylation level. AMPK protein expressions and phosphorylation in HeLa and KO HeLa cells with or without viral infection were detected with Western blotting. (A) The expression and phosphorylation of AMPK protein on KO HeLa cells compared with HeLa cells. (B) The expression and phosphorylation of AMPK protein on HeLa cells after viral infection. (C) The expression and phosphorylation of AMPK protein on KO HeLa cells after viral infection.
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Image Search Results


Figure 6. Western blotting analysis on the effects of irisin on the expression level of ferroptosis-associated proteins. (a) Representative western blotting images for the expression of ACSL4, COX-2, GPX4, p-AMPK, and t-AMPK in lung tissues. GAPDH was selected as the loading control protein. (b) Quantification analysis of the related bands of ACSL4, COX-2, GPX4, p-AMPK, and t-AMPK in lung tissues. Lung tissues were harvested on day 3 post-CLP. Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-hoc test. n ¼ 6 per group. Data are presented as means SEM. *p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001.

Journal: The Journal of international medical research

Article Title: The therapeutic potential of irisin in alleviating acute lung injury via inflammation and ferroptosis modulation.

doi: 10.1177/03000605251340338

Figure Lengend Snippet: Figure 6. Western blotting analysis on the effects of irisin on the expression level of ferroptosis-associated proteins. (a) Representative western blotting images for the expression of ACSL4, COX-2, GPX4, p-AMPK, and t-AMPK in lung tissues. GAPDH was selected as the loading control protein. (b) Quantification analysis of the related bands of ACSL4, COX-2, GPX4, p-AMPK, and t-AMPK in lung tissues. Lung tissues were harvested on day 3 post-CLP. Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-hoc test. n ¼ 6 per group. Data are presented as means SEM. *p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001.

Article Snippet: Subsequently, the membranes were incubated with rabbit anti-AMPK (MCE, Cat# HY-P80541), anti-p-AMPK (MCE, HYP80452), GPX4 (MCE, HY-P80450), ACSL4 (Santa Cruz Biotechnology, Dallas, Texas, USA; Cat# sc-365230), COX-2 (Abcam, Cambridge, United Kingdom; Cat# ab283574), and GAPDH (MCE, HY-P80137) antibodies at 4 C overnight.

Techniques: Western Blot, Expressing, Control

Figure 4. The cellular AMPK expression and phosphorylation level. AMPK protein expressions and phosphorylation in HeLa and KO HeLa cells with or without viral infection were detected with Western blotting. (A) The expression and phosphorylation of AMPK protein on KO HeLa cells compared with HeLa cells. (B) The expression and phosphorylation of AMPK protein on HeLa cells after viral infection. (C) The expression and phosphorylation of AMPK protein on KO HeLa cells after viral infection.

Journal: Viruses

Article Title: The Function behind the Relation between Lipid Metabolism and Vimentin on H9N2 Subtype AIV Replication.

doi: 10.3390/v14081814

Figure Lengend Snippet: Figure 4. The cellular AMPK expression and phosphorylation level. AMPK protein expressions and phosphorylation in HeLa and KO HeLa cells with or without viral infection were detected with Western blotting. (A) The expression and phosphorylation of AMPK protein on KO HeLa cells compared with HeLa cells. (B) The expression and phosphorylation of AMPK protein on HeLa cells after viral infection. (C) The expression and phosphorylation of AMPK protein on KO HeLa cells after viral infection.

Article Snippet: GAPDH monoclonal antibody was purchased from Enogene Biologicals (Nanjing, China). β-actin monoclonal antibody, AMPK monoclonal antibody and AMPK phosphorylated monoclonal antibody P-AMPK were purchased from BOSTER Biologicals (Nanjing, China).

Techniques: Expressing, Phospho-proteomics, Infection, Western Blot

Figure 7. Model of lipid metabolism and vimentin on H9N2 subtype AIV. When vimentin was knocked down, the phosphorylation level of AMPK was decreased, resulting in the decreased level of HMGCR phosphorylation, which increased the enzyme activity, thereby increasing cholesterol. After the destruction of lipid rafts, the virus binding was inhibited, and cholesterol helped to stabilize the structure of lipid rafts, which might help the virus bind to cells.

Journal: Viruses

Article Title: The Function behind the Relation between Lipid Metabolism and Vimentin on H9N2 Subtype AIV Replication.

doi: 10.3390/v14081814

Figure Lengend Snippet: Figure 7. Model of lipid metabolism and vimentin on H9N2 subtype AIV. When vimentin was knocked down, the phosphorylation level of AMPK was decreased, resulting in the decreased level of HMGCR phosphorylation, which increased the enzyme activity, thereby increasing cholesterol. After the destruction of lipid rafts, the virus binding was inhibited, and cholesterol helped to stabilize the structure of lipid rafts, which might help the virus bind to cells.

Article Snippet: GAPDH monoclonal antibody was purchased from Enogene Biologicals (Nanjing, China). β-actin monoclonal antibody, AMPK monoclonal antibody and AMPK phosphorylated monoclonal antibody P-AMPK were purchased from BOSTER Biologicals (Nanjing, China).

Techniques: Phospho-proteomics, Activity Assay, Virus, Binding Assay