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rabbit polyclonal antibody against p ampk  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc rabbit polyclonal antibody against p ampk
    Rabbit Polyclonal Antibody Against P Ampk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 5243 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal antibody against p ampk/product/Cell Signaling Technology Inc
    Average 99 stars, based on 5243 article reviews
    rabbit polyclonal antibody against p ampk - by Bioz Stars, 2026-02
    99/100 stars

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    PRRSV infection activates the PP2A–HMGCR pathway. (A) Model of cholesterol synthesis via the <t>AMPK–HMGCR</t> and PP2A–HMGCR pathways. Level of p-HMGCR (inactive form) was enhanced by AMPK, resulting in the downregulation of cholesterol synthesis, but reduced by PP2A, resulting in the upregulation of cholesterol synthesis. (B – D) PAMs or PK-15 CD163 cells infected with PRRSV (MOI = 1.0) were harvested at 12, 24, and 36 hpi. The expression levels of total HMGCR and phosphorylated HMGCR (p-HMGCR) (B) , total AMPK and p-AMPK (C) , or total PP2Ac and p-PP2Ac (D) were analyzed with western blotting. PRRSV infection was verified by detecting the expression of viral N protein with anti-N antibody. The β-actin was used as the protein loading control.
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    Effect of ADP355 on the TGF-β1-induced downstream pathways. TGF-β1-induced increases in phosphorylation of SMAD2, <t>SMAD3,</t> <t>ERK,</t> and <t>AMPK.</t> Treatment with ADP355 (10 µg/mL) and adiponectin recombinant, AdipoQ (10 µg/mL), reversed TGF-β1-induced phosphorylation of SMAD3 and ERK and accentuated phosphorylation of AMPK. ( A ) Western blot analysis results. ( B ) Quantification of western blot results (* p ≤ 0.05, control vs. TGF- β, # p ≤ 0.05, TGF- β vs. TGF-β + ADP355, and & p ≤ 0.05, TGF-β vs. TGF-β + AdipoQ). The data are expressed as mean ± SD. Representative data are shown from three independent experiments.
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    Cell Signaling Technology Inc rabbit polyclonal antibodies against p ampk
    Fig. 2. The Effects of 100 nM Insulin on the Phosphorylation Levels of Akt (A), <t>AMPK</t> (B) and Nuclear and Cytoplasm Protein Levels of SREBP-1c (C) of HepG2 Cell
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    Cell Signaling Technology Inc primary rabbit polyclonal antibody against peif2α, eif2α, p-ampk and ampk
    Fig. 2. The Effects of 100 nM Insulin on the Phosphorylation Levels of Akt (A), <t>AMPK</t> (B) and Nuclear and Cytoplasm Protein Levels of SREBP-1c (C) of HepG2 Cell
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    Cell Signaling Technology Inc rabbit polyclonal antibody against p-ampk
    Fig. 2. The Effects of 100 nM Insulin on the Phosphorylation Levels of Akt (A), <t>AMPK</t> (B) and Nuclear and Cytoplasm Protein Levels of SREBP-1c (C) of HepG2 Cell
    Rabbit Polyclonal Antibody Against P Ampk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    PRRSV infection activates the PP2A–HMGCR pathway. (A) Model of cholesterol synthesis via the AMPK–HMGCR and PP2A–HMGCR pathways. Level of p-HMGCR (inactive form) was enhanced by AMPK, resulting in the downregulation of cholesterol synthesis, but reduced by PP2A, resulting in the upregulation of cholesterol synthesis. (B – D) PAMs or PK-15 CD163 cells infected with PRRSV (MOI = 1.0) were harvested at 12, 24, and 36 hpi. The expression levels of total HMGCR and phosphorylated HMGCR (p-HMGCR) (B) , total AMPK and p-AMPK (C) , or total PP2Ac and p-PP2Ac (D) were analyzed with western blotting. PRRSV infection was verified by detecting the expression of viral N protein with anti-N antibody. The β-actin was used as the protein loading control.

    Journal: Redox Biology

    Article Title: Porcine reproductive and respiratory syndrome virus nsp4 positively regulates cellular cholesterol to inhibit type I interferon production

    doi: 10.1016/j.redox.2021.102207

    Figure Lengend Snippet: PRRSV infection activates the PP2A–HMGCR pathway. (A) Model of cholesterol synthesis via the AMPK–HMGCR and PP2A–HMGCR pathways. Level of p-HMGCR (inactive form) was enhanced by AMPK, resulting in the downregulation of cholesterol synthesis, but reduced by PP2A, resulting in the upregulation of cholesterol synthesis. (B – D) PAMs or PK-15 CD163 cells infected with PRRSV (MOI = 1.0) were harvested at 12, 24, and 36 hpi. The expression levels of total HMGCR and phosphorylated HMGCR (p-HMGCR) (B) , total AMPK and p-AMPK (C) , or total PP2Ac and p-PP2Ac (D) were analyzed with western blotting. PRRSV infection was verified by detecting the expression of viral N protein with anti-N antibody. The β-actin was used as the protein loading control.

    Article Snippet: Rabbit polyclonal antibodies (pAbs) directed against p-AMPK and AMPK were purchased from Cell Signaling Technology (CST, USA).

    Techniques: Infection, Expressing, Western Blot, Control

    Effect of ADP355 on the TGF-β1-induced downstream pathways. TGF-β1-induced increases in phosphorylation of SMAD2, SMAD3, ERK, and AMPK. Treatment with ADP355 (10 µg/mL) and adiponectin recombinant, AdipoQ (10 µg/mL), reversed TGF-β1-induced phosphorylation of SMAD3 and ERK and accentuated phosphorylation of AMPK. ( A ) Western blot analysis results. ( B ) Quantification of western blot results (* p ≤ 0.05, control vs. TGF- β, # p ≤ 0.05, TGF- β vs. TGF-β + ADP355, and & p ≤ 0.05, TGF-β vs. TGF-β + AdipoQ). The data are expressed as mean ± SD. Representative data are shown from three independent experiments.

    Journal: International Journal of Molecular Sciences

    Article Title: Adiponectin-Based Peptide (ADP355) Inhibits Transforming Growth Factor-β1-Induced Fibrosis in Keloids

    doi: 10.3390/ijms21082833

    Figure Lengend Snippet: Effect of ADP355 on the TGF-β1-induced downstream pathways. TGF-β1-induced increases in phosphorylation of SMAD2, SMAD3, ERK, and AMPK. Treatment with ADP355 (10 µg/mL) and adiponectin recombinant, AdipoQ (10 µg/mL), reversed TGF-β1-induced phosphorylation of SMAD3 and ERK and accentuated phosphorylation of AMPK. ( A ) Western blot analysis results. ( B ) Quantification of western blot results (* p ≤ 0.05, control vs. TGF- β, # p ≤ 0.05, TGF- β vs. TGF-β + ADP355, and & p ≤ 0.05, TGF-β vs. TGF-β + AdipoQ). The data are expressed as mean ± SD. Representative data are shown from three independent experiments.

    Article Snippet: The membranes were washed and incubated with mouse polyclonal antibodies (Genetex, CA, USA) against β-actin and procollagen, and rabbit polyclonal antibodies (Genetex) against p-ERK, p-SMAD2, p-SMAD3, p-AMPK, and t-AMPK.

    Techniques: Recombinant, Western Blot

    Macrographic examination of xenotransplanted tissue on the back of athymic nude mice before and after treatment ( A ). Weight of xenografted keloid tissues after intralesional injection of ADP355 and AdipoQ. The weight of the tissues was normalized to the baseline weight, and the weight of adiponectin-treated tissue was compared to that of control. ADP355-treated lesions showed a significant weight reduction ( B , * p ≤ 0.05). Procollagen protein expression was significantly reduced while p-AMPK expression increased following treatment with ADP355 and AdipoQ ( C , * p ≤ 0.05). The data are expressed as mean ± SD. Representative data are shown from three independent experiments.

    Journal: International Journal of Molecular Sciences

    Article Title: Adiponectin-Based Peptide (ADP355) Inhibits Transforming Growth Factor-β1-Induced Fibrosis in Keloids

    doi: 10.3390/ijms21082833

    Figure Lengend Snippet: Macrographic examination of xenotransplanted tissue on the back of athymic nude mice before and after treatment ( A ). Weight of xenografted keloid tissues after intralesional injection of ADP355 and AdipoQ. The weight of the tissues was normalized to the baseline weight, and the weight of adiponectin-treated tissue was compared to that of control. ADP355-treated lesions showed a significant weight reduction ( B , * p ≤ 0.05). Procollagen protein expression was significantly reduced while p-AMPK expression increased following treatment with ADP355 and AdipoQ ( C , * p ≤ 0.05). The data are expressed as mean ± SD. Representative data are shown from three independent experiments.

    Article Snippet: The membranes were washed and incubated with mouse polyclonal antibodies (Genetex, CA, USA) against β-actin and procollagen, and rabbit polyclonal antibodies (Genetex) against p-ERK, p-SMAD2, p-SMAD3, p-AMPK, and t-AMPK.

    Techniques: Injection, Expressing

    Fig. 2. The Effects of 100 nM Insulin on the Phosphorylation Levels of Akt (A), AMPK (B) and Nuclear and Cytoplasm Protein Levels of SREBP-1c (C) of HepG2 Cell

    Journal: Biological & pharmaceutical bulletin

    Article Title: Polydatin Improves Glucose and Lipid Metabolisms in Insulin-Resistant HepG2 Cells through the AMPK Pathway.

    doi: 10.1248/bpb.b17-01027

    Figure Lengend Snippet: Fig. 2. The Effects of 100 nM Insulin on the Phosphorylation Levels of Akt (A), AMPK (B) and Nuclear and Cytoplasm Protein Levels of SREBP-1c (C) of HepG2 Cell

    Article Snippet: In the wake of washing, the layers were brooded overnight at 4°C with one of these primary antibodies: rabbit polyclonal antibodies against p-AMPK (Thr172; Cell Signaling Technology, Cat. No. 2535, U.S.A.), P-ACC (Ser79; Cell Signaling Technology, Cat. No. 11818), AMPK (Cell Signaling Technology, Cat. No. 5831), ACC (Cell Signaling Technology, Cat. No. 3676), P-Akt (ser473, Cell Signaling Technology; Cat. No. 4060), P-glycogen synthase kinase (GSK)-3β (ser9; Cell Signaling Technology, Cat. No. 5558), GSK-3β (1 : 1000; Cell Signaling Technology, Cat. No. 9315), and SREBP-1c (1 : 300; Santa Cruz Biotechnology, Cat. No. sc-17755, U.S.A.); rabbit monoclonal immune response against low-density lipoprotein receptor (LDLR) (1 : 1000; Proteintech, Cat. No. 10785-1-AP, U.S.A.) and Akt (pan; 1 : 1000; Cell Signaling Technology, Cat. No. 4691); mouse monoclonal immunizer against Tubulin (1 : 10000; Sigma), Actin (1 : 1000; Beyotime) and Histone 1.4 (1 : 1000; Sigma).

    Techniques: Phospho-proteomics

    Fig. 5. The Effects of Polydatin on the Phosphorylation Levels of AMPK (A), Akt (B) and GSK-3β (C) of Insulin-Resistant HepG2 Cells

    Journal: Biological & pharmaceutical bulletin

    Article Title: Polydatin Improves Glucose and Lipid Metabolisms in Insulin-Resistant HepG2 Cells through the AMPK Pathway.

    doi: 10.1248/bpb.b17-01027

    Figure Lengend Snippet: Fig. 5. The Effects of Polydatin on the Phosphorylation Levels of AMPK (A), Akt (B) and GSK-3β (C) of Insulin-Resistant HepG2 Cells

    Article Snippet: In the wake of washing, the layers were brooded overnight at 4°C with one of these primary antibodies: rabbit polyclonal antibodies against p-AMPK (Thr172; Cell Signaling Technology, Cat. No. 2535, U.S.A.), P-ACC (Ser79; Cell Signaling Technology, Cat. No. 11818), AMPK (Cell Signaling Technology, Cat. No. 5831), ACC (Cell Signaling Technology, Cat. No. 3676), P-Akt (ser473, Cell Signaling Technology; Cat. No. 4060), P-glycogen synthase kinase (GSK)-3β (ser9; Cell Signaling Technology, Cat. No. 5558), GSK-3β (1 : 1000; Cell Signaling Technology, Cat. No. 9315), and SREBP-1c (1 : 300; Santa Cruz Biotechnology, Cat. No. sc-17755, U.S.A.); rabbit monoclonal immune response against low-density lipoprotein receptor (LDLR) (1 : 1000; Proteintech, Cat. No. 10785-1-AP, U.S.A.) and Akt (pan; 1 : 1000; Cell Signaling Technology, Cat. No. 4691); mouse monoclonal immunizer against Tubulin (1 : 10000; Sigma), Actin (1 : 1000; Beyotime) and Histone 1.4 (1 : 1000; Sigma).

    Techniques: Phospho-proteomics