acetyl-coa Search Results


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  • 95
    Millipore acetyl coa
    Acetyl Coa, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 1624 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc acetyl coa carboxylase acc
    Effects of the expression of an active form of AMP-activated protein kinase (AMPK) in the liver on body weight and food intake. Ten-week-old male C57BL/6J mice received injections of adenovirus (Ad) expressing the green fluorescent protein (GFP) or a constitutively active form of AMPKα2 (AMPK-CA) and were studied for the indicated times after adenovirus injection and in the indicated nutritional state. ( A ) Western blot analysis of liver lysates with antibodies raised against pan-AMPKα and myc-tagged AMPK-CA was performed on days 2 and day 8 after adenovirus administration; ( B ) Western blot analysis of liver lysates from fed mice 48 h after the injection of Ad GFP or Ad AMPK-CA, with the antibodies indicated. Each lane represents a liver sample from an individual mouse. The panel on the right shows Ser79 phosphorylated acetyl <t>CoA</t> carboxylase/ total acetyl CoA carboxylase <t>(P-ACC/ACC)</t> ratios from the quantification of immunoblot images ( n = 5); ( C ) Hepatic malonyl-CoA levels in 8 h-fasted mice 48 h after the injection of Ad GFP or Ad AMPK-CA ( n = 5); ( D ) Effect of AMPK activation in the liver on the expression of Cpt1a and Cpt 2 genes. Total RNA was isolated from the liver of 24 h-fasted mice 48 h after the injection of Ad GFP or Ad AMPK-CA ( n = 6). The expression of Cpt1a and Cpt2 genes was assessed by real-time quantitative RT-PCR. Relative mRNA levels are expressed as fold-activation relative to levels in Ad GFP livers; ( E ) Body weight changes and ( F ) cumulative food intake measured for 8 days after adenovirus administration ( n = 11–12 per group). Data are means ± standard error of mean (SEM). * p
    Acetyl Coa Carboxylase Acc, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 571 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/acetyl coa carboxylase acc/product/Cell Signaling Technology Inc
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    99
    Cell Signaling Technology Inc acetyl coa carboxylase
    Molecular characterization of hepatocellular carcinomas developed in sgPten/c-Met mice. ( a ) Levels of activation of AKT/mTOR and Ras/MAPK pathways in wild-type (WT) and sgPten/c-Met mouse livers, as detected by western blot analysis. Representative blots are shown. GAPDH and β-actin were used as loading controls. ( b ) Immunohistochemical staining of WT and sgPten/c-Met mouse livers. Original magnifications: × 100 for Pten, p-AKT S473 , fatty acid <t>synthase</t> (FASN) and <t>acetyl-CoA</t> carboxylase (ACC) proteins; × 200 for Ki67. p, phosphorylated; t, total.
    Acetyl Coa Carboxylase, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 381 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/acetyl coa carboxylase/product/Cell Signaling Technology Inc
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    99
    Cell Signaling Technology Inc phospho acetyl coa carboxylase
    Effects of the expression of an active form of AMP-activated protein kinase (AMPK) in the liver on body weight and food intake. Ten-week-old male C57BL/6J mice received injections of adenovirus (Ad) expressing the green fluorescent protein (GFP) or a constitutively active form of AMPKα2 (AMPK-CA) and were studied for the indicated times after adenovirus injection and in the indicated nutritional state. ( A ) Western blot analysis of liver lysates with antibodies raised against pan-AMPKα and myc-tagged AMPK-CA was performed on days 2 and day 8 after adenovirus administration; ( B ) Western blot analysis of liver lysates from fed mice 48 h after the injection of Ad GFP or Ad AMPK-CA, with the antibodies indicated. Each lane represents a liver sample from an individual mouse. The panel on the right shows <t>Ser79</t> phosphorylated acetyl CoA carboxylase/ total acetyl CoA carboxylase (P-ACC/ACC) ratios from the quantification of immunoblot images ( n = 5); ( C ) Hepatic malonyl-CoA levels in 8 h-fasted mice 48 h after the injection of Ad GFP or Ad AMPK-CA ( n = 5); ( D ) Effect of AMPK activation in the liver on the expression of Cpt1a and Cpt 2 genes. Total RNA was isolated from the liver of 24 h-fasted mice 48 h after the injection of Ad GFP or Ad AMPK-CA ( n = 6). The expression of Cpt1a and Cpt2 genes was assessed by real-time quantitative RT-PCR. Relative mRNA levels are expressed as fold-activation relative to levels in Ad GFP livers; ( E ) Body weight changes and ( F ) cumulative food intake measured for 8 days after adenovirus administration ( n = 11–12 per group). Data are means ± standard error of mean (SEM). * p
    Phospho Acetyl Coa Carboxylase, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 209 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho acetyl coa carboxylase/product/Cell Signaling Technology Inc
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    98
    Millipore acetyl coenzyme a assay kit
    Effects of the expression of an active form of AMP-activated protein kinase (AMPK) in the liver on body weight and food intake. Ten-week-old male C57BL/6J mice received injections of adenovirus (Ad) expressing the green fluorescent protein (GFP) or a constitutively active form of AMPKα2 (AMPK-CA) and were studied for the indicated times after adenovirus injection and in the indicated nutritional state. ( A ) Western blot analysis of liver lysates with antibodies raised against pan-AMPKα and myc-tagged AMPK-CA was performed on days 2 and day 8 after adenovirus administration; ( B ) Western blot analysis of liver lysates from fed mice 48 h after the injection of Ad GFP or Ad AMPK-CA, with the antibodies indicated. Each lane represents a liver sample from an individual mouse. The panel on the right shows <t>Ser79</t> phosphorylated acetyl CoA carboxylase/ total acetyl CoA carboxylase (P-ACC/ACC) ratios from the quantification of immunoblot images ( n = 5); ( C ) Hepatic malonyl-CoA levels in 8 h-fasted mice 48 h after the injection of Ad GFP or Ad AMPK-CA ( n = 5); ( D ) Effect of AMPK activation in the liver on the expression of Cpt1a and Cpt 2 genes. Total RNA was isolated from the liver of 24 h-fasted mice 48 h after the injection of Ad GFP or Ad AMPK-CA ( n = 6). The expression of Cpt1a and Cpt2 genes was assessed by real-time quantitative RT-PCR. Relative mRNA levels are expressed as fold-activation relative to levels in Ad GFP livers; ( E ) Body weight changes and ( F ) cumulative food intake measured for 8 days after adenovirus administration ( n = 11–12 per group). Data are means ± standard error of mean (SEM). * p
    Acetyl Coenzyme A Assay Kit, supplied by Millipore, used in various techniques. Bioz Stars score: 98/100, based on 48 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Moravek Biochemicals c acetyl coa
    <t>hMOF</t> Lys-274 mutants are thermally destabilized, but are still able to bind cofactor. Normalized thermal denaturation curves for hMOF Lys-274 mutants in the absence ( A ) and presence ( B ) of 100 μ m <t>CoA</t> are shown. SYPRO Orange fluorescence is shown,
    C Acetyl Coa, supplied by Moravek Biochemicals, used in various techniques. Bioz Stars score: 90/100, based on 79 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/c acetyl coa/product/Moravek Biochemicals
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    98
    Abcam picoprobe acetyl coa assay kit
    <t>hMOF</t> Lys-274 mutants are thermally destabilized, but are still able to bind cofactor. Normalized thermal denaturation curves for hMOF Lys-274 mutants in the absence ( A ) and presence ( B ) of 100 μ m <t>CoA</t> are shown. SYPRO Orange fluorescence is shown,
    Picoprobe Acetyl Coa Assay Kit, supplied by Abcam, used in various techniques. Bioz Stars score: 98/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Millipore acetyl coenzyme a sodium salt
    <t>hMOF</t> Lys-274 mutants are thermally destabilized, but are still able to bind cofactor. Normalized thermal denaturation curves for hMOF Lys-274 mutants in the absence ( A ) and presence ( B ) of 100 μ m <t>CoA</t> are shown. SYPRO Orange fluorescence is shown,
    Acetyl Coenzyme A Sodium Salt, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 51 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    BioVision picoprobe acetyl coa fluorometric assay kit
    <t>hMOF</t> Lys-274 mutants are thermally destabilized, but are still able to bind cofactor. Normalized thermal denaturation curves for hMOF Lys-274 mutants in the absence ( A ) and presence ( B ) of 100 μ m <t>CoA</t> are shown. SYPRO Orange fluorescence is shown,
    Picoprobe Acetyl Coa Fluorometric Assay Kit, supplied by BioVision, used in various techniques. Bioz Stars score: 99/100, based on 59 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore acetyl coenzyme a acetyl coa
    <t>hMOF</t> Lys-274 mutants are thermally destabilized, but are still able to bind cofactor. Normalized thermal denaturation curves for hMOF Lys-274 mutants in the absence ( A ) and presence ( B ) of 100 μ m <t>CoA</t> are shown. SYPRO Orange fluorescence is shown,
    Acetyl Coenzyme A Acetyl Coa, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 74 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Abcam acetyl coa
    <t>hMOF</t> Lys-274 mutants are thermally destabilized, but are still able to bind cofactor. Normalized thermal denaturation curves for hMOF Lys-274 mutants in the absence ( A ) and presence ( B ) of 100 μ m <t>CoA</t> are shown. SYPRO Orange fluorescence is shown,
    Acetyl Coa, supplied by Abcam, used in various techniques. Bioz Stars score: 92/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Santa Cruz Biotechnology acetyl coa carboxylase acc
    Effects of FB on hepatic TG content and the lipogenic pathway in PPARα +/+ and PPARα -/- mice. Fenofibrate (+ FB) was administered to PPARα +/+ and PPARα -/- mice on the background of C57BL/6N at a dose (50 mg/kg/day) for 3 weeks. (A) Effects on triglyceride (TG) content. (B) Representative images and (C) Quantification of Western blots for ACOX1 (peroxisomal <t>acyl-CoA</t> oxidase 1, PPARα activation marker) and lipogenic proteins: mSREBP1c (matured form of sterol regulatory element-binding protein 1 c), <t>ACC</t> (acetyl-CoA carboxylase), FAS (fatty acid synthase) and SCD1 (stearoyl-CoA desaturase 1). ** p
    Acetyl Coa Carboxylase Acc, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 138 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Abcam anti acetyl coenzyme a carboxylase antibody ep687y
    Effects of FB on hepatic TG content and the lipogenic pathway in PPARα +/+ and PPARα -/- mice. Fenofibrate (+ FB) was administered to PPARα +/+ and PPARα -/- mice on the background of C57BL/6N at a dose (50 mg/kg/day) for 3 weeks. (A) Effects on triglyceride (TG) content. (B) Representative images and (C) Quantification of Western blots for ACOX1 (peroxisomal <t>acyl-CoA</t> oxidase 1, PPARα activation marker) and lipogenic proteins: mSREBP1c (matured form of sterol regulatory element-binding protein 1 c), <t>ACC</t> (acetyl-CoA carboxylase), FAS (fatty acid synthase) and SCD1 (stearoyl-CoA desaturase 1). ** p
    Anti Acetyl Coenzyme A Carboxylase Antibody Ep687y, supplied by Abcam, used in various techniques. Bioz Stars score: 98/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Effects of the expression of an active form of AMP-activated protein kinase (AMPK) in the liver on body weight and food intake. Ten-week-old male C57BL/6J mice received injections of adenovirus (Ad) expressing the green fluorescent protein (GFP) or a constitutively active form of AMPKα2 (AMPK-CA) and were studied for the indicated times after adenovirus injection and in the indicated nutritional state. ( A ) Western blot analysis of liver lysates with antibodies raised against pan-AMPKα and myc-tagged AMPK-CA was performed on days 2 and day 8 after adenovirus administration; ( B ) Western blot analysis of liver lysates from fed mice 48 h after the injection of Ad GFP or Ad AMPK-CA, with the antibodies indicated. Each lane represents a liver sample from an individual mouse. The panel on the right shows Ser79 phosphorylated acetyl CoA carboxylase/ total acetyl CoA carboxylase (P-ACC/ACC) ratios from the quantification of immunoblot images ( n = 5); ( C ) Hepatic malonyl-CoA levels in 8 h-fasted mice 48 h after the injection of Ad GFP or Ad AMPK-CA ( n = 5); ( D ) Effect of AMPK activation in the liver on the expression of Cpt1a and Cpt 2 genes. Total RNA was isolated from the liver of 24 h-fasted mice 48 h after the injection of Ad GFP or Ad AMPK-CA ( n = 6). The expression of Cpt1a and Cpt2 genes was assessed by real-time quantitative RT-PCR. Relative mRNA levels are expressed as fold-activation relative to levels in Ad GFP livers; ( E ) Body weight changes and ( F ) cumulative food intake measured for 8 days after adenovirus administration ( n = 11–12 per group). Data are means ± standard error of mean (SEM). * p

    Journal: International Journal of Molecular Sciences

    Article Title: AMPK Activation Reduces Hepatic Lipid Content by Increasing Fat Oxidation In Vivo

    doi: 10.3390/ijms19092826

    Figure Lengend Snippet: Effects of the expression of an active form of AMP-activated protein kinase (AMPK) in the liver on body weight and food intake. Ten-week-old male C57BL/6J mice received injections of adenovirus (Ad) expressing the green fluorescent protein (GFP) or a constitutively active form of AMPKα2 (AMPK-CA) and were studied for the indicated times after adenovirus injection and in the indicated nutritional state. ( A ) Western blot analysis of liver lysates with antibodies raised against pan-AMPKα and myc-tagged AMPK-CA was performed on days 2 and day 8 after adenovirus administration; ( B ) Western blot analysis of liver lysates from fed mice 48 h after the injection of Ad GFP or Ad AMPK-CA, with the antibodies indicated. Each lane represents a liver sample from an individual mouse. The panel on the right shows Ser79 phosphorylated acetyl CoA carboxylase/ total acetyl CoA carboxylase (P-ACC/ACC) ratios from the quantification of immunoblot images ( n = 5); ( C ) Hepatic malonyl-CoA levels in 8 h-fasted mice 48 h after the injection of Ad GFP or Ad AMPK-CA ( n = 5); ( D ) Effect of AMPK activation in the liver on the expression of Cpt1a and Cpt 2 genes. Total RNA was isolated from the liver of 24 h-fasted mice 48 h after the injection of Ad GFP or Ad AMPK-CA ( n = 6). The expression of Cpt1a and Cpt2 genes was assessed by real-time quantitative RT-PCR. Relative mRNA levels are expressed as fold-activation relative to levels in Ad GFP livers; ( E ) Body weight changes and ( F ) cumulative food intake measured for 8 days after adenovirus administration ( n = 11–12 per group). Data are means ± standard error of mean (SEM). * p

    Article Snippet: Primary antibodies directed against total AMPKα (#2532), total acetyl-CoA carboxylase (ACC) (#3676), and ACC phosphorylated at Ser79 (#3661) were purchased from Cell Signaling Technology (Danvers, MA, USA) and myc epitope tag (clone 9E10) from Sigma (Saint-Quentin-Fallavier, France).

    Techniques: Expressing, Mouse Assay, Injection, Western Blot, Activation Assay, Cycling Probe Technology, Isolation, Quantitative RT-PCR

    Molecular characterization of hepatocellular carcinomas developed in sgPten/c-Met mice. ( a ) Levels of activation of AKT/mTOR and Ras/MAPK pathways in wild-type (WT) and sgPten/c-Met mouse livers, as detected by western blot analysis. Representative blots are shown. GAPDH and β-actin were used as loading controls. ( b ) Immunohistochemical staining of WT and sgPten/c-Met mouse livers. Original magnifications: × 100 for Pten, p-AKT S473 , fatty acid synthase (FASN) and acetyl-CoA carboxylase (ACC) proteins; × 200 for Ki67. p, phosphorylated; t, total.

    Journal: Experimental & Molecular Medicine

    Article Title: Loss of Pten synergizes with c-Met to promote hepatocellular carcinoma development via mTORC2 pathway

    doi: 10.1038/emm.2017.158

    Figure Lengend Snippet: Molecular characterization of hepatocellular carcinomas developed in sgPten/c-Met mice. ( a ) Levels of activation of AKT/mTOR and Ras/MAPK pathways in wild-type (WT) and sgPten/c-Met mouse livers, as detected by western blot analysis. Representative blots are shown. GAPDH and β-actin were used as loading controls. ( b ) Immunohistochemical staining of WT and sgPten/c-Met mouse livers. Original magnifications: × 100 for Pten, p-AKT S473 , fatty acid synthase (FASN) and acetyl-CoA carboxylase (ACC) proteins; × 200 for Ki67. p, phosphorylated; t, total.

    Article Snippet: Immunohistochemistry (IHC) was performed as previously described., The primary antibodies against c-Met (Abcam, Cambridge, MA, USA; 1:100), p-AKTS473 (Cell Signaling Technology, Danvers, MA, USA; 1:100), Pten (Cell Signaling Technology; 1:100), fatty acid synthase (FASN; Cell Signaling Technology; 1:150), acetyl-CoA carboxylase (ACC; Cell Signaling Technology; 1:100), p-ERK (Cell Signaling Technology; 1:100), and Ki67 (Thermo Fisher Scientific, Waltham, MA, USA; 1:150) were used in the present investigation.

    Techniques: Mouse Assay, Activation Assay, Western Blot, Immunohistochemistry, Staining

    Effects of the expression of an active form of AMP-activated protein kinase (AMPK) in the liver on body weight and food intake. Ten-week-old male C57BL/6J mice received injections of adenovirus (Ad) expressing the green fluorescent protein (GFP) or a constitutively active form of AMPKα2 (AMPK-CA) and were studied for the indicated times after adenovirus injection and in the indicated nutritional state. ( A ) Western blot analysis of liver lysates with antibodies raised against pan-AMPKα and myc-tagged AMPK-CA was performed on days 2 and day 8 after adenovirus administration; ( B ) Western blot analysis of liver lysates from fed mice 48 h after the injection of Ad GFP or Ad AMPK-CA, with the antibodies indicated. Each lane represents a liver sample from an individual mouse. The panel on the right shows Ser79 phosphorylated acetyl CoA carboxylase/ total acetyl CoA carboxylase (P-ACC/ACC) ratios from the quantification of immunoblot images ( n = 5); ( C ) Hepatic malonyl-CoA levels in 8 h-fasted mice 48 h after the injection of Ad GFP or Ad AMPK-CA ( n = 5); ( D ) Effect of AMPK activation in the liver on the expression of Cpt1a and Cpt 2 genes. Total RNA was isolated from the liver of 24 h-fasted mice 48 h after the injection of Ad GFP or Ad AMPK-CA ( n = 6). The expression of Cpt1a and Cpt2 genes was assessed by real-time quantitative RT-PCR. Relative mRNA levels are expressed as fold-activation relative to levels in Ad GFP livers; ( E ) Body weight changes and ( F ) cumulative food intake measured for 8 days after adenovirus administration ( n = 11–12 per group). Data are means ± standard error of mean (SEM). * p

    Journal: International Journal of Molecular Sciences

    Article Title: AMPK Activation Reduces Hepatic Lipid Content by Increasing Fat Oxidation In Vivo

    doi: 10.3390/ijms19092826

    Figure Lengend Snippet: Effects of the expression of an active form of AMP-activated protein kinase (AMPK) in the liver on body weight and food intake. Ten-week-old male C57BL/6J mice received injections of adenovirus (Ad) expressing the green fluorescent protein (GFP) or a constitutively active form of AMPKα2 (AMPK-CA) and were studied for the indicated times after adenovirus injection and in the indicated nutritional state. ( A ) Western blot analysis of liver lysates with antibodies raised against pan-AMPKα and myc-tagged AMPK-CA was performed on days 2 and day 8 after adenovirus administration; ( B ) Western blot analysis of liver lysates from fed mice 48 h after the injection of Ad GFP or Ad AMPK-CA, with the antibodies indicated. Each lane represents a liver sample from an individual mouse. The panel on the right shows Ser79 phosphorylated acetyl CoA carboxylase/ total acetyl CoA carboxylase (P-ACC/ACC) ratios from the quantification of immunoblot images ( n = 5); ( C ) Hepatic malonyl-CoA levels in 8 h-fasted mice 48 h after the injection of Ad GFP or Ad AMPK-CA ( n = 5); ( D ) Effect of AMPK activation in the liver on the expression of Cpt1a and Cpt 2 genes. Total RNA was isolated from the liver of 24 h-fasted mice 48 h after the injection of Ad GFP or Ad AMPK-CA ( n = 6). The expression of Cpt1a and Cpt2 genes was assessed by real-time quantitative RT-PCR. Relative mRNA levels are expressed as fold-activation relative to levels in Ad GFP livers; ( E ) Body weight changes and ( F ) cumulative food intake measured for 8 days after adenovirus administration ( n = 11–12 per group). Data are means ± standard error of mean (SEM). * p

    Article Snippet: Primary antibodies directed against total AMPKα (#2532), total acetyl-CoA carboxylase (ACC) (#3676), and ACC phosphorylated at Ser79 (#3661) were purchased from Cell Signaling Technology (Danvers, MA, USA) and myc epitope tag (clone 9E10) from Sigma (Saint-Quentin-Fallavier, France).

    Techniques: Expressing, Mouse Assay, Injection, Western Blot, Activation Assay, Cycling Probe Technology, Isolation, Quantitative RT-PCR

    hMOF Lys-274 mutants are thermally destabilized, but are still able to bind cofactor. Normalized thermal denaturation curves for hMOF Lys-274 mutants in the absence ( A ) and presence ( B ) of 100 μ m CoA are shown. SYPRO Orange fluorescence is shown,

    Journal: The Journal of Biological Chemistry

    Article Title: Structural and Functional Role of Acetyltransferase hMOF K274 Autoacetylation *

    doi: 10.1074/jbc.M116.736264

    Figure Lengend Snippet: hMOF Lys-274 mutants are thermally destabilized, but are still able to bind cofactor. Normalized thermal denaturation curves for hMOF Lys-274 mutants in the absence ( A ) and presence ( B ) of 100 μ m CoA are shown. SYPRO Orange fluorescence is shown,

    Article Snippet: Briefly, 50 n m hMOF or 200 n m MOZ was incubated with 400 μ m substrate peptide (H4(1–19) peptide for hMOF and H3(1–19) for MOZ) (GenScript) and 50 μ m [14 C]acetyl-CoA (50–60 mCi/mmol, Moravek) in reaction buffer (100 m m acetate, 50 m m Bistris, 50 m m Tris at various pH values 100 m m NaCl, 800 μ m cysteine, and 0.25 mg/ml of BSA for hMOF and 40 m m Tris-HCl (pH 8.0), 100 m m NaCl, 1 m m DTT for MOZ) at a final volume of 50 μl and incubated at room temperature for 1 h. To quench the reaction, 20 μl of the reaction mixture was added to negatively charged P81 paper (Millipore).

    Techniques: Fluorescence

    hMOF WT and hMOF K268M share very similar kinetic profiles. Michaelis-Menten curves are shown for hMOF-WT and hMOF-K268M against acetyl-CoA ( A ) and histone H4 peptide ( B ). Different k cat values were calculated for data in each graph to demonstrate similarities

    Journal: The Journal of Biological Chemistry

    Article Title: Structural and Functional Role of Acetyltransferase hMOF K274 Autoacetylation *

    doi: 10.1074/jbc.M116.736264

    Figure Lengend Snippet: hMOF WT and hMOF K268M share very similar kinetic profiles. Michaelis-Menten curves are shown for hMOF-WT and hMOF-K268M against acetyl-CoA ( A ) and histone H4 peptide ( B ). Different k cat values were calculated for data in each graph to demonstrate similarities

    Article Snippet: Briefly, 50 n m hMOF or 200 n m MOZ was incubated with 400 μ m substrate peptide (H4(1–19) peptide for hMOF and H3(1–19) for MOZ) (GenScript) and 50 μ m [14 C]acetyl-CoA (50–60 mCi/mmol, Moravek) in reaction buffer (100 m m acetate, 50 m m Bistris, 50 m m Tris at various pH values 100 m m NaCl, 800 μ m cysteine, and 0.25 mg/ml of BSA for hMOF and 40 m m Tris-HCl (pH 8.0), 100 m m NaCl, 1 m m DTT for MOZ) at a final volume of 50 μl and incubated at room temperature for 1 h. To quench the reaction, 20 μl of the reaction mixture was added to negatively charged P81 paper (Millipore).

    Techniques:

    Effects of FB on hepatic TG content and the lipogenic pathway in PPARα +/+ and PPARα -/- mice. Fenofibrate (+ FB) was administered to PPARα +/+ and PPARα -/- mice on the background of C57BL/6N at a dose (50 mg/kg/day) for 3 weeks. (A) Effects on triglyceride (TG) content. (B) Representative images and (C) Quantification of Western blots for ACOX1 (peroxisomal acyl-CoA oxidase 1, PPARα activation marker) and lipogenic proteins: mSREBP1c (matured form of sterol regulatory element-binding protein 1 c), ACC (acetyl-CoA carboxylase), FAS (fatty acid synthase) and SCD1 (stearoyl-CoA desaturase 1). ** p

    Journal: PLoS ONE

    Article Title: Chronic activation of PPARα with fenofibrate reduces autophagic proteins in the liver of mice independent of FGF21

    doi: 10.1371/journal.pone.0173676

    Figure Lengend Snippet: Effects of FB on hepatic TG content and the lipogenic pathway in PPARα +/+ and PPARα -/- mice. Fenofibrate (+ FB) was administered to PPARα +/+ and PPARα -/- mice on the background of C57BL/6N at a dose (50 mg/kg/day) for 3 weeks. (A) Effects on triglyceride (TG) content. (B) Representative images and (C) Quantification of Western blots for ACOX1 (peroxisomal acyl-CoA oxidase 1, PPARα activation marker) and lipogenic proteins: mSREBP1c (matured form of sterol regulatory element-binding protein 1 c), ACC (acetyl-CoA carboxylase), FAS (fatty acid synthase) and SCD1 (stearoyl-CoA desaturase 1). ** p

    Article Snippet: Key lipogenic enzymes were examined using specific antibodies including matured form of mSREBP-1c, acetyl-CoA carboxylase (ACC), fatty acid synthase (FAS) and stearoyl-CoA desaturase (SCD1) (Santa Cruz, USA).

    Techniques: Mouse Assay, Western Blot, Activation Assay, Marker, Binding Assay