anti phospho ampk alpha t172  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho ampk alpha t172
    Anti Phospho Ampk Alpha T172, supplied by Cell Signaling Technology Inc, 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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    anti phospho ampk alpha t172 antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho ampk alpha t172 antibody
    Anti Phospho Ampk Alpha T172 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho ampk alpha t172 antibody/product/Cell Signaling Technology Inc
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    anti phospho ampk alpha t172  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho ampk alpha t172
    Anti Phospho Ampk Alpha T172, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho ampk alpha t172/product/Cell Signaling Technology Inc
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    anti phospho ampk alpha t172  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho ampk alpha t172
    LMNA deletion inhibits de novo fat synthesis through AMPKα phosphorylation. ( A ) The expression levels of AMPKα and its phosphorylated form in LMNA -KO 7701 cells are shown with the corresponding plot of the quantitative analysis ( n = 3) ( B ). ( C ) CO-/C IP assays were performed to assess the endogenous interaction between pLamin Aand <t>pAMPKα-T172</t> or between lamin A/C and pAMPKα-T172 in 7701 cells. IgG was used as a negative control, and the input was used to examine the levels of pAMPKα-T172 and lamin A/C. ( D ) An exogenous reverse pull-down experiment was performed in 7701 cell lines. 7701 cells were transiently transfected with the <t>AMPK</t> α-FLAG plasmid or control vector for 48 h. An anti-FLAG antibody was used to immunoprecipitate the cell lysates. ( E ) HEK293T cells were transiently cotransfected with the plasmid containing the LMNA cDNA and the AMPKα -N, -C and -F plasmid or control vector. An anti-FLAG antibody was used to immunoprecipitate the nuclear lysates. Data are presented as the means ± SD. ns , p > 0.05, * p < 0.05, ** p < 0.01, and *** p < 0.001.
    Anti Phospho Ampk Alpha T172, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho ampk alpha t172/product/Cell Signaling Technology Inc
    Average 98 stars, based on 1 article reviews
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    anti phospho ampk alpha t172 - by Bioz Stars, 2024-07
    98/100 stars

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    1) Product Images from "Loss of Mature Lamin A/C Triggers a Shift in Intracellular Metabolic Homeostasis via AMPKα Activation"

    Article Title: Loss of Mature Lamin A/C Triggers a Shift in Intracellular Metabolic Homeostasis via AMPKα Activation

    Journal: Cells

    doi: 10.3390/cells11243988

    LMNA deletion inhibits de novo fat synthesis through AMPKα phosphorylation. ( A ) The expression levels of AMPKα and its phosphorylated form in LMNA -KO 7701 cells are shown with the corresponding plot of the quantitative analysis ( n = 3) ( B ). ( C ) CO-/C IP assays were performed to assess the endogenous interaction between pLamin Aand pAMPKα-T172 or between lamin A/C and pAMPKα-T172 in 7701 cells. IgG was used as a negative control, and the input was used to examine the levels of pAMPKα-T172 and lamin A/C. ( D ) An exogenous reverse pull-down experiment was performed in 7701 cell lines. 7701 cells were transiently transfected with the AMPK α-FLAG plasmid or control vector for 48 h. An anti-FLAG antibody was used to immunoprecipitate the cell lysates. ( E ) HEK293T cells were transiently cotransfected with the plasmid containing the LMNA cDNA and the AMPKα -N, -C and -F plasmid or control vector. An anti-FLAG antibody was used to immunoprecipitate the nuclear lysates. Data are presented as the means ± SD. ns , p > 0.05, * p < 0.05, ** p < 0.01, and *** p < 0.001.
    Figure Legend Snippet: LMNA deletion inhibits de novo fat synthesis through AMPKα phosphorylation. ( A ) The expression levels of AMPKα and its phosphorylated form in LMNA -KO 7701 cells are shown with the corresponding plot of the quantitative analysis ( n = 3) ( B ). ( C ) CO-/C IP assays were performed to assess the endogenous interaction between pLamin Aand pAMPKα-T172 or between lamin A/C and pAMPKα-T172 in 7701 cells. IgG was used as a negative control, and the input was used to examine the levels of pAMPKα-T172 and lamin A/C. ( D ) An exogenous reverse pull-down experiment was performed in 7701 cell lines. 7701 cells were transiently transfected with the AMPK α-FLAG plasmid or control vector for 48 h. An anti-FLAG antibody was used to immunoprecipitate the cell lysates. ( E ) HEK293T cells were transiently cotransfected with the plasmid containing the LMNA cDNA and the AMPKα -N, -C and -F plasmid or control vector. An anti-FLAG antibody was used to immunoprecipitate the nuclear lysates. Data are presented as the means ± SD. ns , p > 0.05, * p < 0.05, ** p < 0.01, and *** p < 0.001.

    Techniques Used: Expressing, Negative Control, Transfection, Plasmid Preparation

    Abnormalities in Lamin A/C function trigger AMPKα activation. ( A ) Mutations in the LMNA structure and sequence are shown: D203N is located in the rod domain and R482W, G465D, and T528R are located in the LTD. Western blotting was performed to detect changes in lamin A/C, pLamin A/C, AMPKα, and pAMPKα-T172 levels upon the rescue of lamin A/C expression via the transfection of the LMNC cDNA, LMNA-GFP cDNA and LMNA mutants, and the corresponding semiquantitative data obtained after GAPDH normalization are shown. ( B ) TG and lactate synthesis were quantified in the different transfected groups ( n = 3). ( C ) Western blotting was performed to assess concentration-dependent changes in lamin A/C, pLamin A/C, AMPKα, pAMPKα, pACC1 and ACC1 levels in 7701, HepG2 and MHCC97-H cells treated with lonafarnib. The corresponding quantitative data were obtained by standardization with GAPDH. Data are presented as the means of at least three independent experiments ± SD. * p < 0.05, ** p < 0.01, and *** p < 0.001.
    Figure Legend Snippet: Abnormalities in Lamin A/C function trigger AMPKα activation. ( A ) Mutations in the LMNA structure and sequence are shown: D203N is located in the rod domain and R482W, G465D, and T528R are located in the LTD. Western blotting was performed to detect changes in lamin A/C, pLamin A/C, AMPKα, and pAMPKα-T172 levels upon the rescue of lamin A/C expression via the transfection of the LMNC cDNA, LMNA-GFP cDNA and LMNA mutants, and the corresponding semiquantitative data obtained after GAPDH normalization are shown. ( B ) TG and lactate synthesis were quantified in the different transfected groups ( n = 3). ( C ) Western blotting was performed to assess concentration-dependent changes in lamin A/C, pLamin A/C, AMPKα, pAMPKα, pACC1 and ACC1 levels in 7701, HepG2 and MHCC97-H cells treated with lonafarnib. The corresponding quantitative data were obtained by standardization with GAPDH. Data are presented as the means of at least three independent experiments ± SD. * p < 0.05, ** p < 0.01, and *** p < 0.001.

    Techniques Used: Activation Assay, Sequencing, Western Blot, Expressing, Transfection, Concentration Assay

    pLamin A/C is an indicator of increased lipid synthesis. ( A ) Treatment with 25 mM glucose for 12 h promoted lamin A/C phosphorylation and FASN expression in 7701, HepG2 and MHCC97-H cells. Semiquantitative analyses of blots are displayed. ( B ) TG synthesis was quantified ( n = 3). ( C ) Lamin A/C phosphorylation was increased by 25 mM glucose in a time-dependent manner in 7701 and HepG2 cells. Gray values from blots are displayed. ( D ) The inhibition of AMPKα activation was shown in 7701, HepG2 or MHCC97-H cells treated with 25 mM glucose. Semiquantitative analyses of blots are displayed. ( E ) Person’s correlation analysis between pLamin A and FASN or pAMPKα-T172 is shown. Data are shown as the means of at least three independent experiments ± SD. * p < 0.05 and ** p < 0.01.
    Figure Legend Snippet: pLamin A/C is an indicator of increased lipid synthesis. ( A ) Treatment with 25 mM glucose for 12 h promoted lamin A/C phosphorylation and FASN expression in 7701, HepG2 and MHCC97-H cells. Semiquantitative analyses of blots are displayed. ( B ) TG synthesis was quantified ( n = 3). ( C ) Lamin A/C phosphorylation was increased by 25 mM glucose in a time-dependent manner in 7701 and HepG2 cells. Gray values from blots are displayed. ( D ) The inhibition of AMPKα activation was shown in 7701, HepG2 or MHCC97-H cells treated with 25 mM glucose. Semiquantitative analyses of blots are displayed. ( E ) Person’s correlation analysis between pLamin A and FASN or pAMPKα-T172 is shown. Data are shown as the means of at least three independent experiments ± SD. * p < 0.05 and ** p < 0.01.

    Techniques Used: Expressing, Inhibition, Activation Assay

    anti phospho ampk alpha t172 antibody  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc anti phospho ampk alpha t172 antibody
    LMNA deletion inhibits de novo fat synthesis through AMPKα phosphorylation. ( A ) The expression levels of AMPKα and its phosphorylated form in LMNA -KO 7701 cells are shown with the corresponding plot of the quantitative analysis ( n = 3) ( B ). ( C ) CO-/C IP assays were performed to assess the endogenous interaction between pLamin Aand <t>pAMPKα-T172</t> or between lamin A/C and pAMPKα-T172 in 7701 cells. IgG was used as a negative control, and the input was used to examine the levels of pAMPKα-T172 and lamin A/C. ( D ) An exogenous reverse pull-down experiment was performed in 7701 cell lines. 7701 cells were transiently transfected with the <t>AMPK</t> α-FLAG plasmid or control vector for 48 h. An anti-FLAG antibody was used to immunoprecipitate the cell lysates. ( E ) HEK293T cells were transiently cotransfected with the plasmid containing the LMNA cDNA and the AMPKα -N, -C and -F plasmid or control vector. An anti-FLAG antibody was used to immunoprecipitate the nuclear lysates. Data are presented as the means ± SD. ns , p > 0.05, * p < 0.05, ** p < 0.01, and *** p < 0.001.
    Anti Phospho Ampk Alpha T172 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho ampk alpha t172 antibody/product/Cell Signaling Technology Inc
    Average 98 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti phospho ampk alpha t172 antibody - by Bioz Stars, 2024-07
    98/100 stars

    Images

    1) Product Images from "Loss of Mature Lamin A/C Triggers a Shift in Intracellular Metabolic Homeostasis via AMPKα Activation"

    Article Title: Loss of Mature Lamin A/C Triggers a Shift in Intracellular Metabolic Homeostasis via AMPKα Activation

    Journal: Cells

    doi: 10.3390/cells11243988

    LMNA deletion inhibits de novo fat synthesis through AMPKα phosphorylation. ( A ) The expression levels of AMPKα and its phosphorylated form in LMNA -KO 7701 cells are shown with the corresponding plot of the quantitative analysis ( n = 3) ( B ). ( C ) CO-/C IP assays were performed to assess the endogenous interaction between pLamin Aand pAMPKα-T172 or between lamin A/C and pAMPKα-T172 in 7701 cells. IgG was used as a negative control, and the input was used to examine the levels of pAMPKα-T172 and lamin A/C. ( D ) An exogenous reverse pull-down experiment was performed in 7701 cell lines. 7701 cells were transiently transfected with the AMPK α-FLAG plasmid or control vector for 48 h. An anti-FLAG antibody was used to immunoprecipitate the cell lysates. ( E ) HEK293T cells were transiently cotransfected with the plasmid containing the LMNA cDNA and the AMPKα -N, -C and -F plasmid or control vector. An anti-FLAG antibody was used to immunoprecipitate the nuclear lysates. Data are presented as the means ± SD. ns , p > 0.05, * p < 0.05, ** p < 0.01, and *** p < 0.001.
    Figure Legend Snippet: LMNA deletion inhibits de novo fat synthesis through AMPKα phosphorylation. ( A ) The expression levels of AMPKα and its phosphorylated form in LMNA -KO 7701 cells are shown with the corresponding plot of the quantitative analysis ( n = 3) ( B ). ( C ) CO-/C IP assays were performed to assess the endogenous interaction between pLamin Aand pAMPKα-T172 or between lamin A/C and pAMPKα-T172 in 7701 cells. IgG was used as a negative control, and the input was used to examine the levels of pAMPKα-T172 and lamin A/C. ( D ) An exogenous reverse pull-down experiment was performed in 7701 cell lines. 7701 cells were transiently transfected with the AMPK α-FLAG plasmid or control vector for 48 h. An anti-FLAG antibody was used to immunoprecipitate the cell lysates. ( E ) HEK293T cells were transiently cotransfected with the plasmid containing the LMNA cDNA and the AMPKα -N, -C and -F plasmid or control vector. An anti-FLAG antibody was used to immunoprecipitate the nuclear lysates. Data are presented as the means ± SD. ns , p > 0.05, * p < 0.05, ** p < 0.01, and *** p < 0.001.

    Techniques Used: Expressing, Negative Control, Transfection, Plasmid Preparation

    Abnormalities in Lamin A/C function trigger AMPKα activation. ( A ) Mutations in the LMNA structure and sequence are shown: D203N is located in the rod domain and R482W, G465D, and T528R are located in the LTD. Western blotting was performed to detect changes in lamin A/C, pLamin A/C, AMPKα, and pAMPKα-T172 levels upon the rescue of lamin A/C expression via the transfection of the LMNC cDNA, LMNA-GFP cDNA and LMNA mutants, and the corresponding semiquantitative data obtained after GAPDH normalization are shown. ( B ) TG and lactate synthesis were quantified in the different transfected groups ( n = 3). ( C ) Western blotting was performed to assess concentration-dependent changes in lamin A/C, pLamin A/C, AMPKα, pAMPKα, pACC1 and ACC1 levels in 7701, HepG2 and MHCC97-H cells treated with lonafarnib. The corresponding quantitative data were obtained by standardization with GAPDH. Data are presented as the means of at least three independent experiments ± SD. * p < 0.05, ** p < 0.01, and *** p < 0.001.
    Figure Legend Snippet: Abnormalities in Lamin A/C function trigger AMPKα activation. ( A ) Mutations in the LMNA structure and sequence are shown: D203N is located in the rod domain and R482W, G465D, and T528R are located in the LTD. Western blotting was performed to detect changes in lamin A/C, pLamin A/C, AMPKα, and pAMPKα-T172 levels upon the rescue of lamin A/C expression via the transfection of the LMNC cDNA, LMNA-GFP cDNA and LMNA mutants, and the corresponding semiquantitative data obtained after GAPDH normalization are shown. ( B ) TG and lactate synthesis were quantified in the different transfected groups ( n = 3). ( C ) Western blotting was performed to assess concentration-dependent changes in lamin A/C, pLamin A/C, AMPKα, pAMPKα, pACC1 and ACC1 levels in 7701, HepG2 and MHCC97-H cells treated with lonafarnib. The corresponding quantitative data were obtained by standardization with GAPDH. Data are presented as the means of at least three independent experiments ± SD. * p < 0.05, ** p < 0.01, and *** p < 0.001.

    Techniques Used: Activation Assay, Sequencing, Western Blot, Expressing, Transfection, Concentration Assay

    pLamin A/C is an indicator of increased lipid synthesis. ( A ) Treatment with 25 mM glucose for 12 h promoted lamin A/C phosphorylation and FASN expression in 7701, HepG2 and MHCC97-H cells. Semiquantitative analyses of blots are displayed. ( B ) TG synthesis was quantified ( n = 3). ( C ) Lamin A/C phosphorylation was increased by 25 mM glucose in a time-dependent manner in 7701 and HepG2 cells. Gray values from blots are displayed. ( D ) The inhibition of AMPKα activation was shown in 7701, HepG2 or MHCC97-H cells treated with 25 mM glucose. Semiquantitative analyses of blots are displayed. ( E ) Person’s correlation analysis between pLamin A and FASN or pAMPKα-T172 is shown. Data are shown as the means of at least three independent experiments ± SD. * p < 0.05 and ** p < 0.01.
    Figure Legend Snippet: pLamin A/C is an indicator of increased lipid synthesis. ( A ) Treatment with 25 mM glucose for 12 h promoted lamin A/C phosphorylation and FASN expression in 7701, HepG2 and MHCC97-H cells. Semiquantitative analyses of blots are displayed. ( B ) TG synthesis was quantified ( n = 3). ( C ) Lamin A/C phosphorylation was increased by 25 mM glucose in a time-dependent manner in 7701 and HepG2 cells. Gray values from blots are displayed. ( D ) The inhibition of AMPKα activation was shown in 7701, HepG2 or MHCC97-H cells treated with 25 mM glucose. Semiquantitative analyses of blots are displayed. ( E ) Person’s correlation analysis between pLamin A and FASN or pAMPKα-T172 is shown. Data are shown as the means of at least three independent experiments ± SD. * p < 0.05 and ** p < 0.01.

    Techniques Used: Expressing, Inhibition, Activation Assay

    anti phospho t172 ampk alpha  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc anti phospho t172 ampk alpha
    Key resources table
    Anti Phospho T172 Ampk Alpha, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho t172 ampk alpha/product/Cell Signaling Technology Inc
    Average 98 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti phospho t172 ampk alpha - by Bioz Stars, 2024-07
    98/100 stars

    Images

    1) Product Images from "Mitochondrial complex I inhibitors suppress tumor growth through concomitant acidification of the intra- and extracellular environment"

    Article Title: Mitochondrial complex I inhibitors suppress tumor growth through concomitant acidification of the intra- and extracellular environment

    Journal: iScience

    doi: 10.1016/j.isci.2021.103497

    Key resources table
    Figure Legend Snippet: Key resources table

    Techniques Used: Recombinant, Synthesized, Staining, Isolation, Activity Assay, Lactate Assay, Software

    anti phospho ampk alpha t172  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc anti phospho ampk alpha t172
    . Effect of PCE on pathway targets for blood cells in the CS inhaled/PCE-treated SD rats. Cell extracts were prepared from blood cells of CS-inhaled/PCE-treated SD rats. The western blot analysis was performed using the cell extracts with anti-Foxo3a, p-Foxo3a (S413), <t>p-AMPK</t> <t>(T172),</t> MnSOD and actin antibodies. Four different western blot analysis results were scanned using A densitometer and the scanned results were plotted as bars. The vertical bars indicate the standard error of the mean for three different experiments. The control SD rats (control) were compared to CS-inhaled SD rats without PCE treatment (CS) (* P < 0.05, ** P < 0.01 and *** P < 0.001) and CS-inhaled/PCE-treated SD rats (CS + PCE) (# P < 0.05, ## P < 0.01 and ### P < 0.001).
    Anti Phospho Ampk Alpha T172, 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
    https://www.bioz.com/result/anti phospho ampk alpha t172/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti phospho ampk alpha t172 - by Bioz Stars, 2024-07
    95/100 stars

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    1) Product Images from "Purple corn extract (PCE) alleviates cigarette smoke (CS)-induced DNA damage in rodent blood cells by activation of AMPK/Foxo3a/MnSOD pathway"

    Article Title: Purple corn extract (PCE) alleviates cigarette smoke (CS)-induced DNA damage in rodent blood cells by activation of AMPK/Foxo3a/MnSOD pathway

    Journal: Animal Cells and Systems

    doi: 10.1080/19768354.2021.1883734

    . Effect of PCE on pathway targets for blood cells in the CS inhaled/PCE-treated SD rats. Cell extracts were prepared from blood cells of CS-inhaled/PCE-treated SD rats. The western blot analysis was performed using the cell extracts with anti-Foxo3a, p-Foxo3a (S413), p-AMPK (T172), MnSOD and actin antibodies. Four different western blot analysis results were scanned using A densitometer and the scanned results were plotted as bars. The vertical bars indicate the standard error of the mean for three different experiments. The control SD rats (control) were compared to CS-inhaled SD rats without PCE treatment (CS) (* P < 0.05, ** P < 0.01 and *** P < 0.001) and CS-inhaled/PCE-treated SD rats (CS + PCE) (# P < 0.05, ## P < 0.01 and ### P < 0.001).
    Figure Legend Snippet: . Effect of PCE on pathway targets for blood cells in the CS inhaled/PCE-treated SD rats. Cell extracts were prepared from blood cells of CS-inhaled/PCE-treated SD rats. The western blot analysis was performed using the cell extracts with anti-Foxo3a, p-Foxo3a (S413), p-AMPK (T172), MnSOD and actin antibodies. Four different western blot analysis results were scanned using A densitometer and the scanned results were plotted as bars. The vertical bars indicate the standard error of the mean for three different experiments. The control SD rats (control) were compared to CS-inhaled SD rats without PCE treatment (CS) (* P < 0.05, ** P < 0.01 and *** P < 0.001) and CS-inhaled/PCE-treated SD rats (CS + PCE) (# P < 0.05, ## P < 0.01 and ### P < 0.001).

    Techniques Used: Western Blot

    phospho ampk alpha t172  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc phospho ampk alpha t172
    Phospho Ampk Alpha T172, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho ampk alpha t172/product/Cell Signaling Technology Inc
    Average 98 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phospho ampk alpha t172 - by Bioz Stars, 2024-07
    98/100 stars

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    phospho ampk alpha t172  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc phospho ampk alpha t172
    Phospho Ampk Alpha T172, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho ampk alpha t172/product/Cell Signaling Technology Inc
    Average 98 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phospho ampk alpha t172 - by Bioz Stars, 2024-07
    98/100 stars

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    Cell Signaling Technology Inc anti phospho ampk alpha t172
    Anti Phospho Ampk Alpha T172, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho ampk alpha t172/product/Cell Signaling Technology Inc
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    Cell Signaling Technology Inc anti phospho ampk alpha t172 antibody
    Anti Phospho Ampk Alpha T172 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho ampk alpha t172 antibody/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
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    Cell Signaling Technology Inc anti phospho t172 ampk alpha
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    Anti Phospho T172 Ampk Alpha, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho t172 ampk alpha/product/Cell Signaling Technology Inc
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    Cell Signaling Technology Inc phospho ampk alpha t172
    Key resources table
    Phospho Ampk Alpha T172, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho ampk alpha t172/product/Cell Signaling Technology Inc
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    Key resources table

    Journal: iScience

    Article Title: Mitochondrial complex I inhibitors suppress tumor growth through concomitant acidification of the intra- and extracellular environment

    doi: 10.1016/j.isci.2021.103497

    Figure Lengend Snippet: Key resources table

    Article Snippet: Anti-phospho-(T172)-AMPK alpha , Cell signaling Technology , Cat#2535; RRID: AB_331250.

    Techniques: Recombinant, Synthesized, Staining, Isolation, Activity Assay, Lactate Assay, Software