phosphor akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphor akt
    Low expression of LINC00173 in DDP-resistant LUAD attributes to the negative regulation of c-Myc. a. Predicted c-Myc binding site in the promoter region of LINC00173. b. Transfection of c-Myc plasmids suppressed LINC00173 expression in A549 and PC9 cells. Student’s two-tailed t-test, ** P < 0.01; *** P < 0.001; **** P < 0.0001. c. ChIP assay and agarose gel electrophoresis verified the binding of c-Myc to LINC00173 promoter in A549 and A549-DDP cells. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. d. Luciferase reporter assay further validated c-Myc was directly binding to LINC00173 promoter. Student’s two-tailed t-test, * P < 0.05; ** P < 0.01; ns, no significance. e. Western blot analysis of PI3K, p-PI3K, <t>AKT,</t> p-AKT and c-Myc expression in A549 and A549-DDP cells. GAPDH was used as a loading control. f. Western blot detection of p-PI3K, p-AKT, c-Myc, PROCA1 <t>and</t> <t>ZFP36L2</t> expression in A549-DDP and PC9-DDP cells after treated with PI3K inhibitor LY294002. GAPDH was used as a loading control. g. The expression level of LINC00173 was obviously increased in A549-DDP and PC9-DDP cell lines after treated with LY294002. h. The IC 50 values to cisplatin were detected in A549 and PC9 cells transfected with a gradient concentration of c-Myc plasmids. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. Error bars, mean ± SD
    Phosphor Akt, supplied by Cell Signaling Technology Inc, 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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    1) Product Images from "Downregulation of Linc00173 increases BCL2 mRNA stability via the miR-1275/PROCA1/ZFP36L2 axis and induces acquired cisplatin resistance of lung adenocarcinoma"

    Article Title: Downregulation of Linc00173 increases BCL2 mRNA stability via the miR-1275/PROCA1/ZFP36L2 axis and induces acquired cisplatin resistance of lung adenocarcinoma

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    doi: 10.1186/s13046-022-02560-6

    Low expression of LINC00173 in DDP-resistant LUAD attributes to the negative regulation of c-Myc. a. Predicted c-Myc binding site in the promoter region of LINC00173. b. Transfection of c-Myc plasmids suppressed LINC00173 expression in A549 and PC9 cells. Student’s two-tailed t-test, ** P < 0.01; *** P < 0.001; **** P < 0.0001. c. ChIP assay and agarose gel electrophoresis verified the binding of c-Myc to LINC00173 promoter in A549 and A549-DDP cells. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. d. Luciferase reporter assay further validated c-Myc was directly binding to LINC00173 promoter. Student’s two-tailed t-test, * P < 0.05; ** P < 0.01; ns, no significance. e. Western blot analysis of PI3K, p-PI3K, AKT, p-AKT and c-Myc expression in A549 and A549-DDP cells. GAPDH was used as a loading control. f. Western blot detection of p-PI3K, p-AKT, c-Myc, PROCA1 and ZFP36L2 expression in A549-DDP and PC9-DDP cells after treated with PI3K inhibitor LY294002. GAPDH was used as a loading control. g. The expression level of LINC00173 was obviously increased in A549-DDP and PC9-DDP cell lines after treated with LY294002. h. The IC 50 values to cisplatin were detected in A549 and PC9 cells transfected with a gradient concentration of c-Myc plasmids. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. Error bars, mean ± SD
    Figure Legend Snippet: Low expression of LINC00173 in DDP-resistant LUAD attributes to the negative regulation of c-Myc. a. Predicted c-Myc binding site in the promoter region of LINC00173. b. Transfection of c-Myc plasmids suppressed LINC00173 expression in A549 and PC9 cells. Student’s two-tailed t-test, ** P < 0.01; *** P < 0.001; **** P < 0.0001. c. ChIP assay and agarose gel electrophoresis verified the binding of c-Myc to LINC00173 promoter in A549 and A549-DDP cells. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. d. Luciferase reporter assay further validated c-Myc was directly binding to LINC00173 promoter. Student’s two-tailed t-test, * P < 0.05; ** P < 0.01; ns, no significance. e. Western blot analysis of PI3K, p-PI3K, AKT, p-AKT and c-Myc expression in A549 and A549-DDP cells. GAPDH was used as a loading control. f. Western blot detection of p-PI3K, p-AKT, c-Myc, PROCA1 and ZFP36L2 expression in A549-DDP and PC9-DDP cells after treated with PI3K inhibitor LY294002. GAPDH was used as a loading control. g. The expression level of LINC00173 was obviously increased in A549-DDP and PC9-DDP cell lines after treated with LY294002. h. The IC 50 values to cisplatin were detected in A549 and PC9 cells transfected with a gradient concentration of c-Myc plasmids. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. Error bars, mean ± SD

    Techniques Used: Expressing, Binding Assay, Transfection, Two Tailed Test, Agarose Gel Electrophoresis, Luciferase, Reporter Assay, Western Blot, Concentration Assay

    phosphor akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphor akt
    Phosphor Akt, 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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    phosphor akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphor akt
    Phosphor Akt, 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 phosphor akt ser473  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phosphor akt ser473
    Anti Phosphor Akt Ser473, 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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    phosphor akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphor akt
    Preferential direct binding of Aurora kinase A (AurA) to the C-terminus of E6-encoded by HPV16. (A) (i). Schematic diagram shows the basic structure of cancer-causing HPV16E6 and potential amino acids recognized by Aurora kinase A (AurA). E6 contains two major functional domains: two zinc (Zn) finger binding domains, the regions where E6 forms complex with E6AP and p53; and the unique dual-functional PDZ binding motif (PBM) at its extreme C-terminal end, the region where E6 binds to PDZ proteins [Disc large protein-1 (Dlg-1), membrane-associated guanylated kinase inverted (MAGI) protein and Scribble)], and which is also a target for <t>PKA/AKT</t> phosphorylation. (ii). The right panel shows the AurA recognition motif [R/K/N]-R-X 0-2 -X-[S/T]-ϕ. Also shown are the key amino acids within E6-encoded by HPV16, 18 and 58, and E7-encoded by HPV18 predicted using Scansite that can be recognized by AurA: HPV16E6 at residues S89, T140, S145 and S150 of HPV16E6; HPV18E6 at residue S59; HPV58 at residues S82 and T133; HPV18E7 at residue T60. (B) (i). An in vitro binding assay was performed by incubating the indicated purified GST fusion proteins with in vitro -translated Aurora kinase A (AurA). After extensive washing, the bound AurA protein was detected via Western blotting using an HA-specific antibody. The immunoblot (IB) on the upper panel shows the interaction of AurA with GST-16 E6 and E7, while the lower panel shows the Ponceau S stained of the blot. (ii). The bar graph shows the quantitation of the relative level of AurA bound to GST fusion proteins indicated from 3 independent experiments ( n = 3). Quantitation was performed using ImageJ software and statistical analysis was performed using Prism. C (i). A similar in vitro binding assay was performed, in which in vitro -translated HA-AurA protein was incubated with purified GST-tagged HPV-11E6 (GST-11E6), -16E6 (GST-16E6), -18E6 (GST-18E6), -58E6 (GST-58E6) and 16E6ΔPBM (GST-16 E6ΔPBM) as indicated. The immunoblot (IB) on the upper panel shows the interaction of AurA with GST-tagged fusion proteins, while the lower panel shows the Ponceau S stained of the blot. (ii). The bar graph shows the binding affinity of AurA to GST-E6 fusion proteins relative to GST-16E6 wild type. The intensities of the bands were analyzed using ImageJ ( n = 3). All data are presented as means ± standard error of the mean (SEM). ( * , P < 0.05, *** * , P < 0.0001). D (i). An in vitro binding assay was performed, in which in vitro -translated HA-AurA protein was incubated with purified GST-tagged HPV16E6 wild types (GST-16E6) and mutants (T140A, S145A, S150A, and S89A), as indicated. After extensive washing, the protein complexes were subjected to Western blotting. The upper panel showed the immunoblot (IB) incubated with HA-specific antibody to detect the expression level of AurA, while the lower panel showed the Ponceau S stain of the blot. (ii). The bar graph shows the binding affinity of AurA to GST-E6 mutants relative to GST-16E6 wild type. The intensities of the bands were analyzed using ImageJ ( n = 3). All data are presented as means ± standard error of the mean (SEM). ( * , P < 0.05; ** * , P < 0.001; *** * , P < 0.0001).
    Phosphor Akt, 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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    1) Product Images from "E6-Encoded by Cancer-Causing Human Papillomavirus Interacts with Aurora Kinase A To Promote HPV-Mediated Carcinogenesis"

    Article Title: E6-Encoded by Cancer-Causing Human Papillomavirus Interacts with Aurora Kinase A To Promote HPV-Mediated Carcinogenesis

    Journal: Journal of Virology

    doi: 10.1128/jvi.01872-22

    Preferential direct binding of Aurora kinase A (AurA) to the C-terminus of E6-encoded by HPV16. (A) (i). Schematic diagram shows the basic structure of cancer-causing HPV16E6 and potential amino acids recognized by Aurora kinase A (AurA). E6 contains two major functional domains: two zinc (Zn) finger binding domains, the regions where E6 forms complex with E6AP and p53; and the unique dual-functional PDZ binding motif (PBM) at its extreme C-terminal end, the region where E6 binds to PDZ proteins [Disc large protein-1 (Dlg-1), membrane-associated guanylated kinase inverted (MAGI) protein and Scribble)], and which is also a target for PKA/AKT phosphorylation. (ii). The right panel shows the AurA recognition motif [R/K/N]-R-X 0-2 -X-[S/T]-ϕ. Also shown are the key amino acids within E6-encoded by HPV16, 18 and 58, and E7-encoded by HPV18 predicted using Scansite that can be recognized by AurA: HPV16E6 at residues S89, T140, S145 and S150 of HPV16E6; HPV18E6 at residue S59; HPV58 at residues S82 and T133; HPV18E7 at residue T60. (B) (i). An in vitro binding assay was performed by incubating the indicated purified GST fusion proteins with in vitro -translated Aurora kinase A (AurA). After extensive washing, the bound AurA protein was detected via Western blotting using an HA-specific antibody. The immunoblot (IB) on the upper panel shows the interaction of AurA with GST-16 E6 and E7, while the lower panel shows the Ponceau S stained of the blot. (ii). The bar graph shows the quantitation of the relative level of AurA bound to GST fusion proteins indicated from 3 independent experiments ( n = 3). Quantitation was performed using ImageJ software and statistical analysis was performed using Prism. C (i). A similar in vitro binding assay was performed, in which in vitro -translated HA-AurA protein was incubated with purified GST-tagged HPV-11E6 (GST-11E6), -16E6 (GST-16E6), -18E6 (GST-18E6), -58E6 (GST-58E6) and 16E6ΔPBM (GST-16 E6ΔPBM) as indicated. The immunoblot (IB) on the upper panel shows the interaction of AurA with GST-tagged fusion proteins, while the lower panel shows the Ponceau S stained of the blot. (ii). The bar graph shows the binding affinity of AurA to GST-E6 fusion proteins relative to GST-16E6 wild type. The intensities of the bands were analyzed using ImageJ ( n = 3). All data are presented as means ± standard error of the mean (SEM). ( * , P < 0.05, *** * , P < 0.0001). D (i). An in vitro binding assay was performed, in which in vitro -translated HA-AurA protein was incubated with purified GST-tagged HPV16E6 wild types (GST-16E6) and mutants (T140A, S145A, S150A, and S89A), as indicated. After extensive washing, the protein complexes were subjected to Western blotting. The upper panel showed the immunoblot (IB) incubated with HA-specific antibody to detect the expression level of AurA, while the lower panel showed the Ponceau S stain of the blot. (ii). The bar graph shows the binding affinity of AurA to GST-E6 mutants relative to GST-16E6 wild type. The intensities of the bands were analyzed using ImageJ ( n = 3). All data are presented as means ± standard error of the mean (SEM). ( * , P < 0.05; ** * , P < 0.001; *** * , P < 0.0001).
    Figure Legend Snippet: Preferential direct binding of Aurora kinase A (AurA) to the C-terminus of E6-encoded by HPV16. (A) (i). Schematic diagram shows the basic structure of cancer-causing HPV16E6 and potential amino acids recognized by Aurora kinase A (AurA). E6 contains two major functional domains: two zinc (Zn) finger binding domains, the regions where E6 forms complex with E6AP and p53; and the unique dual-functional PDZ binding motif (PBM) at its extreme C-terminal end, the region where E6 binds to PDZ proteins [Disc large protein-1 (Dlg-1), membrane-associated guanylated kinase inverted (MAGI) protein and Scribble)], and which is also a target for PKA/AKT phosphorylation. (ii). The right panel shows the AurA recognition motif [R/K/N]-R-X 0-2 -X-[S/T]-ϕ. Also shown are the key amino acids within E6-encoded by HPV16, 18 and 58, and E7-encoded by HPV18 predicted using Scansite that can be recognized by AurA: HPV16E6 at residues S89, T140, S145 and S150 of HPV16E6; HPV18E6 at residue S59; HPV58 at residues S82 and T133; HPV18E7 at residue T60. (B) (i). An in vitro binding assay was performed by incubating the indicated purified GST fusion proteins with in vitro -translated Aurora kinase A (AurA). After extensive washing, the bound AurA protein was detected via Western blotting using an HA-specific antibody. The immunoblot (IB) on the upper panel shows the interaction of AurA with GST-16 E6 and E7, while the lower panel shows the Ponceau S stained of the blot. (ii). The bar graph shows the quantitation of the relative level of AurA bound to GST fusion proteins indicated from 3 independent experiments ( n = 3). Quantitation was performed using ImageJ software and statistical analysis was performed using Prism. C (i). A similar in vitro binding assay was performed, in which in vitro -translated HA-AurA protein was incubated with purified GST-tagged HPV-11E6 (GST-11E6), -16E6 (GST-16E6), -18E6 (GST-18E6), -58E6 (GST-58E6) and 16E6ΔPBM (GST-16 E6ΔPBM) as indicated. The immunoblot (IB) on the upper panel shows the interaction of AurA with GST-tagged fusion proteins, while the lower panel shows the Ponceau S stained of the blot. (ii). The bar graph shows the binding affinity of AurA to GST-E6 fusion proteins relative to GST-16E6 wild type. The intensities of the bands were analyzed using ImageJ ( n = 3). All data are presented as means ± standard error of the mean (SEM). ( * , P < 0.05, *** * , P < 0.0001). D (i). An in vitro binding assay was performed, in which in vitro -translated HA-AurA protein was incubated with purified GST-tagged HPV16E6 wild types (GST-16E6) and mutants (T140A, S145A, S150A, and S89A), as indicated. After extensive washing, the protein complexes were subjected to Western blotting. The upper panel showed the immunoblot (IB) incubated with HA-specific antibody to detect the expression level of AurA, while the lower panel showed the Ponceau S stain of the blot. (ii). The bar graph shows the binding affinity of AurA to GST-E6 mutants relative to GST-16E6 wild type. The intensities of the bands were analyzed using ImageJ ( n = 3). All data are presented as means ± standard error of the mean (SEM). ( * , P < 0.05; ** * , P < 0.001; *** * , P < 0.0001).

    Techniques Used: Binding Assay, Functional Assay, In Vitro, Purification, Western Blot, Staining, Quantitation Assay, Software, Incubation, Expressing

    The association between AurA and E6 perturbs host cellular events. (A) (i). CaSki cells were transfected with short interference RNA (siRNA) against AurA or control (siCtrl) for 72 h. The protein extracts were subjected to Western blotting for the detection phosphorylated/acetylated-Histone H3 (p-Ac-H3), Histone H3 (H3), phosphor-ERK1/2 (pERK1/2), total ERK1/2, phosphor-AKT (pAKT), AKT, p53, AurA, metalloprotease protein 2 (MMP2), vimentin, cyclin E, cyclin B and beta (β)-actin specific antibodies. (ii). The relative expression levels of the cellular proteins relative to CaSki cells transfected with siCtrl were analyzed using ImageJ and GraphPad Prism ( n = 3). (B) (i). The C33A cells were transfected mock-transfected (NC) or transfected with pcDNA3.1:HA-AurA (AurA) or/and pGW1: HA-16E6 (E6) plasmids. After 24 h, the total protein extracts were collected and subjected to Western blotting. The immunoblots were incubated with antibodies specific for phosphorylated/acetylated-Histone H3 (p-Ac-H3), Histone H3 (H3), phosphor-ERK1/2 (pERK1/2), total ERK1/2, phosphor-AKT (pAKT), AKT, HA (16E6), AurA, metalloprotease protein 2 (MMP2), vimentin, cyclin E, cyclin B and β-actin antibodies. (ii). The bar graph shows the expression levels of the proteins indicated relative to the mock-transfected group. The intensities of the bands were analyzed using ImageJ and GraphPad Prism ( n = 3). All data were presented as means ± standard error of the mean (SEM). ( * , P < 0.05; * * , P < 0.01).
    Figure Legend Snippet: The association between AurA and E6 perturbs host cellular events. (A) (i). CaSki cells were transfected with short interference RNA (siRNA) against AurA or control (siCtrl) for 72 h. The protein extracts were subjected to Western blotting for the detection phosphorylated/acetylated-Histone H3 (p-Ac-H3), Histone H3 (H3), phosphor-ERK1/2 (pERK1/2), total ERK1/2, phosphor-AKT (pAKT), AKT, p53, AurA, metalloprotease protein 2 (MMP2), vimentin, cyclin E, cyclin B and beta (β)-actin specific antibodies. (ii). The relative expression levels of the cellular proteins relative to CaSki cells transfected with siCtrl were analyzed using ImageJ and GraphPad Prism ( n = 3). (B) (i). The C33A cells were transfected mock-transfected (NC) or transfected with pcDNA3.1:HA-AurA (AurA) or/and pGW1: HA-16E6 (E6) plasmids. After 24 h, the total protein extracts were collected and subjected to Western blotting. The immunoblots were incubated with antibodies specific for phosphorylated/acetylated-Histone H3 (p-Ac-H3), Histone H3 (H3), phosphor-ERK1/2 (pERK1/2), total ERK1/2, phosphor-AKT (pAKT), AKT, HA (16E6), AurA, metalloprotease protein 2 (MMP2), vimentin, cyclin E, cyclin B and β-actin antibodies. (ii). The bar graph shows the expression levels of the proteins indicated relative to the mock-transfected group. The intensities of the bands were analyzed using ImageJ and GraphPad Prism ( n = 3). All data were presented as means ± standard error of the mean (SEM). ( * , P < 0.05; * * , P < 0.01).

    Techniques Used: Transfection, Western Blot, Expressing, Incubation

    phosphor akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphor akt
    Low expression of LINC00173 in DDP-resistant LUAD attributes to the negative regulation of c-Myc. a. Predicted c-Myc binding site in the promoter region of LINC00173. b. Transfection of c-Myc plasmids suppressed LINC00173 expression in A549 and PC9 cells. Student’s two-tailed t-test, ** P < 0.01; *** P < 0.001; **** P < 0.0001. c. ChIP assay and agarose gel electrophoresis verified the binding of c-Myc to LINC00173 promoter in A549 and A549-DDP cells. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. d. Luciferase reporter assay further validated c-Myc was directly binding to LINC00173 promoter. Student’s two-tailed t-test, * P < 0.05; ** P < 0.01; ns, no significance. e. Western blot analysis of PI3K, p-PI3K, <t>AKT,</t> p-AKT and c-Myc expression in A549 and A549-DDP cells. GAPDH was used as a loading control. f. Western blot detection of p-PI3K, p-AKT, c-Myc, PROCA1 <t>and</t> <t>ZFP36L2</t> expression in A549-DDP and PC9-DDP cells after treated with PI3K inhibitor LY294002. GAPDH was used as a loading control. g. The expression level of LINC00173 was obviously increased in A549-DDP and PC9-DDP cell lines after treated with LY294002. h. The IC 50 values to cisplatin were detected in A549 and PC9 cells transfected with a gradient concentration of c-Myc plasmids. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. Error bars, mean ± SD
    Phosphor Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phosphor akt/product/Cell Signaling Technology Inc
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phosphor akt - by Bioz Stars, 2023-03
    97/100 stars

    Images

    1) Product Images from "Downregulation of Linc00173 increases BCL2 mRNA stability via the miR-1275/PROCA1/ZFP36L2 axis and induces acquired cisplatin resistance of lung adenocarcinoma"

    Article Title: Downregulation of Linc00173 increases BCL2 mRNA stability via the miR-1275/PROCA1/ZFP36L2 axis and induces acquired cisplatin resistance of lung adenocarcinoma

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    doi: 10.1186/s13046-022-02560-6

    Low expression of LINC00173 in DDP-resistant LUAD attributes to the negative regulation of c-Myc. a. Predicted c-Myc binding site in the promoter region of LINC00173. b. Transfection of c-Myc plasmids suppressed LINC00173 expression in A549 and PC9 cells. Student’s two-tailed t-test, ** P < 0.01; *** P < 0.001; **** P < 0.0001. c. ChIP assay and agarose gel electrophoresis verified the binding of c-Myc to LINC00173 promoter in A549 and A549-DDP cells. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. d. Luciferase reporter assay further validated c-Myc was directly binding to LINC00173 promoter. Student’s two-tailed t-test, * P < 0.05; ** P < 0.01; ns, no significance. e. Western blot analysis of PI3K, p-PI3K, AKT, p-AKT and c-Myc expression in A549 and A549-DDP cells. GAPDH was used as a loading control. f. Western blot detection of p-PI3K, p-AKT, c-Myc, PROCA1 and ZFP36L2 expression in A549-DDP and PC9-DDP cells after treated with PI3K inhibitor LY294002. GAPDH was used as a loading control. g. The expression level of LINC00173 was obviously increased in A549-DDP and PC9-DDP cell lines after treated with LY294002. h. The IC 50 values to cisplatin were detected in A549 and PC9 cells transfected with a gradient concentration of c-Myc plasmids. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. Error bars, mean ± SD
    Figure Legend Snippet: Low expression of LINC00173 in DDP-resistant LUAD attributes to the negative regulation of c-Myc. a. Predicted c-Myc binding site in the promoter region of LINC00173. b. Transfection of c-Myc plasmids suppressed LINC00173 expression in A549 and PC9 cells. Student’s two-tailed t-test, ** P < 0.01; *** P < 0.001; **** P < 0.0001. c. ChIP assay and agarose gel electrophoresis verified the binding of c-Myc to LINC00173 promoter in A549 and A549-DDP cells. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. d. Luciferase reporter assay further validated c-Myc was directly binding to LINC00173 promoter. Student’s two-tailed t-test, * P < 0.05; ** P < 0.01; ns, no significance. e. Western blot analysis of PI3K, p-PI3K, AKT, p-AKT and c-Myc expression in A549 and A549-DDP cells. GAPDH was used as a loading control. f. Western blot detection of p-PI3K, p-AKT, c-Myc, PROCA1 and ZFP36L2 expression in A549-DDP and PC9-DDP cells after treated with PI3K inhibitor LY294002. GAPDH was used as a loading control. g. The expression level of LINC00173 was obviously increased in A549-DDP and PC9-DDP cell lines after treated with LY294002. h. The IC 50 values to cisplatin were detected in A549 and PC9 cells transfected with a gradient concentration of c-Myc plasmids. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. Error bars, mean ± SD

    Techniques Used: Expressing, Binding Assay, Transfection, Two Tailed Test, Agarose Gel Electrophoresis, Luciferase, Reporter Assay, Western Blot, Concentration Assay

    phosphor akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphor akt
    NRG-1β increased glucose uptake in PA-treated C2C12 myotubes by activating the <t>PI3K/AKT</t> signaling pathway. Effects of NRG-1β on levels of AKT <t>and</t> <t>Phosphor-Akt</t> (ser 473) in PA-treated (plus insulin) C2C12 myotubes were detected via Western blotting (A,B) . Dimethyl sulphoxide (DMSO) or 10 μM MK2206 (an AKT inhibitor) in DMSO was added before culturing .25 mM PA-treated (plus insulin) C2C12 myotubes, effects of MK2206 on glucose uptake using the 2-NBDG assay (C) . The data are presented as the mean ± SEM. * p < .05; ** p < .01; **** p < .0001.
    Phosphor Akt, 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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    Average 86 stars, based on 1 article reviews
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    1) Product Images from "Neuregulin-1β increases glucose uptake and promotes GLUT4 translocation in palmitate-treated C2C12 myotubes by activating PI3K/AKT signaling pathway"

    Article Title: Neuregulin-1β increases glucose uptake and promotes GLUT4 translocation in palmitate-treated C2C12 myotubes by activating PI3K/AKT signaling pathway

    Journal: Frontiers in Pharmacology

    doi: 10.3389/fphar.2022.1066279

    NRG-1β increased glucose uptake in PA-treated C2C12 myotubes by activating the PI3K/AKT signaling pathway. Effects of NRG-1β on levels of AKT and Phosphor-Akt (ser 473) in PA-treated (plus insulin) C2C12 myotubes were detected via Western blotting (A,B) . Dimethyl sulphoxide (DMSO) or 10 μM MK2206 (an AKT inhibitor) in DMSO was added before culturing .25 mM PA-treated (plus insulin) C2C12 myotubes, effects of MK2206 on glucose uptake using the 2-NBDG assay (C) . The data are presented as the mean ± SEM. * p < .05; ** p < .01; **** p < .0001.
    Figure Legend Snippet: NRG-1β increased glucose uptake in PA-treated C2C12 myotubes by activating the PI3K/AKT signaling pathway. Effects of NRG-1β on levels of AKT and Phosphor-Akt (ser 473) in PA-treated (plus insulin) C2C12 myotubes were detected via Western blotting (A,B) . Dimethyl sulphoxide (DMSO) or 10 μM MK2206 (an AKT inhibitor) in DMSO was added before culturing .25 mM PA-treated (plus insulin) C2C12 myotubes, effects of MK2206 on glucose uptake using the 2-NBDG assay (C) . The data are presented as the mean ± SEM. * p < .05; ** p < .01; **** p < .0001.

    Techniques Used: Western Blot

    rabbit monoclonal antibody against phospho akt phosphor ser473  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit monoclonal antibody against phospho akt phosphor ser473
    Rabbit Monoclonal Antibody Against Phospho Akt Phosphor Ser473, 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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    phosphor akt ser473  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphor akt ser473
    Phosphor Akt Ser473, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phosphor akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphor akt
    Phosphor Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phosphor thr308  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphor akt
    Low expression of LINC00173 in DDP-resistant LUAD attributes to the negative regulation of c-Myc. a. Predicted c-Myc binding site in the promoter region of LINC00173. b. Transfection of c-Myc plasmids suppressed LINC00173 expression in A549 and PC9 cells. Student’s two-tailed t-test, ** P < 0.01; *** P < 0.001; **** P < 0.0001. c. ChIP assay and agarose gel electrophoresis verified the binding of c-Myc to LINC00173 promoter in A549 and A549-DDP cells. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. d. Luciferase reporter assay further validated c-Myc was directly binding to LINC00173 promoter. Student’s two-tailed t-test, * P < 0.05; ** P < 0.01; ns, no significance. e. Western blot analysis of PI3K, p-PI3K, <t>AKT,</t> p-AKT and c-Myc expression in A549 and A549-DDP cells. GAPDH was used as a loading control. f. Western blot detection of p-PI3K, p-AKT, c-Myc, PROCA1 <t>and</t> <t>ZFP36L2</t> expression in A549-DDP and PC9-DDP cells after treated with PI3K inhibitor LY294002. GAPDH was used as a loading control. g. The expression level of LINC00173 was obviously increased in A549-DDP and PC9-DDP cell lines after treated with LY294002. h. The IC 50 values to cisplatin were detected in A549 and PC9 cells transfected with a gradient concentration of c-Myc plasmids. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. Error bars, mean ± SD
    Phosphor Akt, supplied by Cell Signaling Technology Inc, 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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    anti phosphor akt ser473  (Cell Signaling Technology Inc)
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    Low expression of LINC00173 in DDP-resistant LUAD attributes to the negative regulation of c-Myc. a. Predicted c-Myc binding site in the promoter region of LINC00173. b. Transfection of c-Myc plasmids suppressed LINC00173 expression in A549 and PC9 cells. Student’s two-tailed t-test, ** P < 0.01; *** P < 0.001; **** P < 0.0001. c. ChIP assay and agarose gel electrophoresis verified the binding of c-Myc to LINC00173 promoter in A549 and A549-DDP cells. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. d. Luciferase reporter assay further validated c-Myc was directly binding to LINC00173 promoter. Student’s two-tailed t-test, * P < 0.05; ** P < 0.01; ns, no significance. e. Western blot analysis of PI3K, p-PI3K, <t>AKT,</t> p-AKT and c-Myc expression in A549 and A549-DDP cells. GAPDH was used as a loading control. f. Western blot detection of p-PI3K, p-AKT, c-Myc, PROCA1 <t>and</t> <t>ZFP36L2</t> expression in A549-DDP and PC9-DDP cells after treated with PI3K inhibitor LY294002. GAPDH was used as a loading control. g. The expression level of LINC00173 was obviously increased in A549-DDP and PC9-DDP cell lines after treated with LY294002. h. The IC 50 values to cisplatin were detected in A549 and PC9 cells transfected with a gradient concentration of c-Myc plasmids. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. Error bars, mean ± SD
    Anti Phosphor Akt Ser473, 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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    rabbit monoclonal antibody against phospho akt phosphor ser473  (Cell Signaling Technology Inc)
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    Low expression of LINC00173 in DDP-resistant LUAD attributes to the negative regulation of c-Myc. a. Predicted c-Myc binding site in the promoter region of LINC00173. b. Transfection of c-Myc plasmids suppressed LINC00173 expression in A549 and PC9 cells. Student’s two-tailed t-test, ** P < 0.01; *** P < 0.001; **** P < 0.0001. c. ChIP assay and agarose gel electrophoresis verified the binding of c-Myc to LINC00173 promoter in A549 and A549-DDP cells. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. d. Luciferase reporter assay further validated c-Myc was directly binding to LINC00173 promoter. Student’s two-tailed t-test, * P < 0.05; ** P < 0.01; ns, no significance. e. Western blot analysis of PI3K, p-PI3K, <t>AKT,</t> p-AKT and c-Myc expression in A549 and A549-DDP cells. GAPDH was used as a loading control. f. Western blot detection of p-PI3K, p-AKT, c-Myc, PROCA1 <t>and</t> <t>ZFP36L2</t> expression in A549-DDP and PC9-DDP cells after treated with PI3K inhibitor LY294002. GAPDH was used as a loading control. g. The expression level of LINC00173 was obviously increased in A549-DDP and PC9-DDP cell lines after treated with LY294002. h. The IC 50 values to cisplatin were detected in A549 and PC9 cells transfected with a gradient concentration of c-Myc plasmids. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. Error bars, mean ± SD
    Rabbit Monoclonal Antibody Against Phospho Akt Phosphor Ser473, 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/rabbit monoclonal antibody against phospho akt phosphor ser473/product/Cell Signaling Technology Inc
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    phosphor akt ser473  (Cell Signaling Technology Inc)
    96
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    Low expression of LINC00173 in DDP-resistant LUAD attributes to the negative regulation of c-Myc. a. Predicted c-Myc binding site in the promoter region of LINC00173. b. Transfection of c-Myc plasmids suppressed LINC00173 expression in A549 and PC9 cells. Student’s two-tailed t-test, ** P < 0.01; *** P < 0.001; **** P < 0.0001. c. ChIP assay and agarose gel electrophoresis verified the binding of c-Myc to LINC00173 promoter in A549 and A549-DDP cells. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. d. Luciferase reporter assay further validated c-Myc was directly binding to LINC00173 promoter. Student’s two-tailed t-test, * P < 0.05; ** P < 0.01; ns, no significance. e. Western blot analysis of PI3K, p-PI3K, <t>AKT,</t> p-AKT and c-Myc expression in A549 and A549-DDP cells. GAPDH was used as a loading control. f. Western blot detection of p-PI3K, p-AKT, c-Myc, PROCA1 <t>and</t> <t>ZFP36L2</t> expression in A549-DDP and PC9-DDP cells after treated with PI3K inhibitor LY294002. GAPDH was used as a loading control. g. The expression level of LINC00173 was obviously increased in A549-DDP and PC9-DDP cell lines after treated with LY294002. h. The IC 50 values to cisplatin were detected in A549 and PC9 cells transfected with a gradient concentration of c-Myc plasmids. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. Error bars, mean ± SD
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    phosphor thr308  (Cell Signaling Technology Inc)
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    Cell Signaling Technology Inc phosphor thr308
    Low expression of LINC00173 in DDP-resistant LUAD attributes to the negative regulation of c-Myc. a. Predicted c-Myc binding site in the promoter region of LINC00173. b. Transfection of c-Myc plasmids suppressed LINC00173 expression in A549 and PC9 cells. Student’s two-tailed t-test, ** P < 0.01; *** P < 0.001; **** P < 0.0001. c. ChIP assay and agarose gel electrophoresis verified the binding of c-Myc to LINC00173 promoter in A549 and A549-DDP cells. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. d. Luciferase reporter assay further validated c-Myc was directly binding to LINC00173 promoter. Student’s two-tailed t-test, * P < 0.05; ** P < 0.01; ns, no significance. e. Western blot analysis of PI3K, p-PI3K, <t>AKT,</t> p-AKT and c-Myc expression in A549 and A549-DDP cells. GAPDH was used as a loading control. f. Western blot detection of p-PI3K, p-AKT, c-Myc, PROCA1 <t>and</t> <t>ZFP36L2</t> expression in A549-DDP and PC9-DDP cells after treated with PI3K inhibitor LY294002. GAPDH was used as a loading control. g. The expression level of LINC00173 was obviously increased in A549-DDP and PC9-DDP cell lines after treated with LY294002. h. The IC 50 values to cisplatin were detected in A549 and PC9 cells transfected with a gradient concentration of c-Myc plasmids. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. Error bars, mean ± SD
    Phosphor Thr308, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Low expression of LINC00173 in DDP-resistant LUAD attributes to the negative regulation of c-Myc. a. Predicted c-Myc binding site in the promoter region of LINC00173. b. Transfection of c-Myc plasmids suppressed LINC00173 expression in A549 and PC9 cells. Student’s two-tailed t-test, ** P < 0.01; *** P < 0.001; **** P < 0.0001. c. ChIP assay and agarose gel electrophoresis verified the binding of c-Myc to LINC00173 promoter in A549 and A549-DDP cells. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. d. Luciferase reporter assay further validated c-Myc was directly binding to LINC00173 promoter. Student’s two-tailed t-test, * P < 0.05; ** P < 0.01; ns, no significance. e. Western blot analysis of PI3K, p-PI3K, AKT, p-AKT and c-Myc expression in A549 and A549-DDP cells. GAPDH was used as a loading control. f. Western blot detection of p-PI3K, p-AKT, c-Myc, PROCA1 and ZFP36L2 expression in A549-DDP and PC9-DDP cells after treated with PI3K inhibitor LY294002. GAPDH was used as a loading control. g. The expression level of LINC00173 was obviously increased in A549-DDP and PC9-DDP cell lines after treated with LY294002. h. The IC 50 values to cisplatin were detected in A549 and PC9 cells transfected with a gradient concentration of c-Myc plasmids. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. Error bars, mean ± SD

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Downregulation of Linc00173 increases BCL2 mRNA stability via the miR-1275/PROCA1/ZFP36L2 axis and induces acquired cisplatin resistance of lung adenocarcinoma

    doi: 10.1186/s13046-022-02560-6

    Figure Lengend Snippet: Low expression of LINC00173 in DDP-resistant LUAD attributes to the negative regulation of c-Myc. a. Predicted c-Myc binding site in the promoter region of LINC00173. b. Transfection of c-Myc plasmids suppressed LINC00173 expression in A549 and PC9 cells. Student’s two-tailed t-test, ** P < 0.01; *** P < 0.001; **** P < 0.0001. c. ChIP assay and agarose gel electrophoresis verified the binding of c-Myc to LINC00173 promoter in A549 and A549-DDP cells. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. d. Luciferase reporter assay further validated c-Myc was directly binding to LINC00173 promoter. Student’s two-tailed t-test, * P < 0.05; ** P < 0.01; ns, no significance. e. Western blot analysis of PI3K, p-PI3K, AKT, p-AKT and c-Myc expression in A549 and A549-DDP cells. GAPDH was used as a loading control. f. Western blot detection of p-PI3K, p-AKT, c-Myc, PROCA1 and ZFP36L2 expression in A549-DDP and PC9-DDP cells after treated with PI3K inhibitor LY294002. GAPDH was used as a loading control. g. The expression level of LINC00173 was obviously increased in A549-DDP and PC9-DDP cell lines after treated with LY294002. h. The IC 50 values to cisplatin were detected in A549 and PC9 cells transfected with a gradient concentration of c-Myc plasmids. Student’s two-tailed t-test, ** P < 0.01; **** P < 0.0001. Error bars, mean ± SD

    Article Snippet: The antibodies against the following proteins were used: Caspase-3 (Cell Signaling Technology #14220, 1:1000), PARP (Cell Signaling Technology #9542, 1:1000), BCL2 (Cell Signaling Technology #15071, 1:1000), PROCA1 (Biorbyt #orb1703, 1:1000), ZFP36L2 (Santa Cruz #sc-365908, 1:1000), c-Myc (Cell Signaling Technology #9402, 1:1000), phosphor-Akt (Cell Signaling Technology #4060, 1:1000), Akt (Cell Signaling Technology #4691, 1:1000), phosphor-PI3K (Cell Signaling Technology #17366, 1:1000), and PI3K (Cell Signaling Technology #4292, 1:1000).

    Techniques: Expressing, Binding Assay, Transfection, Two Tailed Test, Agarose Gel Electrophoresis, Luciferase, Reporter Assay, Western Blot, Concentration Assay