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    Cell Signaling Technology Inc p akt the308
    P Akt The308, 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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    akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc akt
    Elevated tryptophan are noticed in T2D patients, which can induce insulin resistance in mice. A Tryptophan levels are elevated in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). B Tryptophan levels are positively associated with HbA1c levels in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). C, D Male C57BL/6J mice were fed with standard chow (SC) or tryptophan-rich chow (Trp, 10 g/kg), glucose tolerance (GTT, C) and insulin tolerance (ITT, D) were measured after 12 weeks of feeding (n = 5), and areas under the curve of the GTT and ITT were statistical analyzed and presented as bar graph, respectively. E Impairment of insulin signaling in mice fed with the tryptophan-rich chow. Mice were fasted for 6 h and then treated with intraperitoneally injection of insulin (0.5 units/kg). After 15 min, mice were euthanized and tissues were harvested, the phosphorylation of IR, <t>AKT,</t> <t>and</t> <t>AS160</t> in the inguinal fat was detected by western blot
    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 "Tryptophanylation of insulin receptor by WARS attenuates insulin signaling"

    Article Title: Tryptophanylation of insulin receptor by WARS attenuates insulin signaling

    Journal: Cellular and Molecular Life Sciences: CMLS

    doi: 10.1007/s00018-023-05082-2

    Elevated tryptophan are noticed in T2D patients, which can induce insulin resistance in mice. A Tryptophan levels are elevated in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). B Tryptophan levels are positively associated with HbA1c levels in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). C, D Male C57BL/6J mice were fed with standard chow (SC) or tryptophan-rich chow (Trp, 10 g/kg), glucose tolerance (GTT, C) and insulin tolerance (ITT, D) were measured after 12 weeks of feeding (n = 5), and areas under the curve of the GTT and ITT were statistical analyzed and presented as bar graph, respectively. E Impairment of insulin signaling in mice fed with the tryptophan-rich chow. Mice were fasted for 6 h and then treated with intraperitoneally injection of insulin (0.5 units/kg). After 15 min, mice were euthanized and tissues were harvested, the phosphorylation of IR, AKT, and AS160 in the inguinal fat was detected by western blot
    Figure Legend Snippet: Elevated tryptophan are noticed in T2D patients, which can induce insulin resistance in mice. A Tryptophan levels are elevated in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). B Tryptophan levels are positively associated with HbA1c levels in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). C, D Male C57BL/6J mice were fed with standard chow (SC) or tryptophan-rich chow (Trp, 10 g/kg), glucose tolerance (GTT, C) and insulin tolerance (ITT, D) were measured after 12 weeks of feeding (n = 5), and areas under the curve of the GTT and ITT were statistical analyzed and presented as bar graph, respectively. E Impairment of insulin signaling in mice fed with the tryptophan-rich chow. Mice were fasted for 6 h and then treated with intraperitoneally injection of insulin (0.5 units/kg). After 15 min, mice were euthanized and tissues were harvested, the phosphorylation of IR, AKT, and AS160 in the inguinal fat was detected by western blot

    Techniques Used: Injection, Western Blot

    Tryptophan blocks insulin signaling directly in vitro. A–C Me-Trp treatment impaired insulin signaling. The dose- (A) and time-dependent (B) effects of Me-Trp on the phosphorylation of IR, AKT, and AS160 with insulin-stimulation (100 nM, 10 min), and (C) the insulin-induced dose-dependent IR, AKT, and AS160 phosphorylation with and without of 0.5 mM Me-Trp supplementation in cultured human differentiated HPA-v cells was detected by western blot. D Me-Trp reduced insulin-stimulated glucose uptake. Glucose uptake by differentiated HPA-v cells treated with Me-Trp (0, 0.2, 0.4, 0.6, 0.8 mM) for 40 min and stimulated with 100 nM insulin for 15 min. Data were represented as means ± S.E.M, n = 6. E, F Tryptamine abrogated the inhibition of insulin signaling caused by Me-Trp supplementation. E tryptamine is an analog of tryptophan. F HeLa cells were treated with Me-Trp or tryptamine as indicated, and the phosphorylation levels of IR, AKT, and AS160 after insulin stimulation were detected. G, H Inhibition of IDO and TDO did not reactivate the insulin signaling. Cells were treated with 2.5 μM LM10 (G) or 100 nM INCB024360 (H) for 48 h, then treated with Me-Trp, and with insulin stimulation as indicated. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot. I, J Supplement kynurenine (KYN) or serotonin (5-HT) did not alter the insulin signaling. Differentiated HPA-v cells were treated with different concentrations of Me-Trp, KYN (I), or 5-HT (J), and with insulin stimulation. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot
    Figure Legend Snippet: Tryptophan blocks insulin signaling directly in vitro. A–C Me-Trp treatment impaired insulin signaling. The dose- (A) and time-dependent (B) effects of Me-Trp on the phosphorylation of IR, AKT, and AS160 with insulin-stimulation (100 nM, 10 min), and (C) the insulin-induced dose-dependent IR, AKT, and AS160 phosphorylation with and without of 0.5 mM Me-Trp supplementation in cultured human differentiated HPA-v cells was detected by western blot. D Me-Trp reduced insulin-stimulated glucose uptake. Glucose uptake by differentiated HPA-v cells treated with Me-Trp (0, 0.2, 0.4, 0.6, 0.8 mM) for 40 min and stimulated with 100 nM insulin for 15 min. Data were represented as means ± S.E.M, n = 6. E, F Tryptamine abrogated the inhibition of insulin signaling caused by Me-Trp supplementation. E tryptamine is an analog of tryptophan. F HeLa cells were treated with Me-Trp or tryptamine as indicated, and the phosphorylation levels of IR, AKT, and AS160 after insulin stimulation were detected. G, H Inhibition of IDO and TDO did not reactivate the insulin signaling. Cells were treated with 2.5 μM LM10 (G) or 100 nM INCB024360 (H) for 48 h, then treated with Me-Trp, and with insulin stimulation as indicated. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot. I, J Supplement kynurenine (KYN) or serotonin (5-HT) did not alter the insulin signaling. Differentiated HPA-v cells were treated with different concentrations of Me-Trp, KYN (I), or 5-HT (J), and with insulin stimulation. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot

    Techniques Used: In Vitro, Cell Culture, Western Blot, Inhibition

    WARS tryptophanylates Lys1209 of IR. A Me-Trp had negligible effects on insulin signaling in IR-KO HeLa cells. Phosphorylation of AKT and AS160 was detected in wide-type and IR-KO HeLa cells in the presence of Me-Trp supplementation with insulin stimulation. B WARS directly interacted with IRβ. Co-IP assay of HEK 293T cells ectopically co-expressed WARS-HA and IRβ-Flag. Cell lysates were subjected to immunoprecipitation with anti-Flag antibodies, and whole cell lysates and immunoprecipitants were analyzed with anti-HA or anti-Flag antibodies. C K1209 is the tryptophanylation site of IR. K1209 of IR was mutated to arginine (IRK1209R) or tryptophan (IRK1209W), and was transiently expressed in HepG2 cells. The phosphorylation of IR was detected in the absence or presence of Me-Trp supplementation with insulin stimulation. D K1209R mutation of IR replenished insulin signaling activation. The activation of insulin signaling to Me-Trp treatment was detected for wide-type, IRK1209R knock-in HeLa cells. E WARS tryptophanylated IR K1209 peptide. Synthesized IR peptide containing K1209 site was cultured with or without purified recombinant WARS in an in vitro system, and the formation of tryptophanylated products (red arrows) was assayed by mass spectrometry
    Figure Legend Snippet: WARS tryptophanylates Lys1209 of IR. A Me-Trp had negligible effects on insulin signaling in IR-KO HeLa cells. Phosphorylation of AKT and AS160 was detected in wide-type and IR-KO HeLa cells in the presence of Me-Trp supplementation with insulin stimulation. B WARS directly interacted with IRβ. Co-IP assay of HEK 293T cells ectopically co-expressed WARS-HA and IRβ-Flag. Cell lysates were subjected to immunoprecipitation with anti-Flag antibodies, and whole cell lysates and immunoprecipitants were analyzed with anti-HA or anti-Flag antibodies. C K1209 is the tryptophanylation site of IR. K1209 of IR was mutated to arginine (IRK1209R) or tryptophan (IRK1209W), and was transiently expressed in HepG2 cells. The phosphorylation of IR was detected in the absence or presence of Me-Trp supplementation with insulin stimulation. D K1209R mutation of IR replenished insulin signaling activation. The activation of insulin signaling to Me-Trp treatment was detected for wide-type, IRK1209R knock-in HeLa cells. E WARS tryptophanylated IR K1209 peptide. Synthesized IR peptide containing K1209 site was cultured with or without purified recombinant WARS in an in vitro system, and the formation of tryptophanylated products (red arrows) was assayed by mass spectrometry

    Techniques Used: Co-Immunoprecipitation Assay, Immunoprecipitation, Mutagenesis, Activation Assay, Knock-In, Synthesized, Cell Culture, Purification, Recombinant, In Vitro, Mass Spectrometry

    SIRT1 detryptophanylates W-K1209 and blunts Trp-induced insulin insensitivity. A, B Sirtuin inhibition elevated IRW−K1209 levels and decreased insulin signaling. A IRW−K1209 levels were detected in HeLa cells transfected with IR-Flag and treated with 5 mM NAM as indicated. B HepG2 cells treated with NAM and Me-Trp for 1 h, and stimulated with insulin as indicated. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot. C SIRT1 interacted with IR. Co-IP assay of HeLa cells ectopically co-expressed SIRT1-HA and IR-Flag. Cell lysates were subjected to immunoprecipitation with anti-Flag antibodies, and whole cell lysates and immunoprecipitants were analyzed with anti-HA or anti-Flag antibodies. D, E HepG2 cells were transfected with IR-Flag plus siSIRT1 (D), or plus SIRT1-HA (E), and treated with Me-Trp or not as indicated, the IRW−K1209 levels were determined using specific α- IRW−K1209 antibodies in the immunoprecipitants pulled down by anti-Flag antibodies (left), and the glucose uptake was measured (right). F-G, HepG2 cells were transfected with IR-Flag plus siSIRT1 (F), or plus SIRT1-HA (G), and after 48 h, cells were treated with Me-Trp for 1 h as indicated. The phosphorylation levels of IR, AKT, and AS160 after insulin stimulation were detected by western blot
    Figure Legend Snippet: SIRT1 detryptophanylates W-K1209 and blunts Trp-induced insulin insensitivity. A, B Sirtuin inhibition elevated IRW−K1209 levels and decreased insulin signaling. A IRW−K1209 levels were detected in HeLa cells transfected with IR-Flag and treated with 5 mM NAM as indicated. B HepG2 cells treated with NAM and Me-Trp for 1 h, and stimulated with insulin as indicated. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot. C SIRT1 interacted with IR. Co-IP assay of HeLa cells ectopically co-expressed SIRT1-HA and IR-Flag. Cell lysates were subjected to immunoprecipitation with anti-Flag antibodies, and whole cell lysates and immunoprecipitants were analyzed with anti-HA or anti-Flag antibodies. D, E HepG2 cells were transfected with IR-Flag plus siSIRT1 (D), or plus SIRT1-HA (E), and treated with Me-Trp or not as indicated, the IRW−K1209 levels were determined using specific α- IRW−K1209 antibodies in the immunoprecipitants pulled down by anti-Flag antibodies (left), and the glucose uptake was measured (right). F-G, HepG2 cells were transfected with IR-Flag plus siSIRT1 (F), or plus SIRT1-HA (G), and after 48 h, cells were treated with Me-Trp for 1 h as indicated. The phosphorylation levels of IR, AKT, and AS160 after insulin stimulation were detected by western blot

    Techniques Used: Inhibition, Transfection, Western Blot, Co-Immunoprecipitation Assay, Immunoprecipitation

    p akt the308  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p akt the308
    P Akt The308, 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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    akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc akt
    Elevated tryptophan are noticed in T2D patients, which can induce insulin resistance in mice. A Tryptophan levels are elevated in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). B Tryptophan levels are positively associated with HbA1c levels in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). C, D Male C57BL/6J mice were fed with standard chow (SC) or tryptophan-rich chow (Trp, 10 g/kg), glucose tolerance (GTT, C) and insulin tolerance (ITT, D) were measured after 12 weeks of feeding (n = 5), and areas under the curve of the GTT and ITT were statistical analyzed and presented as bar graph, respectively. E Impairment of insulin signaling in mice fed with the tryptophan-rich chow. Mice were fasted for 6 h and then treated with intraperitoneally injection of insulin (0.5 units/kg). After 15 min, mice were euthanized and tissues were harvested, the phosphorylation of IR, <t>AKT,</t> <t>and</t> <t>AS160</t> in the inguinal fat was detected by western blot
    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
    https://www.bioz.com/result/akt/product/Cell Signaling Technology Inc
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    1) Product Images from "Tryptophanylation of insulin receptor by WARS attenuates insulin signaling"

    Article Title: Tryptophanylation of insulin receptor by WARS attenuates insulin signaling

    Journal: Cellular and Molecular Life Sciences: CMLS

    doi: 10.1007/s00018-023-05082-2

    Elevated tryptophan are noticed in T2D patients, which can induce insulin resistance in mice. A Tryptophan levels are elevated in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). B Tryptophan levels are positively associated with HbA1c levels in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). C, D Male C57BL/6J mice were fed with standard chow (SC) or tryptophan-rich chow (Trp, 10 g/kg), glucose tolerance (GTT, C) and insulin tolerance (ITT, D) were measured after 12 weeks of feeding (n = 5), and areas under the curve of the GTT and ITT were statistical analyzed and presented as bar graph, respectively. E Impairment of insulin signaling in mice fed with the tryptophan-rich chow. Mice were fasted for 6 h and then treated with intraperitoneally injection of insulin (0.5 units/kg). After 15 min, mice were euthanized and tissues were harvested, the phosphorylation of IR, AKT, and AS160 in the inguinal fat was detected by western blot
    Figure Legend Snippet: Elevated tryptophan are noticed in T2D patients, which can induce insulin resistance in mice. A Tryptophan levels are elevated in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). B Tryptophan levels are positively associated with HbA1c levels in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). C, D Male C57BL/6J mice were fed with standard chow (SC) or tryptophan-rich chow (Trp, 10 g/kg), glucose tolerance (GTT, C) and insulin tolerance (ITT, D) were measured after 12 weeks of feeding (n = 5), and areas under the curve of the GTT and ITT were statistical analyzed and presented as bar graph, respectively. E Impairment of insulin signaling in mice fed with the tryptophan-rich chow. Mice were fasted for 6 h and then treated with intraperitoneally injection of insulin (0.5 units/kg). After 15 min, mice were euthanized and tissues were harvested, the phosphorylation of IR, AKT, and AS160 in the inguinal fat was detected by western blot

    Techniques Used: Injection, Western Blot

    Tryptophan blocks insulin signaling directly in vitro. A–C Me-Trp treatment impaired insulin signaling. The dose- (A) and time-dependent (B) effects of Me-Trp on the phosphorylation of IR, AKT, and AS160 with insulin-stimulation (100 nM, 10 min), and (C) the insulin-induced dose-dependent IR, AKT, and AS160 phosphorylation with and without of 0.5 mM Me-Trp supplementation in cultured human differentiated HPA-v cells was detected by western blot. D Me-Trp reduced insulin-stimulated glucose uptake. Glucose uptake by differentiated HPA-v cells treated with Me-Trp (0, 0.2, 0.4, 0.6, 0.8 mM) for 40 min and stimulated with 100 nM insulin for 15 min. Data were represented as means ± S.E.M, n = 6. E, F Tryptamine abrogated the inhibition of insulin signaling caused by Me-Trp supplementation. E tryptamine is an analog of tryptophan. F HeLa cells were treated with Me-Trp or tryptamine as indicated, and the phosphorylation levels of IR, AKT, and AS160 after insulin stimulation were detected. G, H Inhibition of IDO and TDO did not reactivate the insulin signaling. Cells were treated with 2.5 μM LM10 (G) or 100 nM INCB024360 (H) for 48 h, then treated with Me-Trp, and with insulin stimulation as indicated. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot. I, J Supplement kynurenine (KYN) or serotonin (5-HT) did not alter the insulin signaling. Differentiated HPA-v cells were treated with different concentrations of Me-Trp, KYN (I), or 5-HT (J), and with insulin stimulation. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot
    Figure Legend Snippet: Tryptophan blocks insulin signaling directly in vitro. A–C Me-Trp treatment impaired insulin signaling. The dose- (A) and time-dependent (B) effects of Me-Trp on the phosphorylation of IR, AKT, and AS160 with insulin-stimulation (100 nM, 10 min), and (C) the insulin-induced dose-dependent IR, AKT, and AS160 phosphorylation with and without of 0.5 mM Me-Trp supplementation in cultured human differentiated HPA-v cells was detected by western blot. D Me-Trp reduced insulin-stimulated glucose uptake. Glucose uptake by differentiated HPA-v cells treated with Me-Trp (0, 0.2, 0.4, 0.6, 0.8 mM) for 40 min and stimulated with 100 nM insulin for 15 min. Data were represented as means ± S.E.M, n = 6. E, F Tryptamine abrogated the inhibition of insulin signaling caused by Me-Trp supplementation. E tryptamine is an analog of tryptophan. F HeLa cells were treated with Me-Trp or tryptamine as indicated, and the phosphorylation levels of IR, AKT, and AS160 after insulin stimulation were detected. G, H Inhibition of IDO and TDO did not reactivate the insulin signaling. Cells were treated with 2.5 μM LM10 (G) or 100 nM INCB024360 (H) for 48 h, then treated with Me-Trp, and with insulin stimulation as indicated. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot. I, J Supplement kynurenine (KYN) or serotonin (5-HT) did not alter the insulin signaling. Differentiated HPA-v cells were treated with different concentrations of Me-Trp, KYN (I), or 5-HT (J), and with insulin stimulation. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot

    Techniques Used: In Vitro, Cell Culture, Western Blot, Inhibition

    WARS tryptophanylates Lys1209 of IR. A Me-Trp had negligible effects on insulin signaling in IR-KO HeLa cells. Phosphorylation of AKT and AS160 was detected in wide-type and IR-KO HeLa cells in the presence of Me-Trp supplementation with insulin stimulation. B WARS directly interacted with IRβ. Co-IP assay of HEK 293T cells ectopically co-expressed WARS-HA and IRβ-Flag. Cell lysates were subjected to immunoprecipitation with anti-Flag antibodies, and whole cell lysates and immunoprecipitants were analyzed with anti-HA or anti-Flag antibodies. C K1209 is the tryptophanylation site of IR. K1209 of IR was mutated to arginine (IRK1209R) or tryptophan (IRK1209W), and was transiently expressed in HepG2 cells. The phosphorylation of IR was detected in the absence or presence of Me-Trp supplementation with insulin stimulation. D K1209R mutation of IR replenished insulin signaling activation. The activation of insulin signaling to Me-Trp treatment was detected for wide-type, IRK1209R knock-in HeLa cells. E WARS tryptophanylated IR K1209 peptide. Synthesized IR peptide containing K1209 site was cultured with or without purified recombinant WARS in an in vitro system, and the formation of tryptophanylated products (red arrows) was assayed by mass spectrometry
    Figure Legend Snippet: WARS tryptophanylates Lys1209 of IR. A Me-Trp had negligible effects on insulin signaling in IR-KO HeLa cells. Phosphorylation of AKT and AS160 was detected in wide-type and IR-KO HeLa cells in the presence of Me-Trp supplementation with insulin stimulation. B WARS directly interacted with IRβ. Co-IP assay of HEK 293T cells ectopically co-expressed WARS-HA and IRβ-Flag. Cell lysates were subjected to immunoprecipitation with anti-Flag antibodies, and whole cell lysates and immunoprecipitants were analyzed with anti-HA or anti-Flag antibodies. C K1209 is the tryptophanylation site of IR. K1209 of IR was mutated to arginine (IRK1209R) or tryptophan (IRK1209W), and was transiently expressed in HepG2 cells. The phosphorylation of IR was detected in the absence or presence of Me-Trp supplementation with insulin stimulation. D K1209R mutation of IR replenished insulin signaling activation. The activation of insulin signaling to Me-Trp treatment was detected for wide-type, IRK1209R knock-in HeLa cells. E WARS tryptophanylated IR K1209 peptide. Synthesized IR peptide containing K1209 site was cultured with or without purified recombinant WARS in an in vitro system, and the formation of tryptophanylated products (red arrows) was assayed by mass spectrometry

    Techniques Used: Co-Immunoprecipitation Assay, Immunoprecipitation, Mutagenesis, Activation Assay, Knock-In, Synthesized, Cell Culture, Purification, Recombinant, In Vitro, Mass Spectrometry

    SIRT1 detryptophanylates W-K1209 and blunts Trp-induced insulin insensitivity. A, B Sirtuin inhibition elevated IRW−K1209 levels and decreased insulin signaling. A IRW−K1209 levels were detected in HeLa cells transfected with IR-Flag and treated with 5 mM NAM as indicated. B HepG2 cells treated with NAM and Me-Trp for 1 h, and stimulated with insulin as indicated. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot. C SIRT1 interacted with IR. Co-IP assay of HeLa cells ectopically co-expressed SIRT1-HA and IR-Flag. Cell lysates were subjected to immunoprecipitation with anti-Flag antibodies, and whole cell lysates and immunoprecipitants were analyzed with anti-HA or anti-Flag antibodies. D, E HepG2 cells were transfected with IR-Flag plus siSIRT1 (D), or plus SIRT1-HA (E), and treated with Me-Trp or not as indicated, the IRW−K1209 levels were determined using specific α- IRW−K1209 antibodies in the immunoprecipitants pulled down by anti-Flag antibodies (left), and the glucose uptake was measured (right). F-G, HepG2 cells were transfected with IR-Flag plus siSIRT1 (F), or plus SIRT1-HA (G), and after 48 h, cells were treated with Me-Trp for 1 h as indicated. The phosphorylation levels of IR, AKT, and AS160 after insulin stimulation were detected by western blot
    Figure Legend Snippet: SIRT1 detryptophanylates W-K1209 and blunts Trp-induced insulin insensitivity. A, B Sirtuin inhibition elevated IRW−K1209 levels and decreased insulin signaling. A IRW−K1209 levels were detected in HeLa cells transfected with IR-Flag and treated with 5 mM NAM as indicated. B HepG2 cells treated with NAM and Me-Trp for 1 h, and stimulated with insulin as indicated. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot. C SIRT1 interacted with IR. Co-IP assay of HeLa cells ectopically co-expressed SIRT1-HA and IR-Flag. Cell lysates were subjected to immunoprecipitation with anti-Flag antibodies, and whole cell lysates and immunoprecipitants were analyzed with anti-HA or anti-Flag antibodies. D, E HepG2 cells were transfected with IR-Flag plus siSIRT1 (D), or plus SIRT1-HA (E), and treated with Me-Trp or not as indicated, the IRW−K1209 levels were determined using specific α- IRW−K1209 antibodies in the immunoprecipitants pulled down by anti-Flag antibodies (left), and the glucose uptake was measured (right). F-G, HepG2 cells were transfected with IR-Flag plus siSIRT1 (F), or plus SIRT1-HA (G), and after 48 h, cells were treated with Me-Trp for 1 h as indicated. The phosphorylation levels of IR, AKT, and AS160 after insulin stimulation were detected by western blot

    Techniques Used: Inhibition, Transfection, Western Blot, Co-Immunoprecipitation Assay, Immunoprecipitation

    akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc akt
    Inhibition of GPX4 <t>inhibits</t> <t>mTOR/AKT</t> pathway of EGFR T790M/L858R and wild-type EGFR non-small cell lung cancer cells. (A) H3255, A549 and H1975 cells were treated with different concentrations of RSL3 (0, 0.25, 0.5, 1, 2, 4, 8 and 16 µM) for 24 h. The cell viability was detected using MTT. **P<0.01, ***P<0.001 and ****P<0.0001 vs. the control group (0 µM of RSL3) using Dunnett's test. (B) H1975, (C) A549 and (D) H3255 cells were treated with different concentrations of RAD001 (0, 0.5, 1 and 8 µM) combined with RSL3 (0, 0.1 and 0.5 µM). After 24 h, the expression of p-mTOR, mTOR and AKT were detected using western blotting, and GAPDH expression was used as an internal standard. EGFR, epidermal growth factor receptor; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; p-, phosphorylated; mTOR, mammalian target of rapamycin.
    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 "Mechanism of targeting the mTOR pathway to regulate ferroptosis in NSCLC with different EGFR mutations"

    Article Title: Mechanism of targeting the mTOR pathway to regulate ferroptosis in NSCLC with different EGFR mutations

    Journal: Oncology Letters

    doi: 10.3892/ol.2024.14431

    Inhibition of GPX4 inhibits mTOR/AKT pathway of EGFR T790M/L858R and wild-type EGFR non-small cell lung cancer cells. (A) H3255, A549 and H1975 cells were treated with different concentrations of RSL3 (0, 0.25, 0.5, 1, 2, 4, 8 and 16 µM) for 24 h. The cell viability was detected using MTT. **P<0.01, ***P<0.001 and ****P<0.0001 vs. the control group (0 µM of RSL3) using Dunnett's test. (B) H1975, (C) A549 and (D) H3255 cells were treated with different concentrations of RAD001 (0, 0.5, 1 and 8 µM) combined with RSL3 (0, 0.1 and 0.5 µM). After 24 h, the expression of p-mTOR, mTOR and AKT were detected using western blotting, and GAPDH expression was used as an internal standard. EGFR, epidermal growth factor receptor; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; p-, phosphorylated; mTOR, mammalian target of rapamycin.
    Figure Legend Snippet: Inhibition of GPX4 inhibits mTOR/AKT pathway of EGFR T790M/L858R and wild-type EGFR non-small cell lung cancer cells. (A) H3255, A549 and H1975 cells were treated with different concentrations of RSL3 (0, 0.25, 0.5, 1, 2, 4, 8 and 16 µM) for 24 h. The cell viability was detected using MTT. **P<0.01, ***P<0.001 and ****P<0.0001 vs. the control group (0 µM of RSL3) using Dunnett's test. (B) H1975, (C) A549 and (D) H3255 cells were treated with different concentrations of RAD001 (0, 0.5, 1 and 8 µM) combined with RSL3 (0, 0.1 and 0.5 µM). After 24 h, the expression of p-mTOR, mTOR and AKT were detected using western blotting, and GAPDH expression was used as an internal standard. EGFR, epidermal growth factor receptor; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; p-, phosphorylated; mTOR, mammalian target of rapamycin.

    Techniques Used: Inhibition, Expressing, Western Blot

    phospho akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho akt
    SCE <t>regulates</t> <t>AKT/mTOR</t> and its downstream effectors in myotubes. (A) C2C12 myoblasts were induced to differentiate in a DMEM containing 2% horse serum, treated for 5 days with different concentration of SCE (1, 5 and 10 ng/ml) and analyzed using western blotting (left). Quantification of protein expression levels (n=3 per group) (right). **P<0.01 and ***P<0.001 vs. the control. (B) Cells were treated with 10 ng/ml SCE in DM for 1, 3 and 5 days and western blotting was performed using the indicated antibodies (left). Quantification of protein expression levels (n=3 per group) (right). *P<0.05, **P<0.01 and ***P<0.001 vs. the DMSO; #P<0.05, ##P<0.01 and ###P<0.001 vs. the DMSO at the indicated time points. SCE, Saururus chinensis (Lour.) Baill. extract; p-, phosphorylated; p70S6K1, ribosomal protein S6 kinase B1.
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    1) Product Images from "Saururus chinensis (Lour.) Baill. extract promotes skeletal muscle cell differentiation by positively regulating mitochondrial biogenesis and AKT/mTOR signaling in vitro"

    Article Title: Saururus chinensis (Lour.) Baill. extract promotes skeletal muscle cell differentiation by positively regulating mitochondrial biogenesis and AKT/mTOR signaling in vitro

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2024.13250

    SCE regulates AKT/mTOR and its downstream effectors in myotubes. (A) C2C12 myoblasts were induced to differentiate in a DMEM containing 2% horse serum, treated for 5 days with different concentration of SCE (1, 5 and 10 ng/ml) and analyzed using western blotting (left). Quantification of protein expression levels (n=3 per group) (right). **P<0.01 and ***P<0.001 vs. the control. (B) Cells were treated with 10 ng/ml SCE in DM for 1, 3 and 5 days and western blotting was performed using the indicated antibodies (left). Quantification of protein expression levels (n=3 per group) (right). *P<0.05, **P<0.01 and ***P<0.001 vs. the DMSO; #P<0.05, ##P<0.01 and ###P<0.001 vs. the DMSO at the indicated time points. SCE, Saururus chinensis (Lour.) Baill. extract; p-, phosphorylated; p70S6K1, ribosomal protein S6 kinase B1.
    Figure Legend Snippet: SCE regulates AKT/mTOR and its downstream effectors in myotubes. (A) C2C12 myoblasts were induced to differentiate in a DMEM containing 2% horse serum, treated for 5 days with different concentration of SCE (1, 5 and 10 ng/ml) and analyzed using western blotting (left). Quantification of protein expression levels (n=3 per group) (right). **P<0.01 and ***P<0.001 vs. the control. (B) Cells were treated with 10 ng/ml SCE in DM for 1, 3 and 5 days and western blotting was performed using the indicated antibodies (left). Quantification of protein expression levels (n=3 per group) (right). *P<0.05, **P<0.01 and ***P<0.001 vs. the DMSO; #P<0.05, ##P<0.01 and ###P<0.001 vs. the DMSO at the indicated time points. SCE, Saururus chinensis (Lour.) Baill. extract; p-, phosphorylated; p70S6K1, ribosomal protein S6 kinase B1.

    Techniques Used: Concentration Assay, Western Blot, Expressing

    phosphorylated p akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphorylated p akt
    Recombinant adenovirus enhancing apoptosis through PI3K/AKT-caspase-3 ameliorates resistance to DDP on SKOV3 cells. (A) The representative images of the Annexin V-APC staining assay. (B) Recombinant adenovirus and/or DDP promoted the apoptosis of ovarian cancer cells and the apoptosis rate in combination group was significantly higher than that in DDP group (n=4 in each group). (C) PI3K was significantly suppressed by recombinant adenovirus and/or DDP and Ad-siERCC1 could greatly enhanced the effect of DDP (n=4 in each group). (D) AKT was significantly suppressed by recombinant adenovirus and (or) DDP and Ad-siERCC1 could greatly enhanced the effect of DDP (n=4 in each group). (E) Procaspase-3 was significantly reduced after recombinant adenovirus and/or DDP incubation, whereas cleaved caspase-3 was considerably increased (n=4 in each group). Data are shown as the mean ± SEM. *P<0.05, **P<0.01, ***P<0.001 vs. corresponding controls; # P<0.05, ## P<0.01, ### P<0.001 vs. DDP groups, & P<0.05, &&& P<0.001 vs. DDP combined with Ad-NC groups. DDP, cisplatin; si, short interfering; NC, negative control; p-. <t>phosphorylated.</t>
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    1) Product Images from "Dual‑regulated oncolytic adenovirus carrying ERCC1 ‑siRNA gene possesses potent antitumor effect on ovarian cancer cells"

    Article Title: Dual‑regulated oncolytic adenovirus carrying ERCC1 ‑siRNA gene possesses potent antitumor effect on ovarian cancer cells

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2024.13245

    Recombinant adenovirus enhancing apoptosis through PI3K/AKT-caspase-3 ameliorates resistance to DDP on SKOV3 cells. (A) The representative images of the Annexin V-APC staining assay. (B) Recombinant adenovirus and/or DDP promoted the apoptosis of ovarian cancer cells and the apoptosis rate in combination group was significantly higher than that in DDP group (n=4 in each group). (C) PI3K was significantly suppressed by recombinant adenovirus and/or DDP and Ad-siERCC1 could greatly enhanced the effect of DDP (n=4 in each group). (D) AKT was significantly suppressed by recombinant adenovirus and (or) DDP and Ad-siERCC1 could greatly enhanced the effect of DDP (n=4 in each group). (E) Procaspase-3 was significantly reduced after recombinant adenovirus and/or DDP incubation, whereas cleaved caspase-3 was considerably increased (n=4 in each group). Data are shown as the mean ± SEM. *P<0.05, **P<0.01, ***P<0.001 vs. corresponding controls; # P<0.05, ## P<0.01, ### P<0.001 vs. DDP groups, & P<0.05, &&& P<0.001 vs. DDP combined with Ad-NC groups. DDP, cisplatin; si, short interfering; NC, negative control; p-. phosphorylated.
    Figure Legend Snippet: Recombinant adenovirus enhancing apoptosis through PI3K/AKT-caspase-3 ameliorates resistance to DDP on SKOV3 cells. (A) The representative images of the Annexin V-APC staining assay. (B) Recombinant adenovirus and/or DDP promoted the apoptosis of ovarian cancer cells and the apoptosis rate in combination group was significantly higher than that in DDP group (n=4 in each group). (C) PI3K was significantly suppressed by recombinant adenovirus and/or DDP and Ad-siERCC1 could greatly enhanced the effect of DDP (n=4 in each group). (D) AKT was significantly suppressed by recombinant adenovirus and (or) DDP and Ad-siERCC1 could greatly enhanced the effect of DDP (n=4 in each group). (E) Procaspase-3 was significantly reduced after recombinant adenovirus and/or DDP incubation, whereas cleaved caspase-3 was considerably increased (n=4 in each group). Data are shown as the mean ± SEM. *P<0.05, **P<0.01, ***P<0.001 vs. corresponding controls; # P<0.05, ## P<0.01, ### P<0.001 vs. DDP groups, & P<0.05, &&& P<0.001 vs. DDP combined with Ad-NC groups. DDP, cisplatin; si, short interfering; NC, negative control; p-. phosphorylated.

    Techniques Used: Recombinant, Staining, Incubation, Negative Control

    akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc akt
    SCE <t>regulates</t> <t>AKT/mTOR</t> and its downstream effectors in myotubes. (A) C2C12 myoblasts were induced to differentiate in a DMEM containing 2% horse serum, treated for 5 days with different concentration of SCE (1, 5 and 10 ng/ml) and analyzed using western blotting (left). Quantification of protein expression levels (n=3 per group) (right). **P<0.01 and ***P<0.001 vs. the control. (B) Cells were treated with 10 ng/ml SCE in DM for 1, 3 and 5 days and western blotting was performed using the indicated antibodies (left). Quantification of protein expression levels (n=3 per group) (right). *P<0.05, **P<0.01 and ***P<0.001 vs. the DMSO; #P<0.05, ##P<0.01 and ###P<0.001 vs. the DMSO at the indicated time points. SCE, Saururus chinensis (Lour.) Baill. extract; p-, phosphorylated; p70S6K1, ribosomal protein S6 kinase B1.
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    1) Product Images from "Saururus chinensis (Lour.) Baill. extract promotes skeletal muscle cell differentiation by positively regulating mitochondrial biogenesis and AKT/mTOR signaling in vitro"

    Article Title: Saururus chinensis (Lour.) Baill. extract promotes skeletal muscle cell differentiation by positively regulating mitochondrial biogenesis and AKT/mTOR signaling in vitro

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2024.13250

    SCE regulates AKT/mTOR and its downstream effectors in myotubes. (A) C2C12 myoblasts were induced to differentiate in a DMEM containing 2% horse serum, treated for 5 days with different concentration of SCE (1, 5 and 10 ng/ml) and analyzed using western blotting (left). Quantification of protein expression levels (n=3 per group) (right). **P<0.01 and ***P<0.001 vs. the control. (B) Cells were treated with 10 ng/ml SCE in DM for 1, 3 and 5 days and western blotting was performed using the indicated antibodies (left). Quantification of protein expression levels (n=3 per group) (right). *P<0.05, **P<0.01 and ***P<0.001 vs. the DMSO; #P<0.05, ##P<0.01 and ###P<0.001 vs. the DMSO at the indicated time points. SCE, Saururus chinensis (Lour.) Baill. extract; p-, phosphorylated; p70S6K1, ribosomal protein S6 kinase B1.
    Figure Legend Snippet: SCE regulates AKT/mTOR and its downstream effectors in myotubes. (A) C2C12 myoblasts were induced to differentiate in a DMEM containing 2% horse serum, treated for 5 days with different concentration of SCE (1, 5 and 10 ng/ml) and analyzed using western blotting (left). Quantification of protein expression levels (n=3 per group) (right). **P<0.01 and ***P<0.001 vs. the control. (B) Cells were treated with 10 ng/ml SCE in DM for 1, 3 and 5 days and western blotting was performed using the indicated antibodies (left). Quantification of protein expression levels (n=3 per group) (right). *P<0.05, **P<0.01 and ***P<0.001 vs. the DMSO; #P<0.05, ##P<0.01 and ###P<0.001 vs. the DMSO at the indicated time points. SCE, Saururus chinensis (Lour.) Baill. extract; p-, phosphorylated; p70S6K1, ribosomal protein S6 kinase B1.

    Techniques Used: Concentration Assay, Western Blot, Expressing

    phosphorylated p akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphorylated p akt
    Effects of madanin-1 WT and madanin-1 2S on signaling pathways. SKOV3 and MDA-MB-231 cells were pretreated with madanin-1 WT or madanin-1 2S (10 µg/ml for 30 min) prior to treatment with thrombin (2 U/ml for 15 min). The protein expression levels of <t>p-Akt,</t> t-Akt, p-ERK and t-ERK in SKOV3 and MDA-MB-231 cells were analyzed by western blotting. (A) Representative gel images. (B) In SKOV3 cells, thrombin-induced p-Akt and p-ERK expression was significantly attenuated by both madanin-1 WT and madanin-1 2S treatment. In MDA-MB-231 cells, thrombin-induced p-Akt and p-ERK expression was significantly inhibited only by madanin-1 2S treatment. The protein expression levels were normalized to the level of β-actin in the same sample. Data are presented as the mean relative density ratio of each protein <t>(phosphorylated</t> form/total form) ± standard deviation of three independent experiments completed in triplicate (*P<0.05). WT, wild-type; 2S, 2 sulfation; p, phosphorylated; t, total; ERK, extracellular signal-regulated kinase.
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    1) Product Images from "Inhibitory effect of recombinant tyrosine‑sulfated madanin‑1, a thrombin inhibitor, on the behavior of MDA‑MB‑231 and SKOV3 cells in vitro"

    Article Title: Inhibitory effect of recombinant tyrosine‑sulfated madanin‑1, a thrombin inhibitor, on the behavior of MDA‑MB‑231 and SKOV3 cells in vitro

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2024.13238

    Effects of madanin-1 WT and madanin-1 2S on signaling pathways. SKOV3 and MDA-MB-231 cells were pretreated with madanin-1 WT or madanin-1 2S (10 µg/ml for 30 min) prior to treatment with thrombin (2 U/ml for 15 min). The protein expression levels of p-Akt, t-Akt, p-ERK and t-ERK in SKOV3 and MDA-MB-231 cells were analyzed by western blotting. (A) Representative gel images. (B) In SKOV3 cells, thrombin-induced p-Akt and p-ERK expression was significantly attenuated by both madanin-1 WT and madanin-1 2S treatment. In MDA-MB-231 cells, thrombin-induced p-Akt and p-ERK expression was significantly inhibited only by madanin-1 2S treatment. The protein expression levels were normalized to the level of β-actin in the same sample. Data are presented as the mean relative density ratio of each protein (phosphorylated form/total form) ± standard deviation of three independent experiments completed in triplicate (*P<0.05). WT, wild-type; 2S, 2 sulfation; p, phosphorylated; t, total; ERK, extracellular signal-regulated kinase.
    Figure Legend Snippet: Effects of madanin-1 WT and madanin-1 2S on signaling pathways. SKOV3 and MDA-MB-231 cells were pretreated with madanin-1 WT or madanin-1 2S (10 µg/ml for 30 min) prior to treatment with thrombin (2 U/ml for 15 min). The protein expression levels of p-Akt, t-Akt, p-ERK and t-ERK in SKOV3 and MDA-MB-231 cells were analyzed by western blotting. (A) Representative gel images. (B) In SKOV3 cells, thrombin-induced p-Akt and p-ERK expression was significantly attenuated by both madanin-1 WT and madanin-1 2S treatment. In MDA-MB-231 cells, thrombin-induced p-Akt and p-ERK expression was significantly inhibited only by madanin-1 2S treatment. The protein expression levels were normalized to the level of β-actin in the same sample. Data are presented as the mean relative density ratio of each protein (phosphorylated form/total form) ± standard deviation of three independent experiments completed in triplicate (*P<0.05). WT, wild-type; 2S, 2 sulfation; p, phosphorylated; t, total; ERK, extracellular signal-regulated kinase.

    Techniques Used: Expressing, Western Blot, Standard Deviation

    rabbit anti akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti akt
    Rabbit Anti 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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    Cell Signaling Technology Inc p akt the308
    P Akt The308, 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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    Cell Signaling Technology Inc akt
    Elevated tryptophan are noticed in T2D patients, which can induce insulin resistance in mice. A Tryptophan levels are elevated in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). B Tryptophan levels are positively associated with HbA1c levels in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). C, D Male C57BL/6J mice were fed with standard chow (SC) or tryptophan-rich chow (Trp, 10 g/kg), glucose tolerance (GTT, C) and insulin tolerance (ITT, D) were measured after 12 weeks of feeding (n = 5), and areas under the curve of the GTT and ITT were statistical analyzed and presented as bar graph, respectively. E Impairment of insulin signaling in mice fed with the tryptophan-rich chow. Mice were fasted for 6 h and then treated with intraperitoneally injection of insulin (0.5 units/kg). After 15 min, mice were euthanized and tissues were harvested, the phosphorylation of IR, <t>AKT,</t> <t>and</t> <t>AS160</t> in the inguinal fat was detected by western blot
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    Cell Signaling Technology Inc phospho akt
    SCE <t>regulates</t> <t>AKT/mTOR</t> and its downstream effectors in myotubes. (A) C2C12 myoblasts were induced to differentiate in a DMEM containing 2% horse serum, treated for 5 days with different concentration of SCE (1, 5 and 10 ng/ml) and analyzed using western blotting (left). Quantification of protein expression levels (n=3 per group) (right). **P<0.01 and ***P<0.001 vs. the control. (B) Cells were treated with 10 ng/ml SCE in DM for 1, 3 and 5 days and western blotting was performed using the indicated antibodies (left). Quantification of protein expression levels (n=3 per group) (right). *P<0.05, **P<0.01 and ***P<0.001 vs. the DMSO; #P<0.05, ##P<0.01 and ###P<0.001 vs. the DMSO at the indicated time points. SCE, Saururus chinensis (Lour.) Baill. extract; p-, phosphorylated; p70S6K1, ribosomal protein S6 kinase B1.
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    Cell Signaling Technology Inc phosphorylated p akt
    Recombinant adenovirus enhancing apoptosis through PI3K/AKT-caspase-3 ameliorates resistance to DDP on SKOV3 cells. (A) The representative images of the Annexin V-APC staining assay. (B) Recombinant adenovirus and/or DDP promoted the apoptosis of ovarian cancer cells and the apoptosis rate in combination group was significantly higher than that in DDP group (n=4 in each group). (C) PI3K was significantly suppressed by recombinant adenovirus and/or DDP and Ad-siERCC1 could greatly enhanced the effect of DDP (n=4 in each group). (D) AKT was significantly suppressed by recombinant adenovirus and (or) DDP and Ad-siERCC1 could greatly enhanced the effect of DDP (n=4 in each group). (E) Procaspase-3 was significantly reduced after recombinant adenovirus and/or DDP incubation, whereas cleaved caspase-3 was considerably increased (n=4 in each group). Data are shown as the mean ± SEM. *P<0.05, **P<0.01, ***P<0.001 vs. corresponding controls; # P<0.05, ## P<0.01, ### P<0.001 vs. DDP groups, & P<0.05, &&& P<0.001 vs. DDP combined with Ad-NC groups. DDP, cisplatin; si, short interfering; NC, negative control; p-. <t>phosphorylated.</t>
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    Cell Signaling Technology Inc rabbit anti akt
    Recombinant adenovirus enhancing apoptosis through PI3K/AKT-caspase-3 ameliorates resistance to DDP on SKOV3 cells. (A) The representative images of the Annexin V-APC staining assay. (B) Recombinant adenovirus and/or DDP promoted the apoptosis of ovarian cancer cells and the apoptosis rate in combination group was significantly higher than that in DDP group (n=4 in each group). (C) PI3K was significantly suppressed by recombinant adenovirus and/or DDP and Ad-siERCC1 could greatly enhanced the effect of DDP (n=4 in each group). (D) AKT was significantly suppressed by recombinant adenovirus and (or) DDP and Ad-siERCC1 could greatly enhanced the effect of DDP (n=4 in each group). (E) Procaspase-3 was significantly reduced after recombinant adenovirus and/or DDP incubation, whereas cleaved caspase-3 was considerably increased (n=4 in each group). Data are shown as the mean ± SEM. *P<0.05, **P<0.01, ***P<0.001 vs. corresponding controls; # P<0.05, ## P<0.01, ### P<0.001 vs. DDP groups, & P<0.05, &&& P<0.001 vs. DDP combined with Ad-NC groups. DDP, cisplatin; si, short interfering; NC, negative control; p-. <t>phosphorylated.</t>
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    Elevated tryptophan are noticed in T2D patients, which can induce insulin resistance in mice. A Tryptophan levels are elevated in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). B Tryptophan levels are positively associated with HbA1c levels in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). C, D Male C57BL/6J mice were fed with standard chow (SC) or tryptophan-rich chow (Trp, 10 g/kg), glucose tolerance (GTT, C) and insulin tolerance (ITT, D) were measured after 12 weeks of feeding (n = 5), and areas under the curve of the GTT and ITT were statistical analyzed and presented as bar graph, respectively. E Impairment of insulin signaling in mice fed with the tryptophan-rich chow. Mice were fasted for 6 h and then treated with intraperitoneally injection of insulin (0.5 units/kg). After 15 min, mice were euthanized and tissues were harvested, the phosphorylation of IR, AKT, and AS160 in the inguinal fat was detected by western blot

    Journal: Cellular and Molecular Life Sciences: CMLS

    Article Title: Tryptophanylation of insulin receptor by WARS attenuates insulin signaling

    doi: 10.1007/s00018-023-05082-2

    Figure Lengend Snippet: Elevated tryptophan are noticed in T2D patients, which can induce insulin resistance in mice. A Tryptophan levels are elevated in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). B Tryptophan levels are positively associated with HbA1c levels in plasma samples from patients with T2D (Con: n = 60, black; T2D: n = 62, red). C, D Male C57BL/6J mice were fed with standard chow (SC) or tryptophan-rich chow (Trp, 10 g/kg), glucose tolerance (GTT, C) and insulin tolerance (ITT, D) were measured after 12 weeks of feeding (n = 5), and areas under the curve of the GTT and ITT were statistical analyzed and presented as bar graph, respectively. E Impairment of insulin signaling in mice fed with the tryptophan-rich chow. Mice were fasted for 6 h and then treated with intraperitoneally injection of insulin (0.5 units/kg). After 15 min, mice were euthanized and tissues were harvested, the phosphorylation of IR, AKT, and AS160 in the inguinal fat was detected by western blot

    Article Snippet: Antibodies and reagents Antibodies against p-IR Tyr1189/1190 (#3024), IR (#3025), p-AKT The308 (#13038), AKT (#4685), p-AS160 Thr462 (#8881), AS160 (#2670) were purchased from Cell Signaling Technology (Massachusettes, USA).

    Techniques: Injection, Western Blot

    Tryptophan blocks insulin signaling directly in vitro. A–C Me-Trp treatment impaired insulin signaling. The dose- (A) and time-dependent (B) effects of Me-Trp on the phosphorylation of IR, AKT, and AS160 with insulin-stimulation (100 nM, 10 min), and (C) the insulin-induced dose-dependent IR, AKT, and AS160 phosphorylation with and without of 0.5 mM Me-Trp supplementation in cultured human differentiated HPA-v cells was detected by western blot. D Me-Trp reduced insulin-stimulated glucose uptake. Glucose uptake by differentiated HPA-v cells treated with Me-Trp (0, 0.2, 0.4, 0.6, 0.8 mM) for 40 min and stimulated with 100 nM insulin for 15 min. Data were represented as means ± S.E.M, n = 6. E, F Tryptamine abrogated the inhibition of insulin signaling caused by Me-Trp supplementation. E tryptamine is an analog of tryptophan. F HeLa cells were treated with Me-Trp or tryptamine as indicated, and the phosphorylation levels of IR, AKT, and AS160 after insulin stimulation were detected. G, H Inhibition of IDO and TDO did not reactivate the insulin signaling. Cells were treated with 2.5 μM LM10 (G) or 100 nM INCB024360 (H) for 48 h, then treated with Me-Trp, and with insulin stimulation as indicated. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot. I, J Supplement kynurenine (KYN) or serotonin (5-HT) did not alter the insulin signaling. Differentiated HPA-v cells were treated with different concentrations of Me-Trp, KYN (I), or 5-HT (J), and with insulin stimulation. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot

    Journal: Cellular and Molecular Life Sciences: CMLS

    Article Title: Tryptophanylation of insulin receptor by WARS attenuates insulin signaling

    doi: 10.1007/s00018-023-05082-2

    Figure Lengend Snippet: Tryptophan blocks insulin signaling directly in vitro. A–C Me-Trp treatment impaired insulin signaling. The dose- (A) and time-dependent (B) effects of Me-Trp on the phosphorylation of IR, AKT, and AS160 with insulin-stimulation (100 nM, 10 min), and (C) the insulin-induced dose-dependent IR, AKT, and AS160 phosphorylation with and without of 0.5 mM Me-Trp supplementation in cultured human differentiated HPA-v cells was detected by western blot. D Me-Trp reduced insulin-stimulated glucose uptake. Glucose uptake by differentiated HPA-v cells treated with Me-Trp (0, 0.2, 0.4, 0.6, 0.8 mM) for 40 min and stimulated with 100 nM insulin for 15 min. Data were represented as means ± S.E.M, n = 6. E, F Tryptamine abrogated the inhibition of insulin signaling caused by Me-Trp supplementation. E tryptamine is an analog of tryptophan. F HeLa cells were treated with Me-Trp or tryptamine as indicated, and the phosphorylation levels of IR, AKT, and AS160 after insulin stimulation were detected. G, H Inhibition of IDO and TDO did not reactivate the insulin signaling. Cells were treated with 2.5 μM LM10 (G) or 100 nM INCB024360 (H) for 48 h, then treated with Me-Trp, and with insulin stimulation as indicated. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot. I, J Supplement kynurenine (KYN) or serotonin (5-HT) did not alter the insulin signaling. Differentiated HPA-v cells were treated with different concentrations of Me-Trp, KYN (I), or 5-HT (J), and with insulin stimulation. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot

    Article Snippet: Antibodies and reagents Antibodies against p-IR Tyr1189/1190 (#3024), IR (#3025), p-AKT The308 (#13038), AKT (#4685), p-AS160 Thr462 (#8881), AS160 (#2670) were purchased from Cell Signaling Technology (Massachusettes, USA).

    Techniques: In Vitro, Cell Culture, Western Blot, Inhibition

    WARS tryptophanylates Lys1209 of IR. A Me-Trp had negligible effects on insulin signaling in IR-KO HeLa cells. Phosphorylation of AKT and AS160 was detected in wide-type and IR-KO HeLa cells in the presence of Me-Trp supplementation with insulin stimulation. B WARS directly interacted with IRβ. Co-IP assay of HEK 293T cells ectopically co-expressed WARS-HA and IRβ-Flag. Cell lysates were subjected to immunoprecipitation with anti-Flag antibodies, and whole cell lysates and immunoprecipitants were analyzed with anti-HA or anti-Flag antibodies. C K1209 is the tryptophanylation site of IR. K1209 of IR was mutated to arginine (IRK1209R) or tryptophan (IRK1209W), and was transiently expressed in HepG2 cells. The phosphorylation of IR was detected in the absence or presence of Me-Trp supplementation with insulin stimulation. D K1209R mutation of IR replenished insulin signaling activation. The activation of insulin signaling to Me-Trp treatment was detected for wide-type, IRK1209R knock-in HeLa cells. E WARS tryptophanylated IR K1209 peptide. Synthesized IR peptide containing K1209 site was cultured with or without purified recombinant WARS in an in vitro system, and the formation of tryptophanylated products (red arrows) was assayed by mass spectrometry

    Journal: Cellular and Molecular Life Sciences: CMLS

    Article Title: Tryptophanylation of insulin receptor by WARS attenuates insulin signaling

    doi: 10.1007/s00018-023-05082-2

    Figure Lengend Snippet: WARS tryptophanylates Lys1209 of IR. A Me-Trp had negligible effects on insulin signaling in IR-KO HeLa cells. Phosphorylation of AKT and AS160 was detected in wide-type and IR-KO HeLa cells in the presence of Me-Trp supplementation with insulin stimulation. B WARS directly interacted with IRβ. Co-IP assay of HEK 293T cells ectopically co-expressed WARS-HA and IRβ-Flag. Cell lysates were subjected to immunoprecipitation with anti-Flag antibodies, and whole cell lysates and immunoprecipitants were analyzed with anti-HA or anti-Flag antibodies. C K1209 is the tryptophanylation site of IR. K1209 of IR was mutated to arginine (IRK1209R) or tryptophan (IRK1209W), and was transiently expressed in HepG2 cells. The phosphorylation of IR was detected in the absence or presence of Me-Trp supplementation with insulin stimulation. D K1209R mutation of IR replenished insulin signaling activation. The activation of insulin signaling to Me-Trp treatment was detected for wide-type, IRK1209R knock-in HeLa cells. E WARS tryptophanylated IR K1209 peptide. Synthesized IR peptide containing K1209 site was cultured with or without purified recombinant WARS in an in vitro system, and the formation of tryptophanylated products (red arrows) was assayed by mass spectrometry

    Article Snippet: Antibodies and reagents Antibodies against p-IR Tyr1189/1190 (#3024), IR (#3025), p-AKT The308 (#13038), AKT (#4685), p-AS160 Thr462 (#8881), AS160 (#2670) were purchased from Cell Signaling Technology (Massachusettes, USA).

    Techniques: Co-Immunoprecipitation Assay, Immunoprecipitation, Mutagenesis, Activation Assay, Knock-In, Synthesized, Cell Culture, Purification, Recombinant, In Vitro, Mass Spectrometry

    SIRT1 detryptophanylates W-K1209 and blunts Trp-induced insulin insensitivity. A, B Sirtuin inhibition elevated IRW−K1209 levels and decreased insulin signaling. A IRW−K1209 levels were detected in HeLa cells transfected with IR-Flag and treated with 5 mM NAM as indicated. B HepG2 cells treated with NAM and Me-Trp for 1 h, and stimulated with insulin as indicated. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot. C SIRT1 interacted with IR. Co-IP assay of HeLa cells ectopically co-expressed SIRT1-HA and IR-Flag. Cell lysates were subjected to immunoprecipitation with anti-Flag antibodies, and whole cell lysates and immunoprecipitants were analyzed with anti-HA or anti-Flag antibodies. D, E HepG2 cells were transfected with IR-Flag plus siSIRT1 (D), or plus SIRT1-HA (E), and treated with Me-Trp or not as indicated, the IRW−K1209 levels were determined using specific α- IRW−K1209 antibodies in the immunoprecipitants pulled down by anti-Flag antibodies (left), and the glucose uptake was measured (right). F-G, HepG2 cells were transfected with IR-Flag plus siSIRT1 (F), or plus SIRT1-HA (G), and after 48 h, cells were treated with Me-Trp for 1 h as indicated. The phosphorylation levels of IR, AKT, and AS160 after insulin stimulation were detected by western blot

    Journal: Cellular and Molecular Life Sciences: CMLS

    Article Title: Tryptophanylation of insulin receptor by WARS attenuates insulin signaling

    doi: 10.1007/s00018-023-05082-2

    Figure Lengend Snippet: SIRT1 detryptophanylates W-K1209 and blunts Trp-induced insulin insensitivity. A, B Sirtuin inhibition elevated IRW−K1209 levels and decreased insulin signaling. A IRW−K1209 levels were detected in HeLa cells transfected with IR-Flag and treated with 5 mM NAM as indicated. B HepG2 cells treated with NAM and Me-Trp for 1 h, and stimulated with insulin as indicated. The phosphorylation levels of IR, AKT, and AS160 were detected by western blot. C SIRT1 interacted with IR. Co-IP assay of HeLa cells ectopically co-expressed SIRT1-HA and IR-Flag. Cell lysates were subjected to immunoprecipitation with anti-Flag antibodies, and whole cell lysates and immunoprecipitants were analyzed with anti-HA or anti-Flag antibodies. D, E HepG2 cells were transfected with IR-Flag plus siSIRT1 (D), or plus SIRT1-HA (E), and treated with Me-Trp or not as indicated, the IRW−K1209 levels were determined using specific α- IRW−K1209 antibodies in the immunoprecipitants pulled down by anti-Flag antibodies (left), and the glucose uptake was measured (right). F-G, HepG2 cells were transfected with IR-Flag plus siSIRT1 (F), or plus SIRT1-HA (G), and after 48 h, cells were treated with Me-Trp for 1 h as indicated. The phosphorylation levels of IR, AKT, and AS160 after insulin stimulation were detected by western blot

    Article Snippet: Antibodies and reagents Antibodies against p-IR Tyr1189/1190 (#3024), IR (#3025), p-AKT The308 (#13038), AKT (#4685), p-AS160 Thr462 (#8881), AS160 (#2670) were purchased from Cell Signaling Technology (Massachusettes, USA).

    Techniques: Inhibition, Transfection, Western Blot, Co-Immunoprecipitation Assay, Immunoprecipitation

    SCE regulates AKT/mTOR and its downstream effectors in myotubes. (A) C2C12 myoblasts were induced to differentiate in a DMEM containing 2% horse serum, treated for 5 days with different concentration of SCE (1, 5 and 10 ng/ml) and analyzed using western blotting (left). Quantification of protein expression levels (n=3 per group) (right). **P<0.01 and ***P<0.001 vs. the control. (B) Cells were treated with 10 ng/ml SCE in DM for 1, 3 and 5 days and western blotting was performed using the indicated antibodies (left). Quantification of protein expression levels (n=3 per group) (right). *P<0.05, **P<0.01 and ***P<0.001 vs. the DMSO; #P<0.05, ##P<0.01 and ###P<0.001 vs. the DMSO at the indicated time points. SCE, Saururus chinensis (Lour.) Baill. extract; p-, phosphorylated; p70S6K1, ribosomal protein S6 kinase B1.

    Journal: Molecular Medicine Reports

    Article Title: Saururus chinensis (Lour.) Baill. extract promotes skeletal muscle cell differentiation by positively regulating mitochondrial biogenesis and AKT/mTOR signaling in vitro

    doi: 10.3892/mmr.2024.13250

    Figure Lengend Snippet: SCE regulates AKT/mTOR and its downstream effectors in myotubes. (A) C2C12 myoblasts were induced to differentiate in a DMEM containing 2% horse serum, treated for 5 days with different concentration of SCE (1, 5 and 10 ng/ml) and analyzed using western blotting (left). Quantification of protein expression levels (n=3 per group) (right). **P<0.01 and ***P<0.001 vs. the control. (B) Cells were treated with 10 ng/ml SCE in DM for 1, 3 and 5 days and western blotting was performed using the indicated antibodies (left). Quantification of protein expression levels (n=3 per group) (right). *P<0.05, **P<0.01 and ***P<0.001 vs. the DMSO; #P<0.05, ##P<0.01 and ###P<0.001 vs. the DMSO at the indicated time points. SCE, Saururus chinensis (Lour.) Baill. extract; p-, phosphorylated; p70S6K1, ribosomal protein S6 kinase B1.

    Article Snippet: Specific antibodies against myosin heavy chain (MyHC; 1:500; cat. no. sc-376157), myogenic differentiation 1 (MyoD; 1:1,000; cat. no. sc-377460), myogenin and peroxisome proliferator-activated receptor-gamma coactivator-1 α (PGC-1α; 1:1,000; cat. no. sc-518038) were obtained from Santa Cruz Biotechnology, Inc. Antibodies against non-phospho (active) β-catenin (1:1,000; cat. no. 8814), β-catenin (1:1,000; cat. no. 9582), phospho-AMPK (1:1,000; cat. no. 2535), AMPK (1:1,000; cat. no. 2532), phospho-AKT (1:1,000; cat. no. 9271), AKT (1:1,000; cat. no. 9272), phospho-mTOR (1:1,000; cat. no. 2971), mTOR (1:1,000; cat. no. 2983), phospho-ribosomal protein S6 kinase B1(p70S6K1) (1:1,000; cat. no. 9234), p70S6K1 (1:1,000; cat. no. 2708) and glyceraldehyde 3-phosphate dehydrogenase (GAPDH; 1:1,000; cat. no. 2118) were purchased from Cell Signaling Technology, Inc.

    Techniques: Concentration Assay, Western Blot, Expressing

    Recombinant adenovirus enhancing apoptosis through PI3K/AKT-caspase-3 ameliorates resistance to DDP on SKOV3 cells. (A) The representative images of the Annexin V-APC staining assay. (B) Recombinant adenovirus and/or DDP promoted the apoptosis of ovarian cancer cells and the apoptosis rate in combination group was significantly higher than that in DDP group (n=4 in each group). (C) PI3K was significantly suppressed by recombinant adenovirus and/or DDP and Ad-siERCC1 could greatly enhanced the effect of DDP (n=4 in each group). (D) AKT was significantly suppressed by recombinant adenovirus and (or) DDP and Ad-siERCC1 could greatly enhanced the effect of DDP (n=4 in each group). (E) Procaspase-3 was significantly reduced after recombinant adenovirus and/or DDP incubation, whereas cleaved caspase-3 was considerably increased (n=4 in each group). Data are shown as the mean ± SEM. *P<0.05, **P<0.01, ***P<0.001 vs. corresponding controls; # P<0.05, ## P<0.01, ### P<0.001 vs. DDP groups, & P<0.05, &&& P<0.001 vs. DDP combined with Ad-NC groups. DDP, cisplatin; si, short interfering; NC, negative control; p-. phosphorylated.

    Journal: Molecular Medicine Reports

    Article Title: Dual‑regulated oncolytic adenovirus carrying ERCC1 ‑siRNA gene possesses potent antitumor effect on ovarian cancer cells

    doi: 10.3892/mmr.2024.13245

    Figure Lengend Snippet: Recombinant adenovirus enhancing apoptosis through PI3K/AKT-caspase-3 ameliorates resistance to DDP on SKOV3 cells. (A) The representative images of the Annexin V-APC staining assay. (B) Recombinant adenovirus and/or DDP promoted the apoptosis of ovarian cancer cells and the apoptosis rate in combination group was significantly higher than that in DDP group (n=4 in each group). (C) PI3K was significantly suppressed by recombinant adenovirus and/or DDP and Ad-siERCC1 could greatly enhanced the effect of DDP (n=4 in each group). (D) AKT was significantly suppressed by recombinant adenovirus and (or) DDP and Ad-siERCC1 could greatly enhanced the effect of DDP (n=4 in each group). (E) Procaspase-3 was significantly reduced after recombinant adenovirus and/or DDP incubation, whereas cleaved caspase-3 was considerably increased (n=4 in each group). Data are shown as the mean ± SEM. *P<0.05, **P<0.01, ***P<0.001 vs. corresponding controls; # P<0.05, ## P<0.01, ### P<0.001 vs. DDP groups, & P<0.05, &&& P<0.001 vs. DDP combined with Ad-NC groups. DDP, cisplatin; si, short interfering; NC, negative control; p-. phosphorylated.

    Article Snippet: The membranes were incubated with the following primary antibodies: anti-PI3K (1:1,000; cat. no. 4257; Cell Signaling Technology, Inc.), phosphorylated (p)-Akt (Ser473; 1:1,000; cat. no. 4060; Cell Signaling Technology, Inc.), anti-AKT (1:1,000; cat. no. ab179463; Abcam), anti-caspase-3 (1:1,000; cat. no. sc-7272; Santa Cruz Biotechnology, Inc.), cleaved caspase-3 (1:1,000; cat. no. 9661S; Cell Signaling Technology, Inc.), GAPDH (1:2,000; cat. no. sc-32233; Santa Cruz Biotechnology), β-Actin (1:2,000; cat. no. sc-8432; Santa Cruz Biotechnology).

    Techniques: Recombinant, Staining, Incubation, Negative Control