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gst(tev)-human_deptor_1-409-13s/t-a mutant (t241a,s244a,t259a,s260a,s263a,s265a,s282a,s283a,s287a, s293a,s297a,s298a,s299a) (full length 13a)  (Addgene inc)


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    Structured Review

    Addgene inc gst(tev)-human_deptor_1-409-13s/t-a mutant (t241a,s244a,t259a,s260a,s263a,s265a,s282a,s283a,s287a, s293a,s297a,s298a,s299a) (full length 13a)
    ( A ) DEPTOR deletion variants tested as inhibitors and substrates for mTORC1. ( B ) Immunoblots showing the residual phosphorylation of 4EBP1 in the presence of various DEPTOR deletion variants. Images of western blots with long (L) and short exposures (S) are shown. ( C ) and ( D ) quantification of western blots of phosphorylated 4EBP1 plotted as a fraction of the control (0 µM inhibitor) vs. inhibited (mean ± SD, n ≥ 3) and fit to a non-linear regression for all deletion variants to determine IC 50 . While all experiments were performed at 30°C, inhibition of mTORC1 by the PDZ domain was tested at 20°C for 20 min as the domain stability was low. N-terminally extended PDZ constructs that showed increased temperature stability showed no inhibition of mTORC1 . To demonstrate that the temperature difference had no effect on the inhibition, DEPTOR (WT) was tested at 20°C for mTORC1 inhibition . The data shown for DEPTOR (WT) is also part of . DEPTOR <t>13A</t> inhibition of the mTORC1 A1459P mutant is shown in . Figure 2—source data 1. Uncropped blots. Figure 2—source data 2. Data values for .
    Gst(Tev) Human Deptor 1 409 13s/T A Mutant (T241a,S244a,T259a,S260a,S263a,S265a,S282a,S283a,S287a, S293a,S297a,S298a,S299a) (Full Length 13a), supplied by Addgene inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gst(tev)-human_deptor_1-409-13s/t-a mutant (t241a,s244a,t259a,s260a,s263a,s265a,s282a,s283a,s287a, s293a,s297a,s298a,s299a) (full length 13a)/product/Addgene inc
    Average 90 stars, based on 1 article reviews
    gst(tev)-human_deptor_1-409-13s/t-a mutant (t241a,s244a,t259a,s260a,s263a,s265a,s282a,s283a,s287a, s293a,s297a,s298a,s299a) (full length 13a) - by Bioz Stars, 2026-02
    90/100 stars

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    1) Product Images from "Bipartite binding and partial inhibition links DEPTOR and mTOR in a mutually antagonistic embrace"

    Article Title: Bipartite binding and partial inhibition links DEPTOR and mTOR in a mutually antagonistic embrace

    Journal: eLife

    doi: 10.7554/eLife.68799

    ( A ) DEPTOR deletion variants tested as inhibitors and substrates for mTORC1. ( B ) Immunoblots showing the residual phosphorylation of 4EBP1 in the presence of various DEPTOR deletion variants. Images of western blots with long (L) and short exposures (S) are shown. ( C ) and ( D ) quantification of western blots of phosphorylated 4EBP1 plotted as a fraction of the control (0 µM inhibitor) vs. inhibited (mean ± SD, n ≥ 3) and fit to a non-linear regression for all deletion variants to determine IC 50 . While all experiments were performed at 30°C, inhibition of mTORC1 by the PDZ domain was tested at 20°C for 20 min as the domain stability was low. N-terminally extended PDZ constructs that showed increased temperature stability showed no inhibition of mTORC1 . To demonstrate that the temperature difference had no effect on the inhibition, DEPTOR (WT) was tested at 20°C for mTORC1 inhibition . The data shown for DEPTOR (WT) is also part of . DEPTOR 13A inhibition of the mTORC1 A1459P mutant is shown in . Figure 2—source data 1. Uncropped blots. Figure 2—source data 2. Data values for .
    Figure Legend Snippet: ( A ) DEPTOR deletion variants tested as inhibitors and substrates for mTORC1. ( B ) Immunoblots showing the residual phosphorylation of 4EBP1 in the presence of various DEPTOR deletion variants. Images of western blots with long (L) and short exposures (S) are shown. ( C ) and ( D ) quantification of western blots of phosphorylated 4EBP1 plotted as a fraction of the control (0 µM inhibitor) vs. inhibited (mean ± SD, n ≥ 3) and fit to a non-linear regression for all deletion variants to determine IC 50 . While all experiments were performed at 30°C, inhibition of mTORC1 by the PDZ domain was tested at 20°C for 20 min as the domain stability was low. N-terminally extended PDZ constructs that showed increased temperature stability showed no inhibition of mTORC1 . To demonstrate that the temperature difference had no effect on the inhibition, DEPTOR (WT) was tested at 20°C for mTORC1 inhibition . The data shown for DEPTOR (WT) is also part of . DEPTOR 13A inhibition of the mTORC1 A1459P mutant is shown in . Figure 2—source data 1. Uncropped blots. Figure 2—source data 2. Data values for .

    Techniques Used: Western Blot, Phospho-proteomics, Control, Inhibition, Construct, Mutagenesis

    ( A ) The PDZ construct (324-409) was extended at the N-terminus to encompass residues 305–409 or 315–409 in order to obtain a more stable construct that could be used for assays at 30°C. No inhibition of mTORC1 kinase activity was observed in a western blot experiment with these two PDZ constructs at 30°C. ( B ) DEPTOR inhibition of mTORC1 was tested at 20°C (as compared with the results at 30°C, as shown in ) via western blot experiment to allow a direct comparison with the inhibitory properties of temperature-sensitive DEPTOR PDZ domain. The data (mean ± SD, n ≥ 3) were fit by a nonlinear regression to determine IC 50 . ( C ) DEPTOR 13A inhibition of the mTORC1-A1459P mutant phosphorylating GST-S6K 367-404 peptide measured by western blots. Band intensities were normalized to the control (0 µM DEPTOR). The data (mean ± SD, n = 3) were fitted. ( D ) The tandem DEPDEP and the PDZ domain are not substrates of mTORC1. No phosphorylation is observed in a Phos-tag SDS PAGE experiment. ( E ) DEPTOR as an mTORC1 substrate was investigated via Phos-tag SDS PAGE. DEPDEP-linker construct (residues 1–323) is phosphorylated slower than the full-length DEPTOR (WT), suggesting that the PDZ domain helps successful interaction at the FRB and active site (one representative of a triplicate experiment is shown). Figure 2—figure supplement 1—source data 1. Uncropped stained gels. Figure 2—figure supplement 1—source data 2. Data values.
    Figure Legend Snippet: ( A ) The PDZ construct (324-409) was extended at the N-terminus to encompass residues 305–409 or 315–409 in order to obtain a more stable construct that could be used for assays at 30°C. No inhibition of mTORC1 kinase activity was observed in a western blot experiment with these two PDZ constructs at 30°C. ( B ) DEPTOR inhibition of mTORC1 was tested at 20°C (as compared with the results at 30°C, as shown in ) via western blot experiment to allow a direct comparison with the inhibitory properties of temperature-sensitive DEPTOR PDZ domain. The data (mean ± SD, n ≥ 3) were fit by a nonlinear regression to determine IC 50 . ( C ) DEPTOR 13A inhibition of the mTORC1-A1459P mutant phosphorylating GST-S6K 367-404 peptide measured by western blots. Band intensities were normalized to the control (0 µM DEPTOR). The data (mean ± SD, n = 3) were fitted. ( D ) The tandem DEPDEP and the PDZ domain are not substrates of mTORC1. No phosphorylation is observed in a Phos-tag SDS PAGE experiment. ( E ) DEPTOR as an mTORC1 substrate was investigated via Phos-tag SDS PAGE. DEPDEP-linker construct (residues 1–323) is phosphorylated slower than the full-length DEPTOR (WT), suggesting that the PDZ domain helps successful interaction at the FRB and active site (one representative of a triplicate experiment is shown). Figure 2—figure supplement 1—source data 1. Uncropped stained gels. Figure 2—figure supplement 1—source data 2. Data values.

    Techniques Used: Construct, Inhibition, Activity Assay, Western Blot, Comparison, Mutagenesis, Control, Phospho-proteomics, SDS Page, Staining


    Figure Legend Snippet:

    Techniques Used: Recombinant, Plasmid Preparation, Variant Assay, Mutagenesis, Protease Inhibitor, Staining, Expressing, Software, Pore Size



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    ( A ) DEPTOR deletion variants tested as inhibitors and substrates for mTORC1. ( B ) Immunoblots showing the residual phosphorylation of 4EBP1 in the presence of various DEPTOR deletion variants. Images of western blots with long (L) and short exposures (S) are shown. ( C ) and ( D ) quantification of western blots of phosphorylated 4EBP1 plotted as a fraction of the control (0 µM inhibitor) vs. inhibited (mean ± SD, n ≥ 3) and fit to a non-linear regression for all deletion variants to determine IC 50 . While all experiments were performed at 30°C, inhibition of mTORC1 by the PDZ domain was tested at 20°C for 20 min as the domain stability was low. N-terminally extended PDZ constructs that showed increased temperature stability showed no inhibition of mTORC1 . To demonstrate that the temperature difference had no effect on the inhibition, DEPTOR (WT) was tested at 20°C for mTORC1 inhibition . The data shown for DEPTOR (WT) is also part of . DEPTOR <t>13A</t> inhibition of the mTORC1 A1459P mutant is shown in . Figure 2—source data 1. Uncropped blots. Figure 2—source data 2. Data values for .
    Gst(Tev) Human Deptor 1 409 13s/T A Mutant (T241a,S244a,T259a,S260a,S263a,S265a,S282a,S283a,S287a, S293a,S297a,S298a,S299a) (Full Length 13a), supplied by Addgene inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gst(tev)-human_deptor_1-409-13s/t-a mutant (t241a,s244a,t259a,s260a,s263a,s265a,s282a,s283a,s287a, s293a,s297a,s298a,s299a) (full length 13a)/product/Addgene inc
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    ( A ) DEPTOR deletion variants tested as inhibitors and substrates for mTORC1. ( B ) Immunoblots showing the residual phosphorylation of 4EBP1 in the presence of various DEPTOR deletion variants. Images of western blots with long (L) and short exposures (S) are shown. ( C ) and ( D ) quantification of western blots of phosphorylated 4EBP1 plotted as a fraction of the control (0 µM inhibitor) vs. inhibited (mean ± SD, n ≥ 3) and fit to a non-linear regression for all deletion variants to determine IC 50 . While all experiments were performed at 30°C, inhibition of mTORC1 by the PDZ domain was tested at 20°C for 20 min as the domain stability was low. N-terminally extended PDZ constructs that showed increased temperature stability showed no inhibition of mTORC1 . To demonstrate that the temperature difference had no effect on the inhibition, DEPTOR (WT) was tested at 20°C for mTORC1 inhibition . The data shown for DEPTOR (WT) is also part of . DEPTOR <t>13A</t> inhibition of the mTORC1 A1459P mutant is shown in . Figure 2—source data 1. Uncropped blots. Figure 2—source data 2. Data values for .
    Full Length 13a, supplied by Addgene inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    ( A ) DEPTOR deletion variants tested as inhibitors and substrates for mTORC1. ( B ) Immunoblots showing the residual phosphorylation of 4EBP1 in the presence of various DEPTOR deletion variants. Images of western blots with long (L) and short exposures (S) are shown. ( C ) and ( D ) quantification of western blots of phosphorylated 4EBP1 plotted as a fraction of the control (0 µM inhibitor) vs. inhibited (mean ± SD, n ≥ 3) and fit to a non-linear regression for all deletion variants to determine IC 50 . While all experiments were performed at 30°C, inhibition of mTORC1 by the PDZ domain was tested at 20°C for 20 min as the domain stability was low. N-terminally extended PDZ constructs that showed increased temperature stability showed no inhibition of mTORC1 . To demonstrate that the temperature difference had no effect on the inhibition, DEPTOR (WT) was tested at 20°C for mTORC1 inhibition . The data shown for DEPTOR (WT) is also part of . DEPTOR 13A inhibition of the mTORC1 A1459P mutant is shown in . Figure 2—source data 1. Uncropped blots. Figure 2—source data 2. Data values for .

    Journal: eLife

    Article Title: Bipartite binding and partial inhibition links DEPTOR and mTOR in a mutually antagonistic embrace

    doi: 10.7554/eLife.68799

    Figure Lengend Snippet: ( A ) DEPTOR deletion variants tested as inhibitors and substrates for mTORC1. ( B ) Immunoblots showing the residual phosphorylation of 4EBP1 in the presence of various DEPTOR deletion variants. Images of western blots with long (L) and short exposures (S) are shown. ( C ) and ( D ) quantification of western blots of phosphorylated 4EBP1 plotted as a fraction of the control (0 µM inhibitor) vs. inhibited (mean ± SD, n ≥ 3) and fit to a non-linear regression for all deletion variants to determine IC 50 . While all experiments were performed at 30°C, inhibition of mTORC1 by the PDZ domain was tested at 20°C for 20 min as the domain stability was low. N-terminally extended PDZ constructs that showed increased temperature stability showed no inhibition of mTORC1 . To demonstrate that the temperature difference had no effect on the inhibition, DEPTOR (WT) was tested at 20°C for mTORC1 inhibition . The data shown for DEPTOR (WT) is also part of . DEPTOR 13A inhibition of the mTORC1 A1459P mutant is shown in . Figure 2—source data 1. Uncropped blots. Figure 2—source data 2. Data values for .

    Article Snippet: Recombinant DNA reagent , pOPL139 (plasmid) , This paper , , GST(tev)-Human_DEPTOR_1-409-13S/T-A mutant (T241A,S244A,T259A,S260A,S263A,S265A,S282A,S283A,S287A, S293A,S297A,S298A,S299A) (Full length 13A), in pOPTG (PCR-ed from Addgene clone 21702) (Available from RLW lab).

    Techniques: Western Blot, Phospho-proteomics, Control, Inhibition, Construct, Mutagenesis

    ( A ) The PDZ construct (324-409) was extended at the N-terminus to encompass residues 305–409 or 315–409 in order to obtain a more stable construct that could be used for assays at 30°C. No inhibition of mTORC1 kinase activity was observed in a western blot experiment with these two PDZ constructs at 30°C. ( B ) DEPTOR inhibition of mTORC1 was tested at 20°C (as compared with the results at 30°C, as shown in ) via western blot experiment to allow a direct comparison with the inhibitory properties of temperature-sensitive DEPTOR PDZ domain. The data (mean ± SD, n ≥ 3) were fit by a nonlinear regression to determine IC 50 . ( C ) DEPTOR 13A inhibition of the mTORC1-A1459P mutant phosphorylating GST-S6K 367-404 peptide measured by western blots. Band intensities were normalized to the control (0 µM DEPTOR). The data (mean ± SD, n = 3) were fitted. ( D ) The tandem DEPDEP and the PDZ domain are not substrates of mTORC1. No phosphorylation is observed in a Phos-tag SDS PAGE experiment. ( E ) DEPTOR as an mTORC1 substrate was investigated via Phos-tag SDS PAGE. DEPDEP-linker construct (residues 1–323) is phosphorylated slower than the full-length DEPTOR (WT), suggesting that the PDZ domain helps successful interaction at the FRB and active site (one representative of a triplicate experiment is shown). Figure 2—figure supplement 1—source data 1. Uncropped stained gels. Figure 2—figure supplement 1—source data 2. Data values.

    Journal: eLife

    Article Title: Bipartite binding and partial inhibition links DEPTOR and mTOR in a mutually antagonistic embrace

    doi: 10.7554/eLife.68799

    Figure Lengend Snippet: ( A ) The PDZ construct (324-409) was extended at the N-terminus to encompass residues 305–409 or 315–409 in order to obtain a more stable construct that could be used for assays at 30°C. No inhibition of mTORC1 kinase activity was observed in a western blot experiment with these two PDZ constructs at 30°C. ( B ) DEPTOR inhibition of mTORC1 was tested at 20°C (as compared with the results at 30°C, as shown in ) via western blot experiment to allow a direct comparison with the inhibitory properties of temperature-sensitive DEPTOR PDZ domain. The data (mean ± SD, n ≥ 3) were fit by a nonlinear regression to determine IC 50 . ( C ) DEPTOR 13A inhibition of the mTORC1-A1459P mutant phosphorylating GST-S6K 367-404 peptide measured by western blots. Band intensities were normalized to the control (0 µM DEPTOR). The data (mean ± SD, n = 3) were fitted. ( D ) The tandem DEPDEP and the PDZ domain are not substrates of mTORC1. No phosphorylation is observed in a Phos-tag SDS PAGE experiment. ( E ) DEPTOR as an mTORC1 substrate was investigated via Phos-tag SDS PAGE. DEPDEP-linker construct (residues 1–323) is phosphorylated slower than the full-length DEPTOR (WT), suggesting that the PDZ domain helps successful interaction at the FRB and active site (one representative of a triplicate experiment is shown). Figure 2—figure supplement 1—source data 1. Uncropped stained gels. Figure 2—figure supplement 1—source data 2. Data values.

    Article Snippet: Recombinant DNA reagent , pOPL139 (plasmid) , This paper , , GST(tev)-Human_DEPTOR_1-409-13S/T-A mutant (T241A,S244A,T259A,S260A,S263A,S265A,S282A,S283A,S287A, S293A,S297A,S298A,S299A) (Full length 13A), in pOPTG (PCR-ed from Addgene clone 21702) (Available from RLW lab).

    Techniques: Construct, Inhibition, Activity Assay, Western Blot, Comparison, Mutagenesis, Control, Phospho-proteomics, SDS Page, Staining

    Journal: eLife

    Article Title: Bipartite binding and partial inhibition links DEPTOR and mTOR in a mutually antagonistic embrace

    doi: 10.7554/eLife.68799

    Figure Lengend Snippet:

    Article Snippet: Recombinant DNA reagent , pOPL139 (plasmid) , This paper , , GST(tev)-Human_DEPTOR_1-409-13S/T-A mutant (T241A,S244A,T259A,S260A,S263A,S265A,S282A,S283A,S287A, S293A,S297A,S298A,S299A) (Full length 13A), in pOPTG (PCR-ed from Addgene clone 21702) (Available from RLW lab).

    Techniques: Recombinant, Plasmid Preparation, Variant Assay, Mutagenesis, Protease Inhibitor, Staining, Expressing, Software, Pore Size