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ns11021  (Tocris)


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    Structured Review

    Tocris ns11021
    a Dose-response curves of BAY1000493, BAY2586116, A293, and A1899 on TASK-1 homodimers (blue) or after co-expression with TASK-5 (red) and c in comparison with the putative pore facing TASK-5 L122A mutant (light red). The IC 50 was determined from Hill plots. Numbers of biological replicates are given in brackets. b Fold-change in IC 50 of respective compounds for TASK-1/5 versus TASK-1. d Fold-change in IC 50 of heteromers containing the TASK-5 L122A mutant, compared to wild-type TASK-5 heterodimers. e Block of TASK-3 (green) or heteromeric TASK-3/5 channels (red) by 5 µM ruthenium red (RR), recorded by applying voltage-steps to +40 mV. f Block of TASK-3 (green) and TASK-3/5 (red, left) or TASK-1 (blue) and TASK-1/5 (red, right) currents by 5 µM RR. g Activation of TASK-1 (blue) or heteromeric TASK-1/5 channels (red) by 20 µM PD118057, recorded by applying voltage-steps to +40 mV. Activation of TASK-1 (blue) or TASK-1/5 currents (red) by 20 µM PD118057. Significance was probed by comparing TASK-1 with TASK-1/5. h Activation of TASK-1 and TASK-1/5 currents by ML67-33, NS3623, BL-1249, or <t>NS11021.</t> Significance was probed by comparing TASK-1 with TASK-1/5. Data are presented as mean ± s.e.m. Significance was probed using two-sided unpaired Student’s t -test ( g ) or two-sided Mann–Whitney U-test ( h ), p -values are given within the graphs. Data were considered as significant with a confidence interval of 95% ( p < 0.05). Source data are provided as a Source Data file.
    Ns11021, supplied by Tocris, used in various techniques. Bioz Stars score: 93/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ns11021/product/Tocris
    Average 93 stars, based on 27 article reviews
    ns11021 - by Bioz Stars, 2026-03
    93/100 stars

    Images

    1) Product Images from "Potassium channel TASK-5 forms functional heterodimers with TASK-1 and TASK-3 to break its silence"

    Article Title: Potassium channel TASK-5 forms functional heterodimers with TASK-1 and TASK-3 to break its silence

    Journal: Nature Communications

    doi: 10.1038/s41467-024-51288-8

    a Dose-response curves of BAY1000493, BAY2586116, A293, and A1899 on TASK-1 homodimers (blue) or after co-expression with TASK-5 (red) and c in comparison with the putative pore facing TASK-5 L122A mutant (light red). The IC 50 was determined from Hill plots. Numbers of biological replicates are given in brackets. b Fold-change in IC 50 of respective compounds for TASK-1/5 versus TASK-1. d Fold-change in IC 50 of heteromers containing the TASK-5 L122A mutant, compared to wild-type TASK-5 heterodimers. e Block of TASK-3 (green) or heteromeric TASK-3/5 channels (red) by 5 µM ruthenium red (RR), recorded by applying voltage-steps to +40 mV. f Block of TASK-3 (green) and TASK-3/5 (red, left) or TASK-1 (blue) and TASK-1/5 (red, right) currents by 5 µM RR. g Activation of TASK-1 (blue) or heteromeric TASK-1/5 channels (red) by 20 µM PD118057, recorded by applying voltage-steps to +40 mV. Activation of TASK-1 (blue) or TASK-1/5 currents (red) by 20 µM PD118057. Significance was probed by comparing TASK-1 with TASK-1/5. h Activation of TASK-1 and TASK-1/5 currents by ML67-33, NS3623, BL-1249, or NS11021. Significance was probed by comparing TASK-1 with TASK-1/5. Data are presented as mean ± s.e.m. Significance was probed using two-sided unpaired Student’s t -test ( g ) or two-sided Mann–Whitney U-test ( h ), p -values are given within the graphs. Data were considered as significant with a confidence interval of 95% ( p < 0.05). Source data are provided as a Source Data file.
    Figure Legend Snippet: a Dose-response curves of BAY1000493, BAY2586116, A293, and A1899 on TASK-1 homodimers (blue) or after co-expression with TASK-5 (red) and c in comparison with the putative pore facing TASK-5 L122A mutant (light red). The IC 50 was determined from Hill plots. Numbers of biological replicates are given in brackets. b Fold-change in IC 50 of respective compounds for TASK-1/5 versus TASK-1. d Fold-change in IC 50 of heteromers containing the TASK-5 L122A mutant, compared to wild-type TASK-5 heterodimers. e Block of TASK-3 (green) or heteromeric TASK-3/5 channels (red) by 5 µM ruthenium red (RR), recorded by applying voltage-steps to +40 mV. f Block of TASK-3 (green) and TASK-3/5 (red, left) or TASK-1 (blue) and TASK-1/5 (red, right) currents by 5 µM RR. g Activation of TASK-1 (blue) or heteromeric TASK-1/5 channels (red) by 20 µM PD118057, recorded by applying voltage-steps to +40 mV. Activation of TASK-1 (blue) or TASK-1/5 currents (red) by 20 µM PD118057. Significance was probed by comparing TASK-1 with TASK-1/5. h Activation of TASK-1 and TASK-1/5 currents by ML67-33, NS3623, BL-1249, or NS11021. Significance was probed by comparing TASK-1 with TASK-1/5. Data are presented as mean ± s.e.m. Significance was probed using two-sided unpaired Student’s t -test ( g ) or two-sided Mann–Whitney U-test ( h ), p -values are given within the graphs. Data were considered as significant with a confidence interval of 95% ( p < 0.05). Source data are provided as a Source Data file.

    Techniques Used: Expressing, Comparison, Mutagenesis, Blocking Assay, Activation Assay, MANN-WHITNEY



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    a Dose-response curves of BAY1000493, BAY2586116, A293, and A1899 on TASK-1 homodimers (blue) or after co-expression with TASK-5 (red) and c in comparison with the putative pore facing TASK-5 L122A mutant (light red). The IC 50 was determined from Hill plots. Numbers of biological replicates are given in brackets. b Fold-change in IC 50 of respective compounds for TASK-1/5 versus TASK-1. d Fold-change in IC 50 of heteromers containing the TASK-5 L122A mutant, compared to wild-type TASK-5 heterodimers. e Block of TASK-3 (green) or heteromeric TASK-3/5 channels (red) by 5 µM ruthenium red (RR), recorded by applying voltage-steps to +40 mV. f Block of TASK-3 (green) and TASK-3/5 (red, left) or TASK-1 (blue) and TASK-1/5 (red, right) currents by 5 µM RR. g Activation of TASK-1 (blue) or heteromeric TASK-1/5 channels (red) by 20 µM PD118057, recorded by applying voltage-steps to +40 mV. Activation of TASK-1 (blue) or TASK-1/5 currents (red) by 20 µM PD118057. Significance was probed by comparing TASK-1 with TASK-1/5. h Activation of TASK-1 and TASK-1/5 currents by ML67-33, NS3623, BL-1249, or <t>NS11021.</t> Significance was probed by comparing TASK-1 with TASK-1/5. Data are presented as mean ± s.e.m. Significance was probed using two-sided unpaired Student’s t -test ( g ) or two-sided Mann–Whitney U-test ( h ), p -values are given within the graphs. Data were considered as significant with a confidence interval of 95% ( p < 0.05). Source data are provided as a Source Data file.
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    a Dose-response curves of BAY1000493, BAY2586116, A293, and A1899 on TASK-1 homodimers (blue) or after co-expression with TASK-5 (red) and c in comparison with the putative pore facing TASK-5 L122A mutant (light red). The IC 50 was determined from Hill plots. Numbers of biological replicates are given in brackets. b Fold-change in IC 50 of respective compounds for TASK-1/5 versus TASK-1. d Fold-change in IC 50 of heteromers containing the TASK-5 L122A mutant, compared to wild-type TASK-5 heterodimers. e Block of TASK-3 (green) or heteromeric TASK-3/5 channels (red) by 5 µM ruthenium red (RR), recorded by applying voltage-steps to +40 mV. f Block of TASK-3 (green) and TASK-3/5 (red, left) or TASK-1 (blue) and TASK-1/5 (red, right) currents by 5 µM RR. g Activation of TASK-1 (blue) or heteromeric TASK-1/5 channels (red) by 20 µM PD118057, recorded by applying voltage-steps to +40 mV. Activation of TASK-1 (blue) or TASK-1/5 currents (red) by 20 µM PD118057. Significance was probed by comparing TASK-1 with TASK-1/5. h Activation of TASK-1 and TASK-1/5 currents by ML67-33, NS3623, BL-1249, or <t>NS11021.</t> Significance was probed by comparing TASK-1 with TASK-1/5. Data are presented as mean ± s.e.m. Significance was probed using two-sided unpaired Student’s t -test ( g ) or two-sided Mann–Whitney U-test ( h ), p -values are given within the graphs. Data were considered as significant with a confidence interval of 95% ( p < 0.05). Source data are provided as a Source Data file.
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    a Dose-response curves of BAY1000493, BAY2586116, A293, and A1899 on TASK-1 homodimers (blue) or after co-expression with TASK-5 (red) and c in comparison with the putative pore facing TASK-5 L122A mutant (light red). The IC 50 was determined from Hill plots. Numbers of biological replicates are given in brackets. b Fold-change in IC 50 of respective compounds for TASK-1/5 versus TASK-1. d Fold-change in IC 50 of heteromers containing the TASK-5 L122A mutant, compared to wild-type TASK-5 heterodimers. e Block of TASK-3 (green) or heteromeric TASK-3/5 channels (red) by 5 µM ruthenium red (RR), recorded by applying voltage-steps to +40 mV. f Block of TASK-3 (green) and TASK-3/5 (red, left) or TASK-1 (blue) and TASK-1/5 (red, right) currents by 5 µM RR. g Activation of TASK-1 (blue) or heteromeric TASK-1/5 channels (red) by 20 µM PD118057, recorded by applying voltage-steps to +40 mV. Activation of TASK-1 (blue) or TASK-1/5 currents (red) by 20 µM PD118057. Significance was probed by comparing TASK-1 with TASK-1/5. h Activation of TASK-1 and TASK-1/5 currents by ML67-33, NS3623, BL-1249, or <t>NS11021.</t> Significance was probed by comparing TASK-1 with TASK-1/5. Data are presented as mean ± s.e.m. Significance was probed using two-sided unpaired Student’s t -test ( g ) or two-sided Mann–Whitney U-test ( h ), p -values are given within the graphs. Data were considered as significant with a confidence interval of 95% ( p < 0.05). Source data are provided as a Source Data file.
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    a Dose-response curves of BAY1000493, BAY2586116, A293, and A1899 on TASK-1 homodimers (blue) or after co-expression with TASK-5 (red) and c in comparison with the putative pore facing TASK-5 L122A mutant (light red). The IC 50 was determined from Hill plots. Numbers of biological replicates are given in brackets. b Fold-change in IC 50 of respective compounds for TASK-1/5 versus TASK-1. d Fold-change in IC 50 of heteromers containing the TASK-5 L122A mutant, compared to wild-type TASK-5 heterodimers. e Block of TASK-3 (green) or heteromeric TASK-3/5 channels (red) by 5 µM ruthenium red (RR), recorded by applying voltage-steps to +40 mV. f Block of TASK-3 (green) and TASK-3/5 (red, left) or TASK-1 (blue) and TASK-1/5 (red, right) currents by 5 µM RR. g Activation of TASK-1 (blue) or heteromeric TASK-1/5 channels (red) by 20 µM PD118057, recorded by applying voltage-steps to +40 mV. Activation of TASK-1 (blue) or TASK-1/5 currents (red) by 20 µM PD118057. Significance was probed by comparing TASK-1 with TASK-1/5. h Activation of TASK-1 and TASK-1/5 currents by ML67-33, NS3623, BL-1249, or <t>NS11021.</t> Significance was probed by comparing TASK-1 with TASK-1/5. Data are presented as mean ± s.e.m. Significance was probed using two-sided unpaired Student’s t -test ( g ) or two-sided Mann–Whitney U-test ( h ), p -values are given within the graphs. Data were considered as significant with a confidence interval of 95% ( p < 0.05). Source data are provided as a Source Data file.
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    Image Search Results


    a Dose-response curves of BAY1000493, BAY2586116, A293, and A1899 on TASK-1 homodimers (blue) or after co-expression with TASK-5 (red) and c in comparison with the putative pore facing TASK-5 L122A mutant (light red). The IC 50 was determined from Hill plots. Numbers of biological replicates are given in brackets. b Fold-change in IC 50 of respective compounds for TASK-1/5 versus TASK-1. d Fold-change in IC 50 of heteromers containing the TASK-5 L122A mutant, compared to wild-type TASK-5 heterodimers. e Block of TASK-3 (green) or heteromeric TASK-3/5 channels (red) by 5 µM ruthenium red (RR), recorded by applying voltage-steps to +40 mV. f Block of TASK-3 (green) and TASK-3/5 (red, left) or TASK-1 (blue) and TASK-1/5 (red, right) currents by 5 µM RR. g Activation of TASK-1 (blue) or heteromeric TASK-1/5 channels (red) by 20 µM PD118057, recorded by applying voltage-steps to +40 mV. Activation of TASK-1 (blue) or TASK-1/5 currents (red) by 20 µM PD118057. Significance was probed by comparing TASK-1 with TASK-1/5. h Activation of TASK-1 and TASK-1/5 currents by ML67-33, NS3623, BL-1249, or NS11021. Significance was probed by comparing TASK-1 with TASK-1/5. Data are presented as mean ± s.e.m. Significance was probed using two-sided unpaired Student’s t -test ( g ) or two-sided Mann–Whitney U-test ( h ), p -values are given within the graphs. Data were considered as significant with a confidence interval of 95% ( p < 0.05). Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Potassium channel TASK-5 forms functional heterodimers with TASK-1 and TASK-3 to break its silence

    doi: 10.1038/s41467-024-51288-8

    Figure Lengend Snippet: a Dose-response curves of BAY1000493, BAY2586116, A293, and A1899 on TASK-1 homodimers (blue) or after co-expression with TASK-5 (red) and c in comparison with the putative pore facing TASK-5 L122A mutant (light red). The IC 50 was determined from Hill plots. Numbers of biological replicates are given in brackets. b Fold-change in IC 50 of respective compounds for TASK-1/5 versus TASK-1. d Fold-change in IC 50 of heteromers containing the TASK-5 L122A mutant, compared to wild-type TASK-5 heterodimers. e Block of TASK-3 (green) or heteromeric TASK-3/5 channels (red) by 5 µM ruthenium red (RR), recorded by applying voltage-steps to +40 mV. f Block of TASK-3 (green) and TASK-3/5 (red, left) or TASK-1 (blue) and TASK-1/5 (red, right) currents by 5 µM RR. g Activation of TASK-1 (blue) or heteromeric TASK-1/5 channels (red) by 20 µM PD118057, recorded by applying voltage-steps to +40 mV. Activation of TASK-1 (blue) or TASK-1/5 currents (red) by 20 µM PD118057. Significance was probed by comparing TASK-1 with TASK-1/5. h Activation of TASK-1 and TASK-1/5 currents by ML67-33, NS3623, BL-1249, or NS11021. Significance was probed by comparing TASK-1 with TASK-1/5. Data are presented as mean ± s.e.m. Significance was probed using two-sided unpaired Student’s t -test ( g ) or two-sided Mann–Whitney U-test ( h ), p -values are given within the graphs. Data were considered as significant with a confidence interval of 95% ( p < 0.05). Source data are provided as a Source Data file.

    Article Snippet: Methoxamine hydrochloride and PD118057 were obtained from SIGMA, BAY1000493, and BAY2586116 from Bayer AG, A293, and A1899 from Sanofi GmbH, and ruthenium red, ML67-33, NS11021, BL-1249 and NS3623 from Tocris.

    Techniques: Expressing, Comparison, Mutagenesis, Blocking Assay, Activation Assay, MANN-WHITNEY