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sec system mals qels modules  (Waters Corporation)


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    Waters Corporation sec system mals qels modules
    MORC2 is a GHKL-type ATPase. a Domain organization of human MORC2. The GHKL ATP binding domain and the transducer-like domain (trans.) together form the ATPase module, as marked. CC indicates a predicted coiled coil; CW indicates a CW-type zinc finger domain; TCD indicates a predicted tudor-chromodomain. b Fitted T m s derived from differential scanning fluorimetry (DSF) for several MORC2 variants at 5 µM, in the absence (solid bar) and presence (striped bar) of 2 mM Mg-AMPPNP. This non-hydrolysable ATP analog significantly increases the thermal stability of wild-type (WT) MORC2(1–603), while the N39A point mutant abrogates binding and WT MORC2(1–282) is stabilized to a much smaller extent than WT MORC2(1–603). Quoted T m values are an average of at least two replicates; note that the deviation between these measurements was <0.2 °C in all cases. c Portions of <t>overlaid</t> <t>SEC-MALS</t> UV traces for 40 µM WT MORC2(1–603) in the absence (solid line) and presence (dashed line) of 2 mM Mg-AMPPNP. The MALS data across the center of the major peaks in each case are shown on the right-hand axis, and are consistent with monomeric (expected mass: 70 kDa) and dimeric (expected mass: 140 kDa) species for the apo and AMPPNP-bound protein, respectively. Also shown are the fitted hydrodynamic radii obtained from <t>QELS</t> analysis of the peaks. The peak at 48 min in the AMPPNP-treated trace is the elution of excess (unbound) nucleotide. d Rate of ATP hydrolysis by wild-type (WT) and N39A MORC2(1–603) variants at 37 °C in the presence of 7.5 mM ATP, measured using an NADH-coupled continuous assay. Error bars represent standard deviation between measurements; n = 8 (WT), n = 7 (N39A). e Steady-state ATPase activity of 4 µM WT MORC2(1–603) at 37 °C fitted to a model of Michaelis–Menten kinetics
    Sec System Mals Qels Modules, supplied by Waters Corporation, 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/product/mals+qels+modules/pmc05811534-394-9-11?v=Waters+Corporation
    Average 90 stars, based on 1 article reviews
    sec system mals qels modules - by Bioz Stars, 2026-07
    90/100 stars

    Images

    1) Product Images from "Neuropathic MORC2 mutations perturb GHKL ATPase dimerization dynamics and epigenetic silencing by multiple structural mechanisms"

    Article Title: Neuropathic MORC2 mutations perturb GHKL ATPase dimerization dynamics and epigenetic silencing by multiple structural mechanisms

    Journal: Nature Communications

    doi: 10.1038/s41467-018-03045-x

    MORC2 is a GHKL-type ATPase. a Domain organization of human MORC2. The GHKL ATP binding domain and the transducer-like domain (trans.) together form the ATPase module, as marked. CC indicates a predicted coiled coil; CW indicates a CW-type zinc finger domain; TCD indicates a predicted tudor-chromodomain. b Fitted T m s derived from differential scanning fluorimetry (DSF) for several MORC2 variants at 5 µM, in the absence (solid bar) and presence (striped bar) of 2 mM Mg-AMPPNP. This non-hydrolysable ATP analog significantly increases the thermal stability of wild-type (WT) MORC2(1–603), while the N39A point mutant abrogates binding and WT MORC2(1–282) is stabilized to a much smaller extent than WT MORC2(1–603). Quoted T m values are an average of at least two replicates; note that the deviation between these measurements was <0.2 °C in all cases. c Portions of overlaid SEC-MALS UV traces for 40 µM WT MORC2(1–603) in the absence (solid line) and presence (dashed line) of 2 mM Mg-AMPPNP. The MALS data across the center of the major peaks in each case are shown on the right-hand axis, and are consistent with monomeric (expected mass: 70 kDa) and dimeric (expected mass: 140 kDa) species for the apo and AMPPNP-bound protein, respectively. Also shown are the fitted hydrodynamic radii obtained from QELS analysis of the peaks. The peak at 48 min in the AMPPNP-treated trace is the elution of excess (unbound) nucleotide. d Rate of ATP hydrolysis by wild-type (WT) and N39A MORC2(1–603) variants at 37 °C in the presence of 7.5 mM ATP, measured using an NADH-coupled continuous assay. Error bars represent standard deviation between measurements; n = 8 (WT), n = 7 (N39A). e Steady-state ATPase activity of 4 µM WT MORC2(1–603) at 37 °C fitted to a model of Michaelis–Menten kinetics
    Figure Legend Snippet: MORC2 is a GHKL-type ATPase. a Domain organization of human MORC2. The GHKL ATP binding domain and the transducer-like domain (trans.) together form the ATPase module, as marked. CC indicates a predicted coiled coil; CW indicates a CW-type zinc finger domain; TCD indicates a predicted tudor-chromodomain. b Fitted T m s derived from differential scanning fluorimetry (DSF) for several MORC2 variants at 5 µM, in the absence (solid bar) and presence (striped bar) of 2 mM Mg-AMPPNP. This non-hydrolysable ATP analog significantly increases the thermal stability of wild-type (WT) MORC2(1–603), while the N39A point mutant abrogates binding and WT MORC2(1–282) is stabilized to a much smaller extent than WT MORC2(1–603). Quoted T m values are an average of at least two replicates; note that the deviation between these measurements was <0.2 °C in all cases. c Portions of overlaid SEC-MALS UV traces for 40 µM WT MORC2(1–603) in the absence (solid line) and presence (dashed line) of 2 mM Mg-AMPPNP. The MALS data across the center of the major peaks in each case are shown on the right-hand axis, and are consistent with monomeric (expected mass: 70 kDa) and dimeric (expected mass: 140 kDa) species for the apo and AMPPNP-bound protein, respectively. Also shown are the fitted hydrodynamic radii obtained from QELS analysis of the peaks. The peak at 48 min in the AMPPNP-treated trace is the elution of excess (unbound) nucleotide. d Rate of ATP hydrolysis by wild-type (WT) and N39A MORC2(1–603) variants at 37 °C in the presence of 7.5 mM ATP, measured using an NADH-coupled continuous assay. Error bars represent standard deviation between measurements; n = 8 (WT), n = 7 (N39A). e Steady-state ATPase activity of 4 µM WT MORC2(1–603) at 37 °C fitted to a model of Michaelis–Menten kinetics

    Techniques Used: Binding Assay, Derivative Assay, Mutagenesis, Standard Deviation, Activity Assay



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    sec system mals qels modules  (Waters Corporation)
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    Waters Corporation sec system mals qels modules
    MORC2 is a GHKL-type ATPase. a Domain organization of human MORC2. The GHKL ATP binding domain and the transducer-like domain (trans.) together form the ATPase module, as marked. CC indicates a predicted coiled coil; CW indicates a CW-type zinc finger domain; TCD indicates a predicted tudor-chromodomain. b Fitted T m s derived from differential scanning fluorimetry (DSF) for several MORC2 variants at 5 µM, in the absence (solid bar) and presence (striped bar) of 2 mM Mg-AMPPNP. This non-hydrolysable ATP analog significantly increases the thermal stability of wild-type (WT) MORC2(1–603), while the N39A point mutant abrogates binding and WT MORC2(1–282) is stabilized to a much smaller extent than WT MORC2(1–603). Quoted T m values are an average of at least two replicates; note that the deviation between these measurements was <0.2 °C in all cases. c Portions of <t>overlaid</t> <t>SEC-MALS</t> UV traces for 40 µM WT MORC2(1–603) in the absence (solid line) and presence (dashed line) of 2 mM Mg-AMPPNP. The MALS data across the center of the major peaks in each case are shown on the right-hand axis, and are consistent with monomeric (expected mass: 70 kDa) and dimeric (expected mass: 140 kDa) species for the apo and AMPPNP-bound protein, respectively. Also shown are the fitted hydrodynamic radii obtained from <t>QELS</t> analysis of the peaks. The peak at 48 min in the AMPPNP-treated trace is the elution of excess (unbound) nucleotide. d Rate of ATP hydrolysis by wild-type (WT) and N39A MORC2(1–603) variants at 37 °C in the presence of 7.5 mM ATP, measured using an NADH-coupled continuous assay. Error bars represent standard deviation between measurements; n = 8 (WT), n = 7 (N39A). e Steady-state ATPase activity of 4 µM WT MORC2(1–603) at 37 °C fitted to a model of Michaelis–Menten kinetics
    Sec System Mals Qels Modules, supplied by Waters Corporation, 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/product/mals+qels+modules/pmc05811534-394-9-11?v=Waters+Corporation
    Average 90 stars, based on 1 article reviews
    sec system mals qels modules - by Bioz Stars, 2026-07
    90/100 stars
    		  Buy from Supplier
    mals qels modules  (Waters Corporation)
    90
    Waters Corporation mals qels modules
    MORC2 is a GHKL-type ATPase. a Domain organization of human MORC2. The GHKL ATP binding domain and the transducer-like domain (trans.) together form the ATPase module, as marked. CC indicates a predicted coiled coil; CW indicates a CW-type zinc finger domain; TCD indicates a predicted tudor-chromodomain. b Fitted T m s derived from differential scanning fluorimetry (DSF) for several MORC2 variants at 5 µM, in the absence (solid bar) and presence (striped bar) of 2 mM Mg-AMPPNP. This non-hydrolysable ATP analog significantly increases the thermal stability of wild-type (WT) MORC2(1–603), while the N39A point mutant abrogates binding and WT MORC2(1–282) is stabilized to a much smaller extent than WT MORC2(1–603). Quoted T m values are an average of at least two replicates; note that the deviation between these measurements was <0.2 °C in all cases. c Portions of <t>overlaid</t> <t>SEC-MALS</t> UV traces for 40 µM WT MORC2(1–603) in the absence (solid line) and presence (dashed line) of 2 mM Mg-AMPPNP. The MALS data across the center of the major peaks in each case are shown on the right-hand axis, and are consistent with monomeric (expected mass: 70 kDa) and dimeric (expected mass: 140 kDa) species for the apo and AMPPNP-bound protein, respectively. Also shown are the fitted hydrodynamic radii obtained from <t>QELS</t> analysis of the peaks. The peak at 48 min in the AMPPNP-treated trace is the elution of excess (unbound) nucleotide. d Rate of ATP hydrolysis by wild-type (WT) and N39A MORC2(1–603) variants at 37 °C in the presence of 7.5 mM ATP, measured using an NADH-coupled continuous assay. Error bars represent standard deviation between measurements; n = 8 (WT), n = 7 (N39A). e Steady-state ATPase activity of 4 µM WT MORC2(1–603) at 37 °C fitted to a model of Michaelis–Menten kinetics
    Mals Qels Modules, supplied by Waters Corporation, 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/product/mals+qels+modules/pmc05811534-394-7-11?v=Waters+Corporation
    Average 90 stars, based on 1 article reviews
    mals qels modules - by Bioz Stars, 2026-07
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    MORC2 is a GHKL-type ATPase. a Domain organization of human MORC2. The GHKL ATP binding domain and the transducer-like domain (trans.) together form the ATPase module, as marked. CC indicates a predicted coiled coil; CW indicates a CW-type zinc finger domain; TCD indicates a predicted tudor-chromodomain. b Fitted T m s derived from differential scanning fluorimetry (DSF) for several MORC2 variants at 5 µM, in the absence (solid bar) and presence (striped bar) of 2 mM Mg-AMPPNP. This non-hydrolysable ATP analog significantly increases the thermal stability of wild-type (WT) MORC2(1–603), while the N39A point mutant abrogates binding and WT MORC2(1–282) is stabilized to a much smaller extent than WT MORC2(1–603). Quoted T m values are an average of at least two replicates; note that the deviation between these measurements was <0.2 °C in all cases. c Portions of overlaid SEC-MALS UV traces for 40 µM WT MORC2(1–603) in the absence (solid line) and presence (dashed line) of 2 mM Mg-AMPPNP. The MALS data across the center of the major peaks in each case are shown on the right-hand axis, and are consistent with monomeric (expected mass: 70 kDa) and dimeric (expected mass: 140 kDa) species for the apo and AMPPNP-bound protein, respectively. Also shown are the fitted hydrodynamic radii obtained from QELS analysis of the peaks. The peak at 48 min in the AMPPNP-treated trace is the elution of excess (unbound) nucleotide. d Rate of ATP hydrolysis by wild-type (WT) and N39A MORC2(1–603) variants at 37 °C in the presence of 7.5 mM ATP, measured using an NADH-coupled continuous assay. Error bars represent standard deviation between measurements; n = 8 (WT), n = 7 (N39A). e Steady-state ATPase activity of 4 µM WT MORC2(1–603) at 37 °C fitted to a model of Michaelis–Menten kinetics

    Journal: Nature Communications

    Article Title: Neuropathic MORC2 mutations perturb GHKL ATPase dimerization dynamics and epigenetic silencing by multiple structural mechanisms

    doi: 10.1038/s41467-018-03045-x

    Figure Lengend Snippet: MORC2 is a GHKL-type ATPase. a Domain organization of human MORC2. The GHKL ATP binding domain and the transducer-like domain (trans.) together form the ATPase module, as marked. CC indicates a predicted coiled coil; CW indicates a CW-type zinc finger domain; TCD indicates a predicted tudor-chromodomain. b Fitted T m s derived from differential scanning fluorimetry (DSF) for several MORC2 variants at 5 µM, in the absence (solid bar) and presence (striped bar) of 2 mM Mg-AMPPNP. This non-hydrolysable ATP analog significantly increases the thermal stability of wild-type (WT) MORC2(1–603), while the N39A point mutant abrogates binding and WT MORC2(1–282) is stabilized to a much smaller extent than WT MORC2(1–603). Quoted T m values are an average of at least two replicates; note that the deviation between these measurements was <0.2 °C in all cases. c Portions of overlaid SEC-MALS UV traces for 40 µM WT MORC2(1–603) in the absence (solid line) and presence (dashed line) of 2 mM Mg-AMPPNP. The MALS data across the center of the major peaks in each case are shown on the right-hand axis, and are consistent with monomeric (expected mass: 70 kDa) and dimeric (expected mass: 140 kDa) species for the apo and AMPPNP-bound protein, respectively. Also shown are the fitted hydrodynamic radii obtained from QELS analysis of the peaks. The peak at 48 min in the AMPPNP-treated trace is the elution of excess (unbound) nucleotide. d Rate of ATP hydrolysis by wild-type (WT) and N39A MORC2(1–603) variants at 37 °C in the presence of 7.5 mM ATP, measured using an NADH-coupled continuous assay. Error bars represent standard deviation between measurements; n = 8 (WT), n = 7 (N39A). e Steady-state ATPase activity of 4 µM WT MORC2(1–603) at 37 °C fitted to a model of Michaelis–Menten kinetics

    Article Snippet: The SEC system was coupled to both MALS and QELS modules (Wyatt Technology).

    Techniques: Binding Assay, Derivative Assay, Mutagenesis, Standard Deviation, Activity Assay