96-well pcr plates Search Results


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  • 99
    Thermo Fisher 96 well pcr plates
    96 Well Pcr Plates, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1192 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 1192 article reviews
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    99
    Millipore 96 well plates
    96 Well Plates, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3740 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad 96 well pcr plate
    96 Well Pcr Plate, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1136 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 1136 article reviews
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    99
    Eppendorf AG 96 well pcr plates
    96 Well Pcr Plates, supplied by Eppendorf AG, used in various techniques. Bioz Stars score: 99/100, based on 264 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 264 article reviews
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    Bio-Rad hard shell 96 well pcr plates
    Hard Shell 96 Well Pcr Plates, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 275 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Becton Dickinson 96 well pcr plates
    96 Well Pcr Plates, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 92/100, based on 149 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Avantor 96 well pcr plates
    Fig 4 shows examples of TSA melting curves of Pf MDH WT (dark bold lines), Pf MDH-V190W (dotted red lines), Pf MDH-E18W (dotted blue lines) and Pf MDH-E18Q (faint lines) in various buffer conditions: (a) PBS, (b) 400 mM NaCl, (c) 100 mM Na-Citrate pH 5.5 and (d) Assay Buffer (100 mM Na-Phosphate pH 7.4, 400 mM NaCl). Melting temperatures of each sample are displayed next to the respective curves. Analysis of these curves shows that Pf MDH is rather unstable in PBS (a) and requires optimized buffer conditions for further experiments. This effect is more pronounced for its mutant forms, where native oligomeric assembly has been disrupted (dotted lines). Pf MDH-E18Q mutant shows higher thermal stability, thus supporting the hypothesis that introduction of the additional hydrogen bond pair at the AB interface has had the desired stabilization effect. (b) 400 mM NaCl has significantly stabilized the wild type Pf MDH (ΔT m = 10 K), dimeric V190W mutant (ΔT m = 7 K) and tetrameric E18Q mutant (ΔT m = 8.5 K), while having minor effect of the E18W dimeric mutant (ΔT m = 2.5 K). (c) 100 mM Na-Citrate pH 5.5 significantly stabilized the wild type enzyme (ΔT m = 17.5 K) and the E18Q mutant (ΔT m = 15.5 K), while having lesser effect on V190W mutant (ΔT m = 6 K) and negligible effect on E18W (ΔT m = 0.5 K). (d) Selection of the Assay Buffer allowed further experiments to be performed for all four Pf MDH constructs used in this study in the same stabilizing buffer conditions (WT ΔT m = 13 K, V190W ΔT m = 7 K, E18W ΔT m = 5 K, E18Q ΔT m = 12.5 K). TSA assays were performed in <t>96-well</t> <t>PCR</t> plates (VWR) using SFX96 Real-Time PCR reactor (BioRad). Melting curve (in terms of increased fluorescence, RFU) of each sample was plotted against the temperature gradient (293–363 K) using BioRad SFX96 software and the temperatures of the inflection points (T m ’s) were used as indicators of the thermal stability of each sample. ΔT m ’s reflect stabilization effect of each condition compared to the control experiments performed in PBS. For more details refer to Materials and Methods section.
    96 Well Pcr Plates, supplied by Avantor, used in various techniques. Bioz Stars score: 90/100, based on 63 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Bio-Rad 96 well format microseal pcr plates
    Fig 4 shows examples of TSA melting curves of Pf MDH WT (dark bold lines), Pf MDH-V190W (dotted red lines), Pf MDH-E18W (dotted blue lines) and Pf MDH-E18Q (faint lines) in various buffer conditions: (a) PBS, (b) 400 mM NaCl, (c) 100 mM Na-Citrate pH 5.5 and (d) Assay Buffer (100 mM Na-Phosphate pH 7.4, 400 mM NaCl). Melting temperatures of each sample are displayed next to the respective curves. Analysis of these curves shows that Pf MDH is rather unstable in PBS (a) and requires optimized buffer conditions for further experiments. This effect is more pronounced for its mutant forms, where native oligomeric assembly has been disrupted (dotted lines). Pf MDH-E18Q mutant shows higher thermal stability, thus supporting the hypothesis that introduction of the additional hydrogen bond pair at the AB interface has had the desired stabilization effect. (b) 400 mM NaCl has significantly stabilized the wild type Pf MDH (ΔT m = 10 K), dimeric V190W mutant (ΔT m = 7 K) and tetrameric E18Q mutant (ΔT m = 8.5 K), while having minor effect of the E18W dimeric mutant (ΔT m = 2.5 K). (c) 100 mM Na-Citrate pH 5.5 significantly stabilized the wild type enzyme (ΔT m = 17.5 K) and the E18Q mutant (ΔT m = 15.5 K), while having lesser effect on V190W mutant (ΔT m = 6 K) and negligible effect on E18W (ΔT m = 0.5 K). (d) Selection of the Assay Buffer allowed further experiments to be performed for all four Pf MDH constructs used in this study in the same stabilizing buffer conditions (WT ΔT m = 13 K, V190W ΔT m = 7 K, E18W ΔT m = 5 K, E18Q ΔT m = 12.5 K). TSA assays were performed in <t>96-well</t> <t>PCR</t> plates (VWR) using SFX96 Real-Time PCR reactor (BioRad). Melting curve (in terms of increased fluorescence, RFU) of each sample was plotted against the temperature gradient (293–363 K) using BioRad SFX96 software and the temperatures of the inflection points (T m ’s) were used as indicators of the thermal stability of each sample. ΔT m ’s reflect stabilization effect of each condition compared to the control experiments performed in PBS. For more details refer to Materials and Methods section.
    96 Well Format Microseal Pcr Plates, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 159 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 96 stars, based on 159 article reviews
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    96 well format microseal pcr plates - by Bioz Stars, 2020-10
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    93
    Axygen 96 well pcr plates
    Fig 4 shows examples of TSA melting curves of Pf MDH WT (dark bold lines), Pf MDH-V190W (dotted red lines), Pf MDH-E18W (dotted blue lines) and Pf MDH-E18Q (faint lines) in various buffer conditions: (a) PBS, (b) 400 mM NaCl, (c) 100 mM Na-Citrate pH 5.5 and (d) Assay Buffer (100 mM Na-Phosphate pH 7.4, 400 mM NaCl). Melting temperatures of each sample are displayed next to the respective curves. Analysis of these curves shows that Pf MDH is rather unstable in PBS (a) and requires optimized buffer conditions for further experiments. This effect is more pronounced for its mutant forms, where native oligomeric assembly has been disrupted (dotted lines). Pf MDH-E18Q mutant shows higher thermal stability, thus supporting the hypothesis that introduction of the additional hydrogen bond pair at the AB interface has had the desired stabilization effect. (b) 400 mM NaCl has significantly stabilized the wild type Pf MDH (ΔT m = 10 K), dimeric V190W mutant (ΔT m = 7 K) and tetrameric E18Q mutant (ΔT m = 8.5 K), while having minor effect of the E18W dimeric mutant (ΔT m = 2.5 K). (c) 100 mM Na-Citrate pH 5.5 significantly stabilized the wild type enzyme (ΔT m = 17.5 K) and the E18Q mutant (ΔT m = 15.5 K), while having lesser effect on V190W mutant (ΔT m = 6 K) and negligible effect on E18W (ΔT m = 0.5 K). (d) Selection of the Assay Buffer allowed further experiments to be performed for all four Pf MDH constructs used in this study in the same stabilizing buffer conditions (WT ΔT m = 13 K, V190W ΔT m = 7 K, E18W ΔT m = 5 K, E18Q ΔT m = 12.5 K). TSA assays were performed in <t>96-well</t> <t>PCR</t> plates (VWR) using SFX96 Real-Time PCR reactor (BioRad). Melting curve (in terms of increased fluorescence, RFU) of each sample was plotted against the temperature gradient (293–363 K) using BioRad SFX96 software and the temperatures of the inflection points (T m ’s) were used as indicators of the thermal stability of each sample. ΔT m ’s reflect stabilization effect of each condition compared to the control experiments performed in PBS. For more details refer to Materials and Methods section.
    96 Well Pcr Plates, supplied by Axygen, used in various techniques. Bioz Stars score: 93/100, based on 84 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Stratagene 96 well pcr plates
    Fig 4 shows examples of TSA melting curves of Pf MDH WT (dark bold lines), Pf MDH-V190W (dotted red lines), Pf MDH-E18W (dotted blue lines) and Pf MDH-E18Q (faint lines) in various buffer conditions: (a) PBS, (b) 400 mM NaCl, (c) 100 mM Na-Citrate pH 5.5 and (d) Assay Buffer (100 mM Na-Phosphate pH 7.4, 400 mM NaCl). Melting temperatures of each sample are displayed next to the respective curves. Analysis of these curves shows that Pf MDH is rather unstable in PBS (a) and requires optimized buffer conditions for further experiments. This effect is more pronounced for its mutant forms, where native oligomeric assembly has been disrupted (dotted lines). Pf MDH-E18Q mutant shows higher thermal stability, thus supporting the hypothesis that introduction of the additional hydrogen bond pair at the AB interface has had the desired stabilization effect. (b) 400 mM NaCl has significantly stabilized the wild type Pf MDH (ΔT m = 10 K), dimeric V190W mutant (ΔT m = 7 K) and tetrameric E18Q mutant (ΔT m = 8.5 K), while having minor effect of the E18W dimeric mutant (ΔT m = 2.5 K). (c) 100 mM Na-Citrate pH 5.5 significantly stabilized the wild type enzyme (ΔT m = 17.5 K) and the E18Q mutant (ΔT m = 15.5 K), while having lesser effect on V190W mutant (ΔT m = 6 K) and negligible effect on E18W (ΔT m = 0.5 K). (d) Selection of the Assay Buffer allowed further experiments to be performed for all four Pf MDH constructs used in this study in the same stabilizing buffer conditions (WT ΔT m = 13 K, V190W ΔT m = 7 K, E18W ΔT m = 5 K, E18Q ΔT m = 12.5 K). TSA assays were performed in <t>96-well</t> <t>PCR</t> plates (VWR) using SFX96 Real-Time PCR reactor (BioRad). Melting curve (in terms of increased fluorescence, RFU) of each sample was plotted against the temperature gradient (293–363 K) using BioRad SFX96 software and the temperatures of the inflection points (T m ’s) were used as indicators of the thermal stability of each sample. ΔT m ’s reflect stabilization effect of each condition compared to the control experiments performed in PBS. For more details refer to Materials and Methods section.
    96 Well Pcr Plates, supplied by Stratagene, used in various techniques. Bioz Stars score: 92/100, based on 61 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    fluidigm 96 well pcr plates
    Fig 4 shows examples of TSA melting curves of Pf MDH WT (dark bold lines), Pf MDH-V190W (dotted red lines), Pf MDH-E18W (dotted blue lines) and Pf MDH-E18Q (faint lines) in various buffer conditions: (a) PBS, (b) 400 mM NaCl, (c) 100 mM Na-Citrate pH 5.5 and (d) Assay Buffer (100 mM Na-Phosphate pH 7.4, 400 mM NaCl). Melting temperatures of each sample are displayed next to the respective curves. Analysis of these curves shows that Pf MDH is rather unstable in PBS (a) and requires optimized buffer conditions for further experiments. This effect is more pronounced for its mutant forms, where native oligomeric assembly has been disrupted (dotted lines). Pf MDH-E18Q mutant shows higher thermal stability, thus supporting the hypothesis that introduction of the additional hydrogen bond pair at the AB interface has had the desired stabilization effect. (b) 400 mM NaCl has significantly stabilized the wild type Pf MDH (ΔT m = 10 K), dimeric V190W mutant (ΔT m = 7 K) and tetrameric E18Q mutant (ΔT m = 8.5 K), while having minor effect of the E18W dimeric mutant (ΔT m = 2.5 K). (c) 100 mM Na-Citrate pH 5.5 significantly stabilized the wild type enzyme (ΔT m = 17.5 K) and the E18Q mutant (ΔT m = 15.5 K), while having lesser effect on V190W mutant (ΔT m = 6 K) and negligible effect on E18W (ΔT m = 0.5 K). (d) Selection of the Assay Buffer allowed further experiments to be performed for all four Pf MDH constructs used in this study in the same stabilizing buffer conditions (WT ΔT m = 13 K, V190W ΔT m = 7 K, E18W ΔT m = 5 K, E18Q ΔT m = 12.5 K). TSA assays were performed in <t>96-well</t> <t>PCR</t> plates (VWR) using SFX96 Real-Time PCR reactor (BioRad). Melting curve (in terms of increased fluorescence, RFU) of each sample was plotted against the temperature gradient (293–363 K) using BioRad SFX96 software and the temperatures of the inflection points (T m ’s) were used as indicators of the thermal stability of each sample. ΔT m ’s reflect stabilization effect of each condition compared to the control experiments performed in PBS. For more details refer to Materials and Methods section.
    96 Well Pcr Plates, supplied by fluidigm, used in various techniques. Bioz Stars score: 91/100, based on 56 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Bio-Rad 96 well low profile pcr plates
    Fig 4 shows examples of TSA melting curves of Pf MDH WT (dark bold lines), Pf MDH-V190W (dotted red lines), Pf MDH-E18W (dotted blue lines) and Pf MDH-E18Q (faint lines) in various buffer conditions: (a) PBS, (b) 400 mM NaCl, (c) 100 mM Na-Citrate pH 5.5 and (d) Assay Buffer (100 mM Na-Phosphate pH 7.4, 400 mM NaCl). Melting temperatures of each sample are displayed next to the respective curves. Analysis of these curves shows that Pf MDH is rather unstable in PBS (a) and requires optimized buffer conditions for further experiments. This effect is more pronounced for its mutant forms, where native oligomeric assembly has been disrupted (dotted lines). Pf MDH-E18Q mutant shows higher thermal stability, thus supporting the hypothesis that introduction of the additional hydrogen bond pair at the AB interface has had the desired stabilization effect. (b) 400 mM NaCl has significantly stabilized the wild type Pf MDH (ΔT m = 10 K), dimeric V190W mutant (ΔT m = 7 K) and tetrameric E18Q mutant (ΔT m = 8.5 K), while having minor effect of the E18W dimeric mutant (ΔT m = 2.5 K). (c) 100 mM Na-Citrate pH 5.5 significantly stabilized the wild type enzyme (ΔT m = 17.5 K) and the E18Q mutant (ΔT m = 15.5 K), while having lesser effect on V190W mutant (ΔT m = 6 K) and negligible effect on E18W (ΔT m = 0.5 K). (d) Selection of the Assay Buffer allowed further experiments to be performed for all four Pf MDH constructs used in this study in the same stabilizing buffer conditions (WT ΔT m = 13 K, V190W ΔT m = 7 K, E18W ΔT m = 5 K, E18Q ΔT m = 12.5 K). TSA assays were performed in <t>96-well</t> <t>PCR</t> plates (VWR) using SFX96 Real-Time PCR reactor (BioRad). Melting curve (in terms of increased fluorescence, RFU) of each sample was plotted against the temperature gradient (293–363 K) using BioRad SFX96 software and the temperatures of the inflection points (T m ’s) were used as indicators of the thermal stability of each sample. ΔT m ’s reflect stabilization effect of each condition compared to the control experiments performed in PBS. For more details refer to Materials and Methods section.
    96 Well Low Profile Pcr Plates, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 97/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Dot Scientific 96 well pcr plates
    Fig 4 shows examples of TSA melting curves of Pf MDH WT (dark bold lines), Pf MDH-V190W (dotted red lines), Pf MDH-E18W (dotted blue lines) and Pf MDH-E18Q (faint lines) in various buffer conditions: (a) PBS, (b) 400 mM NaCl, (c) 100 mM Na-Citrate pH 5.5 and (d) Assay Buffer (100 mM Na-Phosphate pH 7.4, 400 mM NaCl). Melting temperatures of each sample are displayed next to the respective curves. Analysis of these curves shows that Pf MDH is rather unstable in PBS (a) and requires optimized buffer conditions for further experiments. This effect is more pronounced for its mutant forms, where native oligomeric assembly has been disrupted (dotted lines). Pf MDH-E18Q mutant shows higher thermal stability, thus supporting the hypothesis that introduction of the additional hydrogen bond pair at the AB interface has had the desired stabilization effect. (b) 400 mM NaCl has significantly stabilized the wild type Pf MDH (ΔT m = 10 K), dimeric V190W mutant (ΔT m = 7 K) and tetrameric E18Q mutant (ΔT m = 8.5 K), while having minor effect of the E18W dimeric mutant (ΔT m = 2.5 K). (c) 100 mM Na-Citrate pH 5.5 significantly stabilized the wild type enzyme (ΔT m = 17.5 K) and the E18Q mutant (ΔT m = 15.5 K), while having lesser effect on V190W mutant (ΔT m = 6 K) and negligible effect on E18W (ΔT m = 0.5 K). (d) Selection of the Assay Buffer allowed further experiments to be performed for all four Pf MDH constructs used in this study in the same stabilizing buffer conditions (WT ΔT m = 13 K, V190W ΔT m = 7 K, E18W ΔT m = 5 K, E18Q ΔT m = 12.5 K). TSA assays were performed in <t>96-well</t> <t>PCR</t> plates (VWR) using SFX96 Real-Time PCR reactor (BioRad). Melting curve (in terms of increased fluorescence, RFU) of each sample was plotted against the temperature gradient (293–363 K) using BioRad SFX96 software and the temperatures of the inflection points (T m ’s) were used as indicators of the thermal stability of each sample. ΔT m ’s reflect stabilization effect of each condition compared to the control experiments performed in PBS. For more details refer to Materials and Methods section.
    96 Well Pcr Plates, supplied by Dot Scientific, used in various techniques. Bioz Stars score: 92/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore 96 well pcr plates
    Fig 4 shows examples of TSA melting curves of Pf MDH WT (dark bold lines), Pf MDH-V190W (dotted red lines), Pf MDH-E18W (dotted blue lines) and Pf MDH-E18Q (faint lines) in various buffer conditions: (a) PBS, (b) 400 mM NaCl, (c) 100 mM Na-Citrate pH 5.5 and (d) Assay Buffer (100 mM Na-Phosphate pH 7.4, 400 mM NaCl). Melting temperatures of each sample are displayed next to the respective curves. Analysis of these curves shows that Pf MDH is rather unstable in PBS (a) and requires optimized buffer conditions for further experiments. This effect is more pronounced for its mutant forms, where native oligomeric assembly has been disrupted (dotted lines). Pf MDH-E18Q mutant shows higher thermal stability, thus supporting the hypothesis that introduction of the additional hydrogen bond pair at the AB interface has had the desired stabilization effect. (b) 400 mM NaCl has significantly stabilized the wild type Pf MDH (ΔT m = 10 K), dimeric V190W mutant (ΔT m = 7 K) and tetrameric E18Q mutant (ΔT m = 8.5 K), while having minor effect of the E18W dimeric mutant (ΔT m = 2.5 K). (c) 100 mM Na-Citrate pH 5.5 significantly stabilized the wild type enzyme (ΔT m = 17.5 K) and the E18Q mutant (ΔT m = 15.5 K), while having lesser effect on V190W mutant (ΔT m = 6 K) and negligible effect on E18W (ΔT m = 0.5 K). (d) Selection of the Assay Buffer allowed further experiments to be performed for all four Pf MDH constructs used in this study in the same stabilizing buffer conditions (WT ΔT m = 13 K, V190W ΔT m = 7 K, E18W ΔT m = 5 K, E18Q ΔT m = 12.5 K). TSA assays were performed in <t>96-well</t> <t>PCR</t> plates (VWR) using SFX96 Real-Time PCR reactor (BioRad). Melting curve (in terms of increased fluorescence, RFU) of each sample was plotted against the temperature gradient (293–363 K) using BioRad SFX96 software and the temperatures of the inflection points (T m ’s) were used as indicators of the thermal stability of each sample. ΔT m ’s reflect stabilization effect of each condition compared to the control experiments performed in PBS. For more details refer to Materials and Methods section.
    96 Well Pcr Plates, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 38 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    USA Scientific Inc 96 well pcr plates
    Fig 4 shows examples of TSA melting curves of Pf MDH WT (dark bold lines), Pf MDH-V190W (dotted red lines), Pf MDH-E18W (dotted blue lines) and Pf MDH-E18Q (faint lines) in various buffer conditions: (a) PBS, (b) 400 mM NaCl, (c) 100 mM Na-Citrate pH 5.5 and (d) Assay Buffer (100 mM Na-Phosphate pH 7.4, 400 mM NaCl). Melting temperatures of each sample are displayed next to the respective curves. Analysis of these curves shows that Pf MDH is rather unstable in PBS (a) and requires optimized buffer conditions for further experiments. This effect is more pronounced for its mutant forms, where native oligomeric assembly has been disrupted (dotted lines). Pf MDH-E18Q mutant shows higher thermal stability, thus supporting the hypothesis that introduction of the additional hydrogen bond pair at the AB interface has had the desired stabilization effect. (b) 400 mM NaCl has significantly stabilized the wild type Pf MDH (ΔT m = 10 K), dimeric V190W mutant (ΔT m = 7 K) and tetrameric E18Q mutant (ΔT m = 8.5 K), while having minor effect of the E18W dimeric mutant (ΔT m = 2.5 K). (c) 100 mM Na-Citrate pH 5.5 significantly stabilized the wild type enzyme (ΔT m = 17.5 K) and the E18Q mutant (ΔT m = 15.5 K), while having lesser effect on V190W mutant (ΔT m = 6 K) and negligible effect on E18W (ΔT m = 0.5 K). (d) Selection of the Assay Buffer allowed further experiments to be performed for all four Pf MDH constructs used in this study in the same stabilizing buffer conditions (WT ΔT m = 13 K, V190W ΔT m = 7 K, E18W ΔT m = 5 K, E18Q ΔT m = 12.5 K). TSA assays were performed in <t>96-well</t> <t>PCR</t> plates (VWR) using SFX96 Real-Time PCR reactor (BioRad). Melting curve (in terms of increased fluorescence, RFU) of each sample was plotted against the temperature gradient (293–363 K) using BioRad SFX96 software and the temperatures of the inflection points (T m ’s) were used as indicators of the thermal stability of each sample. ΔT m ’s reflect stabilization effect of each condition compared to the control experiments performed in PBS. For more details refer to Materials and Methods section.
    96 Well Pcr Plates, supplied by USA Scientific Inc, used in various techniques. Bioz Stars score: 92/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96 well pcr plates - by Bioz Stars, 2020-10
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    94
    Thermo Fisher thermo fast 96 well pcr plates
    Fig 4 shows examples of TSA melting curves of Pf MDH WT (dark bold lines), Pf MDH-V190W (dotted red lines), Pf MDH-E18W (dotted blue lines) and Pf MDH-E18Q (faint lines) in various buffer conditions: (a) PBS, (b) 400 mM NaCl, (c) 100 mM Na-Citrate pH 5.5 and (d) Assay Buffer (100 mM Na-Phosphate pH 7.4, 400 mM NaCl). Melting temperatures of each sample are displayed next to the respective curves. Analysis of these curves shows that Pf MDH is rather unstable in PBS (a) and requires optimized buffer conditions for further experiments. This effect is more pronounced for its mutant forms, where native oligomeric assembly has been disrupted (dotted lines). Pf MDH-E18Q mutant shows higher thermal stability, thus supporting the hypothesis that introduction of the additional hydrogen bond pair at the AB interface has had the desired stabilization effect. (b) 400 mM NaCl has significantly stabilized the wild type Pf MDH (ΔT m = 10 K), dimeric V190W mutant (ΔT m = 7 K) and tetrameric E18Q mutant (ΔT m = 8.5 K), while having minor effect of the E18W dimeric mutant (ΔT m = 2.5 K). (c) 100 mM Na-Citrate pH 5.5 significantly stabilized the wild type enzyme (ΔT m = 17.5 K) and the E18Q mutant (ΔT m = 15.5 K), while having lesser effect on V190W mutant (ΔT m = 6 K) and negligible effect on E18W (ΔT m = 0.5 K). (d) Selection of the Assay Buffer allowed further experiments to be performed for all four Pf MDH constructs used in this study in the same stabilizing buffer conditions (WT ΔT m = 13 K, V190W ΔT m = 7 K, E18W ΔT m = 5 K, E18Q ΔT m = 12.5 K). TSA assays were performed in <t>96-well</t> <t>PCR</t> plates (VWR) using SFX96 Real-Time PCR reactor (BioRad). Melting curve (in terms of increased fluorescence, RFU) of each sample was plotted against the temperature gradient (293–363 K) using BioRad SFX96 software and the temperatures of the inflection points (T m ’s) were used as indicators of the thermal stability of each sample. ΔT m ’s reflect stabilization effect of each condition compared to the control experiments performed in PBS. For more details refer to Materials and Methods section.
    Thermo Fast 96 Well Pcr Plates, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 75 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Fig 4 shows examples of TSA melting curves of Pf MDH WT (dark bold lines), Pf MDH-V190W (dotted red lines), Pf MDH-E18W (dotted blue lines) and Pf MDH-E18Q (faint lines) in various buffer conditions: (a) PBS, (b) 400 mM NaCl, (c) 100 mM Na-Citrate pH 5.5 and (d) Assay Buffer (100 mM Na-Phosphate pH 7.4, 400 mM NaCl). Melting temperatures of each sample are displayed next to the respective curves. Analysis of these curves shows that Pf MDH is rather unstable in PBS (a) and requires optimized buffer conditions for further experiments. This effect is more pronounced for its mutant forms, where native oligomeric assembly has been disrupted (dotted lines). Pf MDH-E18Q mutant shows higher thermal stability, thus supporting the hypothesis that introduction of the additional hydrogen bond pair at the AB interface has had the desired stabilization effect. (b) 400 mM NaCl has significantly stabilized the wild type Pf MDH (ΔT m = 10 K), dimeric V190W mutant (ΔT m = 7 K) and tetrameric E18Q mutant (ΔT m = 8.5 K), while having minor effect of the E18W dimeric mutant (ΔT m = 2.5 K). (c) 100 mM Na-Citrate pH 5.5 significantly stabilized the wild type enzyme (ΔT m = 17.5 K) and the E18Q mutant (ΔT m = 15.5 K), while having lesser effect on V190W mutant (ΔT m = 6 K) and negligible effect on E18W (ΔT m = 0.5 K). (d) Selection of the Assay Buffer allowed further experiments to be performed for all four Pf MDH constructs used in this study in the same stabilizing buffer conditions (WT ΔT m = 13 K, V190W ΔT m = 7 K, E18W ΔT m = 5 K, E18Q ΔT m = 12.5 K). TSA assays were performed in 96-well PCR plates (VWR) using SFX96 Real-Time PCR reactor (BioRad). Melting curve (in terms of increased fluorescence, RFU) of each sample was plotted against the temperature gradient (293–363 K) using BioRad SFX96 software and the temperatures of the inflection points (T m ’s) were used as indicators of the thermal stability of each sample. ΔT m ’s reflect stabilization effect of each condition compared to the control experiments performed in PBS. For more details refer to Materials and Methods section.

    Journal: PLoS ONE

    Article Title: Oligomeric interfaces as a tool in drug discovery: Specific interference with activity of malate dehydrogenase of Plasmodium falciparum in vitro

    doi: 10.1371/journal.pone.0195011

    Figure Lengend Snippet: Fig 4 shows examples of TSA melting curves of Pf MDH WT (dark bold lines), Pf MDH-V190W (dotted red lines), Pf MDH-E18W (dotted blue lines) and Pf MDH-E18Q (faint lines) in various buffer conditions: (a) PBS, (b) 400 mM NaCl, (c) 100 mM Na-Citrate pH 5.5 and (d) Assay Buffer (100 mM Na-Phosphate pH 7.4, 400 mM NaCl). Melting temperatures of each sample are displayed next to the respective curves. Analysis of these curves shows that Pf MDH is rather unstable in PBS (a) and requires optimized buffer conditions for further experiments. This effect is more pronounced for its mutant forms, where native oligomeric assembly has been disrupted (dotted lines). Pf MDH-E18Q mutant shows higher thermal stability, thus supporting the hypothesis that introduction of the additional hydrogen bond pair at the AB interface has had the desired stabilization effect. (b) 400 mM NaCl has significantly stabilized the wild type Pf MDH (ΔT m = 10 K), dimeric V190W mutant (ΔT m = 7 K) and tetrameric E18Q mutant (ΔT m = 8.5 K), while having minor effect of the E18W dimeric mutant (ΔT m = 2.5 K). (c) 100 mM Na-Citrate pH 5.5 significantly stabilized the wild type enzyme (ΔT m = 17.5 K) and the E18Q mutant (ΔT m = 15.5 K), while having lesser effect on V190W mutant (ΔT m = 6 K) and negligible effect on E18W (ΔT m = 0.5 K). (d) Selection of the Assay Buffer allowed further experiments to be performed for all four Pf MDH constructs used in this study in the same stabilizing buffer conditions (WT ΔT m = 13 K, V190W ΔT m = 7 K, E18W ΔT m = 5 K, E18Q ΔT m = 12.5 K). TSA assays were performed in 96-well PCR plates (VWR) using SFX96 Real-Time PCR reactor (BioRad). Melting curve (in terms of increased fluorescence, RFU) of each sample was plotted against the temperature gradient (293–363 K) using BioRad SFX96 software and the temperatures of the inflection points (T m ’s) were used as indicators of the thermal stability of each sample. ΔT m ’s reflect stabilization effect of each condition compared to the control experiments performed in PBS. For more details refer to Materials and Methods section.

    Article Snippet: Thermal Stability Assay (TSA) TSA assays were performed in 96-well PCR plates (VWR) using SFX96 Real-Time PCR reactor (BioRad).

    Techniques: Mutagenesis, Selection, Construct, Polymerase Chain Reaction, Real-time Polymerase Chain Reaction, Fluorescence, Software