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synthetic gene with e. coli optimised codons for aβ(m1-42) with the a2v mutation  (GenScript corporation)

 
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    GenScript corporation synthetic gene with e. coli optimised codons for aβ(m1-42) with the a2v mutation
    ( A , B ) Normalized time courses (ThT fluorescence data points) for aggregation reactions starting from 0.8 (grey) to 10 μM (red) <t>Aβ42-A2V</t> monomer in 20 mM NaP, 0.2 mM EDTA, 0.02% NaN 3 , pH 8.0. Each colour shows four technical replicates at each concentration. The solid lines represents the best fits of model 3a (A) and model 4a (B) and plots for all models are shown in . ( A ) The best fit with a model consistent with the Aβ42 wt data: primary nucleation, secondary nucleation and elongation with fixed reaction orders n c = n 2 = 2 (as for wt) (model 3a) and ( B ) the best fit with a model including primary nucleation and multi-step secondary nucleation (model 4a). ( C ) The half time as a function of peptide concentration from the best fit of each model is compared to the experimental data. ( D ) Error square sum, a measure of the goodness of the fit, of each model relative to model 4a. The models, with the number of fitting parameters given in brackets, are: Model1b Primary nucleation and elongation (2). Model2b Primary nucleation, fragmentation and elongation (3). Model3a Primary nucleation, secondary nucleation and elongation (2). Model3b Primary nucleation, secondary nucleation and elongation (4). Model4a Primary nucleation, multi-step secondary nucleation and elongation (3). Although involving one less free parameter than model 3b, model 4a yields a lower error. See for the processes and parameters for each model. ( E ) Normalized aggregation kinetics data for samples that initially contain 2.3 μM monomer supplemented with 0.03, 0.1, 0.3, 1, 3, 10 or 30% seeds (in monomer equivalents) confirm the strong role of surface-catalyzed secondary nucleation. The solid lines are fits of model 4a, using the parameter values found above and one free parameter, the elongation rate constant k + . ( F ) Comparison of k 2 k + and k 2 /kn for Aβ42-A2V relative to Aβ42-wt. In particular note the large increase in the relative importance of secondary over primary nucleation.
    Synthetic Gene With E. Coli Optimised Codons For Aβ(M1 42) With The A2v Mutation, supplied by GenScript 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/synthetic+gene+with+e%2E+coli+optimised+codons+for+a%CE%B2(m1-42)+with+the+a2v+mutation/synthetic+gene+with+e++coli+optimised+codons+for+a%CE%B2+m1+42++with+the+a2v+mutation/pmc04725935-144-12-22
    Average 90 stars, based on 1 article reviews
    synthetic gene with e. coli optimised codons for aβ(m1-42) with the a2v mutation - by Bioz Stars, 2026-11
    90/100 stars

    Images

    1) Product Images from "Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide"

    Article Title: Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide

    Journal: Scientific Reports

    doi: 10.1038/srep18728

    ( A , B ) Normalized time courses (ThT fluorescence data points) for aggregation reactions starting from 0.8 (grey) to 10 μM (red) Aβ42-A2V monomer in 20 mM NaP, 0.2 mM EDTA, 0.02% NaN 3 , pH 8.0. Each colour shows four technical replicates at each concentration. The solid lines represents the best fits of model 3a (A) and model 4a (B) and plots for all models are shown in . ( A ) The best fit with a model consistent with the Aβ42 wt data: primary nucleation, secondary nucleation and elongation with fixed reaction orders n c = n 2 = 2 (as for wt) (model 3a) and ( B ) the best fit with a model including primary nucleation and multi-step secondary nucleation (model 4a). ( C ) The half time as a function of peptide concentration from the best fit of each model is compared to the experimental data. ( D ) Error square sum, a measure of the goodness of the fit, of each model relative to model 4a. The models, with the number of fitting parameters given in brackets, are: Model1b Primary nucleation and elongation (2). Model2b Primary nucleation, fragmentation and elongation (3). Model3a Primary nucleation, secondary nucleation and elongation (2). Model3b Primary nucleation, secondary nucleation and elongation (4). Model4a Primary nucleation, multi-step secondary nucleation and elongation (3). Although involving one less free parameter than model 3b, model 4a yields a lower error. See for the processes and parameters for each model. ( E ) Normalized aggregation kinetics data for samples that initially contain 2.3 μM monomer supplemented with 0.03, 0.1, 0.3, 1, 3, 10 or 30% seeds (in monomer equivalents) confirm the strong role of surface-catalyzed secondary nucleation. The solid lines are fits of model 4a, using the parameter values found above and one free parameter, the elongation rate constant k + . ( F ) Comparison of k 2 k + and k 2 /kn for Aβ42-A2V relative to Aβ42-wt. In particular note the large increase in the relative importance of secondary over primary nucleation.
    Figure Legend Snippet: ( A , B ) Normalized time courses (ThT fluorescence data points) for aggregation reactions starting from 0.8 (grey) to 10 μM (red) Aβ42-A2V monomer in 20 mM NaP, 0.2 mM EDTA, 0.02% NaN 3 , pH 8.0. Each colour shows four technical replicates at each concentration. The solid lines represents the best fits of model 3a (A) and model 4a (B) and plots for all models are shown in . ( A ) The best fit with a model consistent with the Aβ42 wt data: primary nucleation, secondary nucleation and elongation with fixed reaction orders n c = n 2 = 2 (as for wt) (model 3a) and ( B ) the best fit with a model including primary nucleation and multi-step secondary nucleation (model 4a). ( C ) The half time as a function of peptide concentration from the best fit of each model is compared to the experimental data. ( D ) Error square sum, a measure of the goodness of the fit, of each model relative to model 4a. The models, with the number of fitting parameters given in brackets, are: Model1b Primary nucleation and elongation (2). Model2b Primary nucleation, fragmentation and elongation (3). Model3a Primary nucleation, secondary nucleation and elongation (2). Model3b Primary nucleation, secondary nucleation and elongation (4). Model4a Primary nucleation, multi-step secondary nucleation and elongation (3). Although involving one less free parameter than model 3b, model 4a yields a lower error. See for the processes and parameters for each model. ( E ) Normalized aggregation kinetics data for samples that initially contain 2.3 μM monomer supplemented with 0.03, 0.1, 0.3, 1, 3, 10 or 30% seeds (in monomer equivalents) confirm the strong role of surface-catalyzed secondary nucleation. The solid lines are fits of model 4a, using the parameter values found above and one free parameter, the elongation rate constant k + . ( F ) Comparison of k 2 k + and k 2 /kn for Aβ42-A2V relative to Aβ42-wt. In particular note the large increase in the relative importance of secondary over primary nucleation.

    Techniques Used: Fluorescence, Concentration Assay, Comparison



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    synthetic gene with e. coli optimised codons for aβ(m1-42) with the a2v mutation  (GenScript corporation)
    90
    GenScript corporation synthetic gene with e. coli optimised codons for aβ(m1-42) with the a2v mutation
    ( A , B ) Normalized time courses (ThT fluorescence data points) for aggregation reactions starting from 0.8 (grey) to 10 μM (red) <t>Aβ42-A2V</t> monomer in 20 mM NaP, 0.2 mM EDTA, 0.02% NaN 3 , pH 8.0. Each colour shows four technical replicates at each concentration. The solid lines represents the best fits of model 3a (A) and model 4a (B) and plots for all models are shown in . ( A ) The best fit with a model consistent with the Aβ42 wt data: primary nucleation, secondary nucleation and elongation with fixed reaction orders n c = n 2 = 2 (as for wt) (model 3a) and ( B ) the best fit with a model including primary nucleation and multi-step secondary nucleation (model 4a). ( C ) The half time as a function of peptide concentration from the best fit of each model is compared to the experimental data. ( D ) Error square sum, a measure of the goodness of the fit, of each model relative to model 4a. The models, with the number of fitting parameters given in brackets, are: Model1b Primary nucleation and elongation (2). Model2b Primary nucleation, fragmentation and elongation (3). Model3a Primary nucleation, secondary nucleation and elongation (2). Model3b Primary nucleation, secondary nucleation and elongation (4). Model4a Primary nucleation, multi-step secondary nucleation and elongation (3). Although involving one less free parameter than model 3b, model 4a yields a lower error. See for the processes and parameters for each model. ( E ) Normalized aggregation kinetics data for samples that initially contain 2.3 μM monomer supplemented with 0.03, 0.1, 0.3, 1, 3, 10 or 30% seeds (in monomer equivalents) confirm the strong role of surface-catalyzed secondary nucleation. The solid lines are fits of model 4a, using the parameter values found above and one free parameter, the elongation rate constant k + . ( F ) Comparison of k 2 k + and k 2 /kn for Aβ42-A2V relative to Aβ42-wt. In particular note the large increase in the relative importance of secondary over primary nucleation.
    Synthetic Gene With E. Coli Optimised Codons For Aβ(M1 42) With The A2v Mutation, supplied by GenScript 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/synthetic+gene+with+e%2E+coli+optimised+codons+for+a%CE%B2(m1-42)+with+the+a2v+mutation/synthetic+gene+with+e++coli+optimised+codons+for+a%CE%B2+m1+42++with+the+a2v+mutation/pmc04725935-144-12-22
    Average 90 stars, based on 1 article reviews
    synthetic gene with e. coli optimised codons for aβ(m1-42) with the a2v mutation - by Bioz Stars, 2026-11
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    ( A , B ) Normalized time courses (ThT fluorescence data points) for aggregation reactions starting from 0.8 (grey) to 10 μM (red) Aβ42-A2V monomer in 20 mM NaP, 0.2 mM EDTA, 0.02% NaN 3 , pH 8.0. Each colour shows four technical replicates at each concentration. The solid lines represents the best fits of model 3a (A) and model 4a (B) and plots for all models are shown in . ( A ) The best fit with a model consistent with the Aβ42 wt data: primary nucleation, secondary nucleation and elongation with fixed reaction orders n c = n 2 = 2 (as for wt) (model 3a) and ( B ) the best fit with a model including primary nucleation and multi-step secondary nucleation (model 4a). ( C ) The half time as a function of peptide concentration from the best fit of each model is compared to the experimental data. ( D ) Error square sum, a measure of the goodness of the fit, of each model relative to model 4a. The models, with the number of fitting parameters given in brackets, are: Model1b Primary nucleation and elongation (2). Model2b Primary nucleation, fragmentation and elongation (3). Model3a Primary nucleation, secondary nucleation and elongation (2). Model3b Primary nucleation, secondary nucleation and elongation (4). Model4a Primary nucleation, multi-step secondary nucleation and elongation (3). Although involving one less free parameter than model 3b, model 4a yields a lower error. See for the processes and parameters for each model. ( E ) Normalized aggregation kinetics data for samples that initially contain 2.3 μM monomer supplemented with 0.03, 0.1, 0.3, 1, 3, 10 or 30% seeds (in monomer equivalents) confirm the strong role of surface-catalyzed secondary nucleation. The solid lines are fits of model 4a, using the parameter values found above and one free parameter, the elongation rate constant k + . ( F ) Comparison of k 2 k + and k 2 /kn for Aβ42-A2V relative to Aβ42-wt. In particular note the large increase in the relative importance of secondary over primary nucleation.

    Journal: Scientific Reports

    Article Title: Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide

    doi: 10.1038/srep18728

    Figure Lengend Snippet: ( A , B ) Normalized time courses (ThT fluorescence data points) for aggregation reactions starting from 0.8 (grey) to 10 μM (red) Aβ42-A2V monomer in 20 mM NaP, 0.2 mM EDTA, 0.02% NaN 3 , pH 8.0. Each colour shows four technical replicates at each concentration. The solid lines represents the best fits of model 3a (A) and model 4a (B) and plots for all models are shown in . ( A ) The best fit with a model consistent with the Aβ42 wt data: primary nucleation, secondary nucleation and elongation with fixed reaction orders n c = n 2 = 2 (as for wt) (model 3a) and ( B ) the best fit with a model including primary nucleation and multi-step secondary nucleation (model 4a). ( C ) The half time as a function of peptide concentration from the best fit of each model is compared to the experimental data. ( D ) Error square sum, a measure of the goodness of the fit, of each model relative to model 4a. The models, with the number of fitting parameters given in brackets, are: Model1b Primary nucleation and elongation (2). Model2b Primary nucleation, fragmentation and elongation (3). Model3a Primary nucleation, secondary nucleation and elongation (2). Model3b Primary nucleation, secondary nucleation and elongation (4). Model4a Primary nucleation, multi-step secondary nucleation and elongation (3). Although involving one less free parameter than model 3b, model 4a yields a lower error. See for the processes and parameters for each model. ( E ) Normalized aggregation kinetics data for samples that initially contain 2.3 μM monomer supplemented with 0.03, 0.1, 0.3, 1, 3, 10 or 30% seeds (in monomer equivalents) confirm the strong role of surface-catalyzed secondary nucleation. The solid lines are fits of model 4a, using the parameter values found above and one free parameter, the elongation rate constant k + . ( F ) Comparison of k 2 k + and k 2 /kn for Aβ42-A2V relative to Aβ42-wt. In particular note the large increase in the relative importance of secondary over primary nucleation.

    Article Snippet: A synthetic gene with E. coli optimised codons for Aβ(M1-42) with the A2V mutation cloned into the Pet3a vector was purchased from Genscript (Piscataway; New Jersey, USA).

    Techniques: Fluorescence, Concentration Assay, Comparison