m1 42 Search Results


mac 1  (ATCC)
94
ATCC mac 1
Mac 1, supplied by ATCC, 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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tentagel thiol resin  (Chem Impex International)
95
Chem Impex International tentagel thiol resin
Tentagel Thiol Resin, supplied by Chem Impex International, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/tentagel thiol resin/product/Chem Impex International
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plasmid pet sac abeta  (Addgene inc)
93
Addgene inc plasmid pet sac abeta
Plasmid Pet Sac Abeta, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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gene exp lin 42 ce02593603 m1  (Thermo Fisher)
91
Thermo Fisher gene exp lin 42 ce02593603 m1
Gene Exp Lin 42 Ce02593603 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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silicon probes with a nominal spring constant of 2.8 n·m −1  (Nanosensors Inc)
90
Nanosensors Inc silicon probes with a nominal spring constant of 2.8 n·m −1
Silicon Probes With A Nominal Spring Constant Of 2.8 N·M −1, supplied by Nanosensors 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/silicon probes with a nominal spring constant of 2.8 n·m −1/product/Nanosensors Inc
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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
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Average 90 stars, based on 1 article reviews
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anti-mhc class antibody m1/42  (Boehringer Mannheim)
90
Boehringer Mannheim anti-mhc class antibody m1/42
( 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.
Anti Mhc Class Antibody M1/42, supplied by Boehringer Mannheim, 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/anti-mhc class antibody m1/42/product/Boehringer Mannheim
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mhc-1 m1/42.3.9.8  (Becton Dickinson)
90
Becton Dickinson mhc-1 m1/42.3.9.8
( 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.
Mhc 1 M1/42.3.9.8, supplied by Becton Dickinson, 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/mhc-1 m1/42.3.9.8/product/Becton Dickinson
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monotypic antibody m1/42  (Blackwell Science Ltd)
90
Blackwell Science Ltd monotypic antibody m1/42
( 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.
Monotypic Antibody M1/42, supplied by Blackwell Science Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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platinum/iridium-coated afm tips nchpt 42 n m-1  (Nanoworld Services GmbH)
90
Nanoworld Services GmbH platinum/iridium-coated afm tips nchpt 42 n m-1
( 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.
Platinum/Iridium Coated Afm Tips Nchpt 42 N M 1, supplied by Nanoworld Services GmbH, 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/platinum/iridium-coated afm tips nchpt 42 n m-1/product/Nanoworld Services GmbH
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multi-microelectrode arrays in the primary motor cortex (m1-42 channels)  (Blackrock Microsystems LLC)
90
Blackrock Microsystems LLC multi-microelectrode arrays in the primary motor cortex (m1-42 channels)
( 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.
Multi Microelectrode Arrays In The Primary Motor Cortex (M1 42 Channels), supplied by Blackrock Microsystems LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti-class m 1/42  (Becton Dickinson)
90
Becton Dickinson anti-class m 1/42
( 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.
Anti Class M 1/42, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti-class m 1/42 - by Bioz Stars, 2026-05
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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