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aβ42 peptide  (Addgene inc)


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    Structured Review

    Addgene inc aβ42 peptide
    Aβ42 Peptide, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/aβ42 peptide/product/Addgene inc
    Average 93 stars, based on 19 article reviews
    aβ42 peptide - by Bioz Stars, 2026-05
    93/100 stars

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    Fig. 1. Concentration of NaCl affects the kinetics of protein aggregation. (A) Time-dependent ThT fluorescence measurements of 10 μM <t>Aβ42</t> (Peptide: ThT ratio = 1 : 1) incubated at 37 °C in the absence (red) or presence of NaCl at 6.25 mM (cyan), 12.5 mM (green), 25 mM (blue), 50 mM (gray), 100 mM (purple), 150 mM (yellow), and 200 mM (orange). All the kinetic experiments were performed in a 37 °C fluo- rescence plate reader under shaking conditions of 250 rpm and fluorescence data were collected every 10 min. Each data point represents the mean value and error bars represent standard error with n = 3. (B) Aβ42 aggregation kinetics were fitted to a sigmoidal function and the aggregation lag time was plotted as a function of NaCl concentration. Each data point represents the mean value and error bars represent standard error with n = 3.
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    Polysciences inc aβ42 expression plasmid
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    Image Search Results


    Fig. 1. Concentration of NaCl affects the kinetics of protein aggregation. (A) Time-dependent ThT fluorescence measurements of 10 μM Aβ42 (Peptide: ThT ratio = 1 : 1) incubated at 37 °C in the absence (red) or presence of NaCl at 6.25 mM (cyan), 12.5 mM (green), 25 mM (blue), 50 mM (gray), 100 mM (purple), 150 mM (yellow), and 200 mM (orange). All the kinetic experiments were performed in a 37 °C fluo- rescence plate reader under shaking conditions of 250 rpm and fluorescence data were collected every 10 min. Each data point represents the mean value and error bars represent standard error with n = 3. (B) Aβ42 aggregation kinetics were fitted to a sigmoidal function and the aggregation lag time was plotted as a function of NaCl concentration. Each data point represents the mean value and error bars represent standard error with n = 3.

    Journal: The FEBS journal

    Article Title: Membrane protein chaperone and sodium chloride modulate the kinetics and morphology of amyloid beta aggregation.

    doi: 10.1111/febs.16967

    Figure Lengend Snippet: Fig. 1. Concentration of NaCl affects the kinetics of protein aggregation. (A) Time-dependent ThT fluorescence measurements of 10 μM Aβ42 (Peptide: ThT ratio = 1 : 1) incubated at 37 °C in the absence (red) or presence of NaCl at 6.25 mM (cyan), 12.5 mM (green), 25 mM (blue), 50 mM (gray), 100 mM (purple), 150 mM (yellow), and 200 mM (orange). All the kinetic experiments were performed in a 37 °C fluo- rescence plate reader under shaking conditions of 250 rpm and fluorescence data were collected every 10 min. Each data point represents the mean value and error bars represent standard error with n = 3. (B) Aβ42 aggregation kinetics were fitted to a sigmoidal function and the aggregation lag time was plotted as a function of NaCl concentration. Each data point represents the mean value and error bars represent standard error with n = 3.

    Article Snippet: Aβ40 and Aβ42 plasmids [pET-Sac-Abeta (M1-42) and pET-Sac-Abeta (M1-40); Addgene plasmids #71875 and #71876, respectively] containing exogenous methionine at the N-terminus were gifts from Dominic Walsh [80].

    Techniques: Concentration Assay, Incubation

    Fig. 2. Electrostatic repulsion of Aβ42 affects the formation of protein aggregates. (A) Primary sequence of Aβ40 and Aβ42 with the charged residues highlighted. Additional hydrophobic residues in Aβ42 are highlighted in red. (B, C) Electrostatic surface potential (B) and ribbon diagram (C) of the Aβ42 fibril from the Protein Data Bank (PDB: 2NAO) visualized in PYMOL. Positively and negatively charged side chains of amino acids are shown in blue and red, respectively. Hydrophobic residues are shown in white and the protein backbone in green. Electrostatic repulsions are highlighted between fibril layers.

    Journal: The FEBS journal

    Article Title: Membrane protein chaperone and sodium chloride modulate the kinetics and morphology of amyloid beta aggregation.

    doi: 10.1111/febs.16967

    Figure Lengend Snippet: Fig. 2. Electrostatic repulsion of Aβ42 affects the formation of protein aggregates. (A) Primary sequence of Aβ40 and Aβ42 with the charged residues highlighted. Additional hydrophobic residues in Aβ42 are highlighted in red. (B, C) Electrostatic surface potential (B) and ribbon diagram (C) of the Aβ42 fibril from the Protein Data Bank (PDB: 2NAO) visualized in PYMOL. Positively and negatively charged side chains of amino acids are shown in blue and red, respectively. Hydrophobic residues are shown in white and the protein backbone in green. Electrostatic repulsions are highlighted between fibril layers.

    Article Snippet: Aβ40 and Aβ42 plasmids [pET-Sac-Abeta (M1-42) and pET-Sac-Abeta (M1-40); Addgene plasmids #71875 and #71876, respectively] containing exogenous methionine at the N-terminus were gifts from Dominic Walsh [80].

    Techniques: Sequencing

    Fig. 6. TEM and SEM reveal that cpSRP43 can change the morphology of Aβ40 and Aβ42 aggregates. (A, B) Aβ40 (20 μM) monomer was incubated at 37 °C for 3 days either in the absence (A) or presence (B) of 10-fold excess cpSRP43. For each sample, 1 μL was dried and visualized by TEM. The images in both (A) and (B) were obtained at a magnification of 15K×. Scale bars are 500 nm. (C, D) Aβ42 monomer (10 μM) was incubated with 1 μM Aβ42 seeds in the absence (C) or presence (D) of 10-fold excess cpSRP43 for 4 days at 37 °C. For each sample, 1 μL was dried and visualized by SEM. The images in both (C) and (D) were captured at 600×. Scale bars are 50 μm. Data are rep- resentative of three independent experiments.

    Journal: The FEBS journal

    Article Title: Membrane protein chaperone and sodium chloride modulate the kinetics and morphology of amyloid beta aggregation.

    doi: 10.1111/febs.16967

    Figure Lengend Snippet: Fig. 6. TEM and SEM reveal that cpSRP43 can change the morphology of Aβ40 and Aβ42 aggregates. (A, B) Aβ40 (20 μM) monomer was incubated at 37 °C for 3 days either in the absence (A) or presence (B) of 10-fold excess cpSRP43. For each sample, 1 μL was dried and visualized by TEM. The images in both (A) and (B) were obtained at a magnification of 15K×. Scale bars are 500 nm. (C, D) Aβ42 monomer (10 μM) was incubated with 1 μM Aβ42 seeds in the absence (C) or presence (D) of 10-fold excess cpSRP43 for 4 days at 37 °C. For each sample, 1 μL was dried and visualized by SEM. The images in both (C) and (D) were captured at 600×. Scale bars are 50 μm. Data are rep- resentative of three independent experiments.

    Article Snippet: Aβ40 and Aβ42 plasmids [pET-Sac-Abeta (M1-42) and pET-Sac-Abeta (M1-40); Addgene plasmids #71875 and #71876, respectively] containing exogenous methionine at the N-terminus were gifts from Dominic Walsh [80].

    Techniques: Incubation

    Antibodies that were conjugated to magnetic beads to capture antigens.

    Journal: Laboratory investigation; a journal of technical methods and pathology

    Article Title: Luminex-based quantification of Alzheimer’s Disease neuropathologic change in formalin-fixed post-mortem human brain tissue

    doi: 10.1038/s41374-018-0165-x

    Figure Lengend Snippet: Antibodies that were conjugated to magnetic beads to capture antigens.

    Article Snippet: We then transfected HEK cells with the Aβ42 expression plasmid using polyethylenimine (PEI, Polysciences; Warrington, PA) transfection.

    Techniques: Magnetic Beads

    Antibodies that were biotinylated to detect captured antigens.

    Journal: Laboratory investigation; a journal of technical methods and pathology

    Article Title: Luminex-based quantification of Alzheimer’s Disease neuropathologic change in formalin-fixed post-mortem human brain tissue

    doi: 10.1038/s41374-018-0165-x

    Figure Lengend Snippet: Antibodies that were biotinylated to detect captured antigens.

    Article Snippet: We then transfected HEK cells with the Aβ42 expression plasmid using polyethylenimine (PEI, Polysciences; Warrington, PA) transfection.

    Techniques:

    Validation of recombinant Aβ42 standards. (a) Quantification of recombinant Aβ42 using commercial Innogenetics-kit standards and the Innogenetics kit. (b) Comparison of serial dilutions of Innogenetics-kit and recombinant Aβ42 standards measured with the Innogenetics kit. (c) Generation of a standard curve with recombinant Aβ42 standards measured with our newly developed Luminex assay. (d) Test-retest of serially diluted recombinant Aβ42 standards measured with our newly developed Luminex assay. All data are presented as mean ± SEM.

    Journal: Laboratory investigation; a journal of technical methods and pathology

    Article Title: Luminex-based quantification of Alzheimer’s Disease neuropathologic change in formalin-fixed post-mortem human brain tissue

    doi: 10.1038/s41374-018-0165-x

    Figure Lengend Snippet: Validation of recombinant Aβ42 standards. (a) Quantification of recombinant Aβ42 using commercial Innogenetics-kit standards and the Innogenetics kit. (b) Comparison of serial dilutions of Innogenetics-kit and recombinant Aβ42 standards measured with the Innogenetics kit. (c) Generation of a standard curve with recombinant Aβ42 standards measured with our newly developed Luminex assay. (d) Test-retest of serially diluted recombinant Aβ42 standards measured with our newly developed Luminex assay. All data are presented as mean ± SEM.

    Article Snippet: We then transfected HEK cells with the Aβ42 expression plasmid using polyethylenimine (PEI, Polysciences; Warrington, PA) transfection.

    Techniques: Recombinant, Luminex

    Determination of optimal FFPE sample amounts for Luminex analysis of Aβ42, and quantification of Aβ42 in FFPE tissue from cases with Not/Low, Intermediate and High NIA-AA AD severity. (a) Fluorescent-intensity signals for Aβ42 as function of increasing amounts of guanidine-soluble extracts from middle frontal gyrus. (b) Aβ42 levels in MFG samples from cases with varying NIA-AA AD severity (Not/Low: n = 10, Intermediate: n = 10, High: n = 9). (c) Aβ42 levels in hippocampal samples from cases with varying NIA-AA AD severity (Not/Low: n = 10, Intermediate: n = 10, High: n = 9). (d) Aβ42 levels in neostriatal samples from cases with varying NIA-AA AD severity (Not/Low: n = 10, Intermediate: n = 10, High: n = 9). Aβ42 levels in panels (b-d) are normalized to the amount of guanidine-soluble protein (pg per μg). All data are presented as mean ± SEM. ★ p < 0.05 and ★★ p < 0.01.

    Journal: Laboratory investigation; a journal of technical methods and pathology

    Article Title: Luminex-based quantification of Alzheimer’s Disease neuropathologic change in formalin-fixed post-mortem human brain tissue

    doi: 10.1038/s41374-018-0165-x

    Figure Lengend Snippet: Determination of optimal FFPE sample amounts for Luminex analysis of Aβ42, and quantification of Aβ42 in FFPE tissue from cases with Not/Low, Intermediate and High NIA-AA AD severity. (a) Fluorescent-intensity signals for Aβ42 as function of increasing amounts of guanidine-soluble extracts from middle frontal gyrus. (b) Aβ42 levels in MFG samples from cases with varying NIA-AA AD severity (Not/Low: n = 10, Intermediate: n = 10, High: n = 9). (c) Aβ42 levels in hippocampal samples from cases with varying NIA-AA AD severity (Not/Low: n = 10, Intermediate: n = 10, High: n = 9). (d) Aβ42 levels in neostriatal samples from cases with varying NIA-AA AD severity (Not/Low: n = 10, Intermediate: n = 10, High: n = 9). Aβ42 levels in panels (b-d) are normalized to the amount of guanidine-soluble protein (pg per μg). All data are presented as mean ± SEM. ★ p < 0.05 and ★★ p < 0.01.

    Article Snippet: We then transfected HEK cells with the Aβ42 expression plasmid using polyethylenimine (PEI, Polysciences; Warrington, PA) transfection.

    Techniques: Luminex

    Scatter plots of Luminex fluorescent signal intensities for Aβ42 and pTau in MFG, hippocampus and neostriatum. We performed correlation analyses of Aβ42 and pTau signals across all analyzed brain regions and confirmed the following statistically significant positive correlations. (a) Aβ42 levels in MFG vs. Aβ42 levels in hippocampus. (b) Aβ42 levels in MFG vs. Aβ42 levels in neostriatum. (c) Aβ42 levels in hippocampus vs. Aβ42 levels in neostriatum. (d) Aβ42 levels in neostriatum vs. pTau levels in MFG. (e) pTau levels in MFG vs. pTau levels in hippocampus. Statistically significant R 2 values are shown in each scatter plot.

    Journal: Laboratory investigation; a journal of technical methods and pathology

    Article Title: Luminex-based quantification of Alzheimer’s Disease neuropathologic change in formalin-fixed post-mortem human brain tissue

    doi: 10.1038/s41374-018-0165-x

    Figure Lengend Snippet: Scatter plots of Luminex fluorescent signal intensities for Aβ42 and pTau in MFG, hippocampus and neostriatum. We performed correlation analyses of Aβ42 and pTau signals across all analyzed brain regions and confirmed the following statistically significant positive correlations. (a) Aβ42 levels in MFG vs. Aβ42 levels in hippocampus. (b) Aβ42 levels in MFG vs. Aβ42 levels in neostriatum. (c) Aβ42 levels in hippocampus vs. Aβ42 levels in neostriatum. (d) Aβ42 levels in neostriatum vs. pTau levels in MFG. (e) pTau levels in MFG vs. pTau levels in hippocampus. Statistically significant R 2 values are shown in each scatter plot.

    Article Snippet: We then transfected HEK cells with the Aβ42 expression plasmid using polyethylenimine (PEI, Polysciences; Warrington, PA) transfection.

    Techniques: Luminex

    Correlations (R 2 ) between  Aβ42  and pTau levels in MFG, hippocampus and neostriatum in all analyzed samples. Statistically significant correlation coefficients are marked: ★ p < 0.05 and ★★ p < 0.01.

    Journal: Laboratory investigation; a journal of technical methods and pathology

    Article Title: Luminex-based quantification of Alzheimer’s Disease neuropathologic change in formalin-fixed post-mortem human brain tissue

    doi: 10.1038/s41374-018-0165-x

    Figure Lengend Snippet: Correlations (R 2 ) between Aβ42 and pTau levels in MFG, hippocampus and neostriatum in all analyzed samples. Statistically significant correlation coefficients are marked: ★ p < 0.05 and ★★ p < 0.01.

    Article Snippet: We then transfected HEK cells with the Aβ42 expression plasmid using polyethylenimine (PEI, Polysciences; Warrington, PA) transfection.

    Techniques:

    Association of Aβ42 and pTau levels with genetic risk for AD. (a) Aβ42 and (b) pTau levels in MFG, hippocampus and neostriatum of samples from cases with no APOE-ε4 allele (n = 18) and with at least one APOE-ε4 allele (n = 11). All data are presented as mean ± SEM.

    Journal: Laboratory investigation; a journal of technical methods and pathology

    Article Title: Luminex-based quantification of Alzheimer’s Disease neuropathologic change in formalin-fixed post-mortem human brain tissue

    doi: 10.1038/s41374-018-0165-x

    Figure Lengend Snippet: Association of Aβ42 and pTau levels with genetic risk for AD. (a) Aβ42 and (b) pTau levels in MFG, hippocampus and neostriatum of samples from cases with no APOE-ε4 allele (n = 18) and with at least one APOE-ε4 allele (n = 11). All data are presented as mean ± SEM.

    Article Snippet: We then transfected HEK cells with the Aβ42 expression plasmid using polyethylenimine (PEI, Polysciences; Warrington, PA) transfection.

    Techniques: