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sift-2d evaluation software  (Evotec Inc)


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    Evotec Inc sift-2d evaluation software
    Tau phosphorylation verified by western blot and <t>SIFT</t> analysis. A. Mass spectroscopy showed that recombinant human tau (isoform 5, 42967 Da) is of high purity. B. While mock phosphorylation (mTau) does not influence SDS-PAGE mobility of recombinant tau, a typical band shift is observed upon tau phosphorylation (pTau). C. SIFT analysis showed labeling of pTau oligomers with the phosphorylated tau specific AT-8 antibody in presence of 1% DMSO indicating antibody binding, while no coaggregation was observed with mTau. Data was normalized against the coaggregation level of mTau with the T46 antibody, which does not require tau phosphorylation. <t>2D</t> histograms depicting antibody (x-axis) and protein (y-axis) interactions show coaggregates of T46 with both pTau and mTau, while AT-8 only coaggregates with pTau. A scheme describing the appearance of mixed aggregates in 2D histograms is included in Figure 3. Upon combining AT-8 and mTau, only DMSO induced tau aggregates are visible along the y-axis, similar to the control antibody 6E10. Measurements were taken from 12 independent samples; each sample was measured four times. Levels of significance are displayed as * = p < 0.05; ** = p < 0.01; ‡ = p < 0.001.
    Sift 2d Evaluation Software, supplied by Evotec 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/product/sift-2d/2d+sift+software+module/pmc03472288-158-20-23
    Average 90 stars, based on 1 article reviews
    sift-2d evaluation software - by Bioz Stars, 2026-09
    90/100 stars

    Images

    1) Product Images from "Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level"

    Article Title: Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level

    Journal: Molecular Neurodegeneration

    doi: 10.1186/1750-1326-7-35

    Tau phosphorylation verified by western blot and SIFT analysis. A. Mass spectroscopy showed that recombinant human tau (isoform 5, 42967 Da) is of high purity. B. While mock phosphorylation (mTau) does not influence SDS-PAGE mobility of recombinant tau, a typical band shift is observed upon tau phosphorylation (pTau). C. SIFT analysis showed labeling of pTau oligomers with the phosphorylated tau specific AT-8 antibody in presence of 1% DMSO indicating antibody binding, while no coaggregation was observed with mTau. Data was normalized against the coaggregation level of mTau with the T46 antibody, which does not require tau phosphorylation. 2D histograms depicting antibody (x-axis) and protein (y-axis) interactions show coaggregates of T46 with both pTau and mTau, while AT-8 only coaggregates with pTau. A scheme describing the appearance of mixed aggregates in 2D histograms is included in Figure 3. Upon combining AT-8 and mTau, only DMSO induced tau aggregates are visible along the y-axis, similar to the control antibody 6E10. Measurements were taken from 12 independent samples; each sample was measured four times. Levels of significance are displayed as * = p < 0.05; ** = p < 0.01; ‡ = p < 0.001.
    Figure Legend Snippet: Tau phosphorylation verified by western blot and SIFT analysis. A. Mass spectroscopy showed that recombinant human tau (isoform 5, 42967 Da) is of high purity. B. While mock phosphorylation (mTau) does not influence SDS-PAGE mobility of recombinant tau, a typical band shift is observed upon tau phosphorylation (pTau). C. SIFT analysis showed labeling of pTau oligomers with the phosphorylated tau specific AT-8 antibody in presence of 1% DMSO indicating antibody binding, while no coaggregation was observed with mTau. Data was normalized against the coaggregation level of mTau with the T46 antibody, which does not require tau phosphorylation. 2D histograms depicting antibody (x-axis) and protein (y-axis) interactions show coaggregates of T46 with both pTau and mTau, while AT-8 only coaggregates with pTau. A scheme describing the appearance of mixed aggregates in 2D histograms is included in Figure 3. Upon combining AT-8 and mTau, only DMSO induced tau aggregates are visible along the y-axis, similar to the control antibody 6E10. Measurements were taken from 12 independent samples; each sample was measured four times. Levels of significance are displayed as * = p < 0.05; ** = p < 0.01; ‡ = p < 0.001.

    Techniques Used: Western Blot, Mass Spectrometry, Recombinant, SDS Page, Electrophoretic Mobility Shift Assay, Labeling, Binding Assay

    Related Articles

    Concentration Assay:

    Article Title: Different Effects of α-Synuclein Mutants on Lipid Binding and Aggregation Detected by Single Molecule Fluorescence Spectroscopy and ThT Fluorescence-Based Measurements.
    Article Snippet: Six alpha-Synuclein point mutations are currently known to be associated with familial parkinsonism: A30P, E46K, H50Q, G51D, A53E and A53T.. We performed a comprehensive in vitro analysis to study the impact of all aSyn mutations on lipid binding and aggregation behavior.. Markedly reduced lipid binding of A30P, moderately attenuated binding of G51D and only very slightly reduced binding for the other mutants were observed.

    Article Title: Modelling Ser129 Phosphorylation Inhibits Membrane Binding of Pore-Forming Alpha-Synuclein Oligomers
    Article Snippet: Protein aggregation was analyzed as described previously using the software packages SIFT-2D and FCSPPEval Version 2.0 (Evotec Technologies, Hamburg, Germany) .

    Article Title: AMPA-receptor-mediated excitatory synaptic transmission is enhanced by iron-induced α-synuclein oligomers.
    Article Snippet: For SIFT analysis the software tool ‘SIFT-2D’ (Evotec-Technologies) was used.

    Software:

    Article Title: Different Effects of α-Synuclein Mutants on Lipid Binding and Aggregation Detected by Single Molecule Fluorescence Spectroscopy and ThT Fluorescence-Based Measurements.
    Article Snippet: Six alpha-Synuclein point mutations are currently known to be associated with familial parkinsonism: A30P, E46K, H50Q, G51D, A53E and A53T.. We performed a comprehensive in vitro analysis to study the impact of all aSyn mutations on lipid binding and aggregation behavior.. Markedly reduced lipid binding of A30P, moderately attenuated binding of G51D and only very slightly reduced binding for the other mutants were observed.

    Article Title: Modelling Ser129 Phosphorylation Inhibits Membrane Binding of Pore-Forming Alpha-Synuclein Oligomers
    Article Snippet: Protein aggregation was analyzed as described previously using the software packages SIFT-2D and FCSPPEval Version 2.0 (Evotec Technologies, Hamburg, Germany) .

    Article Title: AMPA-receptor-mediated excitatory synaptic transmission is enhanced by iron-induced α-synuclein oligomers.
    Article Snippet: For SIFT analysis the software tool ‘SIFT-2D’ (Evotec-Technologies) was used.



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    Tau phosphorylation verified by western blot and <t>SIFT</t> analysis. A. Mass spectroscopy showed that recombinant human tau (isoform 5, 42967 Da) is of high purity. B. While mock phosphorylation (mTau) does not influence SDS-PAGE mobility of recombinant tau, a typical band shift is observed upon tau phosphorylation (pTau). C. SIFT analysis showed labeling of pTau oligomers with the phosphorylated tau specific AT-8 antibody in presence of 1% DMSO indicating antibody binding, while no coaggregation was observed with mTau. Data was normalized against the coaggregation level of mTau with the T46 antibody, which does not require tau phosphorylation. <t>2D</t> histograms depicting antibody (x-axis) and protein (y-axis) interactions show coaggregates of T46 with both pTau and mTau, while AT-8 only coaggregates with pTau. A scheme describing the appearance of mixed aggregates in 2D histograms is included in Figure 3. Upon combining AT-8 and mTau, only DMSO induced tau aggregates are visible along the y-axis, similar to the control antibody 6E10. Measurements were taken from 12 independent samples; each sample was measured four times. Levels of significance are displayed as * = p < 0.05; ** = p < 0.01; ‡ = p < 0.001.
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    Tau phosphorylation verified by western blot and SIFT analysis. A. Mass spectroscopy showed that recombinant human tau (isoform 5, 42967 Da) is of high purity. B. While mock phosphorylation (mTau) does not influence SDS-PAGE mobility of recombinant tau, a typical band shift is observed upon tau phosphorylation (pTau). C. SIFT analysis showed labeling of pTau oligomers with the phosphorylated tau specific AT-8 antibody in presence of 1% DMSO indicating antibody binding, while no coaggregation was observed with mTau. Data was normalized against the coaggregation level of mTau with the T46 antibody, which does not require tau phosphorylation. 2D histograms depicting antibody (x-axis) and protein (y-axis) interactions show coaggregates of T46 with both pTau and mTau, while AT-8 only coaggregates with pTau. A scheme describing the appearance of mixed aggregates in 2D histograms is included in Figure 3. Upon combining AT-8 and mTau, only DMSO induced tau aggregates are visible along the y-axis, similar to the control antibody 6E10. Measurements were taken from 12 independent samples; each sample was measured four times. Levels of significance are displayed as * = p < 0.05; ** = p < 0.01; ‡ = p < 0.001.

    Journal: Molecular Neurodegeneration

    Article Title: Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level

    doi: 10.1186/1750-1326-7-35

    Figure Lengend Snippet: Tau phosphorylation verified by western blot and SIFT analysis. A. Mass spectroscopy showed that recombinant human tau (isoform 5, 42967 Da) is of high purity. B. While mock phosphorylation (mTau) does not influence SDS-PAGE mobility of recombinant tau, a typical band shift is observed upon tau phosphorylation (pTau). C. SIFT analysis showed labeling of pTau oligomers with the phosphorylated tau specific AT-8 antibody in presence of 1% DMSO indicating antibody binding, while no coaggregation was observed with mTau. Data was normalized against the coaggregation level of mTau with the T46 antibody, which does not require tau phosphorylation. 2D histograms depicting antibody (x-axis) and protein (y-axis) interactions show coaggregates of T46 with both pTau and mTau, while AT-8 only coaggregates with pTau. A scheme describing the appearance of mixed aggregates in 2D histograms is included in Figure 3. Upon combining AT-8 and mTau, only DMSO induced tau aggregates are visible along the y-axis, similar to the control antibody 6E10. Measurements were taken from 12 independent samples; each sample was measured four times. Levels of significance are displayed as * = p < 0.05; ** = p < 0.01; ‡ = p < 0.001.

    Article Snippet: Analysis was performed using FCSPP evaluation software version 2.0 (Evotec-Technologies), allowing auto-correlation, cross-correlation and fluorescence intensity distribution (FIDA) analysis, and SIFT-2D evaluation software (Evotec-Technologies).

    Techniques: Western Blot, Mass Spectrometry, Recombinant, SDS Page, Electrophoretic Mobility Shift Assay, Labeling, Binding Assay