2d cross-correlation analysis Search Results


2d cross-correlation analysis  (MathWorks Inc)
90
MathWorks Inc 2d cross-correlation analysis
2d Cross Correlation Analysis, supplied by MathWorks Inc, 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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2d cross-correlation  (MathWorks Inc)
90
MathWorks Inc 2d cross-correlation
2d Cross Correlation, supplied by MathWorks Inc, 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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cross-correlation analysis  (MathWorks Inc)
90
MathWorks Inc cross-correlation analysis
Cross Correlation Analysis, supplied by MathWorks Inc, 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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mat2dcorr toolbox  (MathWorks Inc)
90
MathWorks Inc mat2dcorr toolbox
Mat2dcorr Toolbox, supplied by MathWorks Inc, 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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sift-2d evaluation software  (Evotec Inc)
90
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
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originpro 2021  (OriginLab corp)
90
OriginLab corp originpro 2021
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.
Originpro 2021, supplied by OriginLab corp, 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/originpro 2021/product/OriginLab corp
Average 90 stars, based on 1 article reviews
originpro 2021 - by Bioz Stars, 2026-03
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fcspp evaluation software version 2.0  (Evotec Inc)
90
Evotec Inc fcspp evaluation software version 2.0
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.
Fcspp Evaluation Software Version 2.0, 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/result/fcspp evaluation software version 2.0/product/Evotec Inc
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enfina spectrometer  (Gatan Inc)
86
Gatan Inc enfina spectrometer
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.
Enfina Spectrometer, supplied by Gatan Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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matlab r14  (MathWorks Inc)
90
MathWorks Inc matlab r14
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.
Matlab R14, supplied by MathWorks Inc, 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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2d fast-fourier-transform (fft) functions (fft2, ifft2)  (MathWorks Inc)
90
MathWorks Inc 2d fast-fourier-transform (fft) functions (fft2, ifft2)
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.
2d Fast Fourier Transform (Fft) Functions (Fft2, Ifft2), supplied by MathWorks Inc, 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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topspin 3.5 processing software  (Bruker Corporation)
90
Bruker Corporation topspin 3.5 processing 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.
Topspin 3.5 Processing Software, supplied by Bruker 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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nmr spectra  (Biofluids Inc)
90
Biofluids Inc nmr spectra
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.
Nmr Spectra, supplied by Biofluids Inc, 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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Image Search Results


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