sift-2d evaluation software (Evotec Inc)
Evotec Inc is a verified supplier 
90
Structured Review
Evotec Inc
sift-2d evaluation software
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+evaluation+software/2d+sift+software+module/pmc03472288-158-20-23
Average 90 stars, based on 1 article reviews
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+evaluation+software/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
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
Software:Article Title: Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level Article Snippet: Analysis was performed using Fluorescence:Article Title: Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level Article Snippet: Analysis was performed using Western Blot:Article Title: Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level Article Snippet: Analysis was performed using Mass Spectrometry:Article Title: Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level Article Snippet: Analysis was performed using Recombinant:Article Title: Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level Article Snippet: Analysis was performed using SDS Page:Article Title: Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level Article Snippet: Analysis was performed using Electrophoretic Mobility Shift Assay:Article Title: Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level Article Snippet: Analysis was performed using Labeling:Article Title: Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level Article Snippet: Analysis was performed using Binding Assay:Article Title: Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level Article Snippet: Analysis was performed using |