Ettan Dige
Ettan Dige - Related Videos
10:51
Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting
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Cited by 8 •
2014
A common protein extraction protocol using urea/thiourea/SDS buffer for human and mice brain tissue allows indentification of proteins by 2D-DIGE and their subsequent characterization by mini 2DE immunoblotting. This method enables one to obtain more reproducible and reliable results from human biopsies and experimental models.
14:43
Selective Labelling of Cell-surface Proteins using CyDye DIGE Fluor Minimal Dyes
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Cited by 14 •
2008
A simple and specific method was demonstrated for fluorescent labeling and enhanced detection of cell surface proteins without a fractionation step. Differential abundance in cell surface proteins was analyzed using two-dimensional (2-D) electrophoresis and Ettan™ DIGE technology.
13:05
Ratiometric Imaging of Extracellular pH in Dental Biofilms
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Cited by 24 •
2016
A pH-sensitive ratiometric dye is used in combination with confocal laser scanning microscopy and digital image analysis to monitor extracellular pH in dental biofilms in real-time.
07:59
The Inverted Heart Model for Interstitial Transudate Collection from the Isolated Rat Heart
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2017
This protocol describes a method to collect cardiac interstitial fluid from the isolated, perfused rat heart. To physically separate interstitial transudate from coronary venous effluent perfusate, the Langendorff perfused heart is inverted, and the transudate (interstitial fluid) formed on the cardiac surface is collected using a soft latex cap.
FAQs
Each protein sample receives a spectrally distinct CyDye label, allowing signals from different samples to be distinguished after separation. An internal standard is included with the samples, providing a shared reference for comparing corresponding protein spots. This design supports relative abundance measurements within the same analytical framework and helps reveal expression changes more consistently than comparisons based only on separate gels.
Keeping labeled samples together reduces the influence of gel-to-gel differences, so observed signal changes are more closely tied to differences between the biological samples. Ettan Dige therefore supports more accurate differential proteomics, particularly when researchers need to compare protein abundance across complex samples and identify spots that change between conditions.
Fluorescence imaging assigns measurable signals to corresponding protein spots from the labeled samples. Comparing those signals indicates relative protein abundance and highlights expression changes within the analyzed material. In biology, this readout can help distinguish proteins that respond differently between samples, creating a focused set of changes for later biological interpretation or identification.
The workflow begins by labeling protein samples with spectrally distinct CyDyes and combining them with an internal standard. The mixture is subjected to isoelectric focusing, followed by SDS-PAGE in the same gel. Fluorescence imaging then records the separated spots, whose signals can be compared across samples to identify differences in protein abundance.
Ettan Dige can support studies of cellular responses, disease-associated protein changes, biomarker candidates, and molecular pathways. Its value is greatest when researchers need to compare protein abundance across complex biological samples and then interpret groups of changing spots in a biological context. The method therefore links differential proteomics with broader questions about cellular or disease biology.
After imaging highlights spots with altered abundance, researchers can use subsequent mass spectrometry to identify the proteins represented by those spots. Linking quantitative spot changes with protein identities helps connect expression differences to disease-associated changes, cellular responses, or molecular pathways, and supports evaluation of biomarker candidates.