Results 261 to 270 of about 210,369 (310)

Two-Dimensional Difference Gel Electrophoresis

2012
Two-dimensional difference gel electrophoresis (2D DIGE) is a modified form of 2D electrophoresis (2DE) that allows one to compare two or three protein samples simultaneously on the same gel. The proteins in each sample are covalently tagged with different color fluorescent dyes that are designed to have no effect on the relative migration of proteins ...
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Dialysis‐assisted two‐dimensional gel electrophoresis

ELECTROPHORESIS, 2006
Abstract2‐DE is an important tool in proteomics research. However, intrinsic gel‐to‐gel variability of 2‐DE often masks the biological differences between the samples and compromises quantitative comparison of protein expression levels. Here, we describe a modification of 2‐DE that results in improved matching and quantification of proteins.
Olivier, Danos, Fedor, Svinartchouk
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Two-Dimensional Difference Gel Electrophoresis

2009
The introduction of two-dimensional fluorescent difference gel electrophoresis has enabled the extensive screening of differential protein expression levels with higher confidence and greater sensitivity than using the classical two-dimensional electrophoresis (2DE) approach.
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Two-dimensional gel electrophoresis of proteins

Journal of Chromatography B: Biomedical Sciences and Applications, 1987
The high-resolution capacity of two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) makes it an excellent tool for the analysis and characterisation of complex protein mixtures. The evolution of two-dimensional electrophoresis is briefly described.
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High Resolution Two-dimensional Polyacrylamide-gel Electrophoresis

TrAC Trends in Analytical Chemistry, 1983
Abstract The combination of two different gel electrophoretic techniques in a two-dimensional separation procedure provides the resolution capacity required for the simultaneous separation and analysis of complex protein mixtures. This technique is therefore a powerful tool for the study of phenotypic expression.
Michael J. Dunn, Arthur H.M. Burghes
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Two‐Dimensional Blue Native Polyacrylamide Gel Electrophoresis

Current Protocols in Cell Biology, 2008
AbstractMultiprotein complexes play crucial roles in nearly all cell biological processes. Blue Native Polyacrylamide Gel Electrophoresis (BN‐PAGE) is a powerful method to study these complexes. It is a native protein separation method that relies on the dye Coomassie blue to confer negative charge for separation.
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Two-dimensional agarose gel electrophoresis without gel manipulation

Analytical Biochemistry, 1985
The apparatus and procedure to perform two-dimensional agarose gel electrophoresis without manipulating the gel used for the first electrophoresis (first-dimension gel) have been developed. The procedure is less complex, less damaging to first-dimension gels, and more precise than procedures that require manipulation of the first-dimension gel.
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Two-dimensional gel electrophoresis of membrane proteins

Biochemistry, 1976
A high-resolution method for two-dimensional separation of membrane proteins is described. It involves a nondiscriminating solubilization of a membrane preparation with sodium dodecyl sulfate, followed by electrophoresis in the first dimension according to charge (by isoelectric focusing).
G F, Ames, K, Nikaido
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Sample preparation for two‐dimensional gel electrophoresis

PROTEOMICS, 2003
Abstract The choice of sample preparation protocol is a critical influential factor for isoelectric focusing which in turn affects the two‐dimensional gel result in terms of quality and protein species distribution. The optimal protocol varies depending on the nature of the sample for analysis and the properties of the constituent ...
Margaret M, Shaw, Beat M, Riederer
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6 Two-dimensional gel electrophoresis

2005
Summary 2-DE continues to set the benchmark as the premier technique for protein separation in protoemic applications. The approach is very well sited for routine separation of moderately abundant proteins within a window of pH 3-10 and M r =10-200 kDa, allowing for cataloging and quantitative measures of protein expression.
Mark P. Molloy, Michael T. McDowell
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