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Two‐Dimensional Gel Electrophoresis

Current Protocols in Protein Science, 1998
AbstractTwo‐dimensional gel electrophoresis combines two different electrophoretic separating techniques in perpendicular directions to provide a much greater separation of complex protein mixtures than either of the individual procedures. Variations of the most common two‐dimensional technique are described in this unit, namely isoelectrofocusing (IEF)
S, Harper, J, Mozdzanowski, D, Speicher
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Two‐Dimensional Gel Electrophoresis

Current Protocols in Immunology, 2004
AbstractTwo‐dimensional gel electrophoresis is the combination of two high‐resolution electrophoretic procedures (isoelectric focusing and SDS‐polyacrylamide gel electrophoresis) to provide much greater resolution than either procedure alone. In the first‐dimension gel, solubilized proteins are separated according to their isoelectric point (pI) by ...
Lonnie D, Adams, Sean R, Gallagher
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Two-Dimensional Difference Gel Electrophoresis

Nature Protocols, 2006
The two-dimensional (2D) polyacrylamide gel-based approach to protein profiling has been successful because it is an accessible, inexpensive, and powerful tool for the analysis of global patterns of protein expression. All protein spots that are resolved and detected within the 104 to 105 dynamic range of gel capacity can be studied qualitatively and ...
Surya, Viswanathan   +2 more
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Two-Dimensional Gel Electrophoresis

Science, 1962
Improved resolution of serum protein mixtures is effected by electrophoresis, first in a 5 percent acrylamide gel following which a strip of the resolved pattern is embedded in 8 percent gel and subjected to a second electrophoresis separation at right angles to the first.
S, Raymond, B, Aurell
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Two-Dimensional Difference Gel Electrophoresis

2018
Two-dimensional difference gel electrophoresis (2D DIGE) is a modified form of 2D electrophoresis (2D E) 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
Malachi, Blundon   +4 more
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Two-Dimensional Gel Electrophoresis Image Analysis

2021
Gel-based proteomics is still quite widespread due to its high-resolution power; the experimental approach is based on differential analysis, where groups of samples (e.g., control vs diseased) are compared to identify panels of potential biomarkers.
Robotti E., Cala Elisa, Marengo E.
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Alignment of two-dimensional electrophoresis gels

Biochemical and Biophysical Research Communications, 2007
Two-dimensional electrophoresis is a major separating technique for proteins in proteomics. Alignment of gel images is critical for intra-laboratory or even more difficult inter-laboratory gel comparisons. In the paper, we propose a novel iterative closest point (ICP) method for 2D-gel electrophoresis image alignment.
Shi, Guihua   +4 more
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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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