Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/90997
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Type: Journal article
Title: State of the art of 2D DIGE
Author: Arentz, G.
Weiland, F.
Oehler, M.
Hoffmann, P.
Citation: Proteomics - Clinical Applications, 2015; 9(3-4):277-288
Publisher: Wiley-VCH Verlag
Issue Date: 2015
ISSN: 1862-8346
1862-8354
Statement of
Responsibility: 
Georgia Arentz, Florian Weiland, Martin K. Oehler, and Peter Hoffmann
Abstract: Difference gel electrophoresis enables the accurate quantification of changes in the proteome including combinations of PTMs and protein isoform expression. Here, we review recent advances in study design, image acquisition, and statistical analysis. We also compare DIGE to established and emerging mass spectrometric analysis technologies. Despite these recent advances in MS and the still unsolved limitations of 2DE to map hydrophobic, high molecular weight proteins with extreme pIs, DIGE remains the most comprehensive top-down method to study changes in abundance of intact proteins.
Keywords: 2DE; DIGE; Gel electrophoresis; MS
Rights: © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
RMID: 0030015411
DOI: 10.1002/prca.201400119
Appears in Collections:Molecular and Biomedical Science publications

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