State of the art of 2D DIGE.
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.
School of Molecular and Biomedical Science, Adelaide Proteomics Centre, The University of Adelaide, Adelaide, Australia.
Georgia
G
Arentz
Florian
F
Weiland
Martin K
MK
Oehler
Peter
P
Hoffmann
D013058:Mass Spectrometry; D040901:Proteomics / Q000379:methods*; D057825:Two-Dimensional Difference Gel Electrophoresis / Q000379:methods*
2DE; DIGE; Gel electrophoresis; MS