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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Updated: May 25, 2026

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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Analysis of protein posttranslational modifications using DIGE-based proteomics.

Robert M DeKroon1, Jennifer B Robinette, Cristina Osorio

  • 1Department of Cell and Developmental Biology, University of North Carolina, Chapel Hill, NC, USA.

Methods in Molecular Biology (Clifton, N.J.)
|February 8, 2012
PubMed
Summary

Difference gel electrophoresis (DIGE) can assess protein expression changes. This method is enhanced to detect specific post-translational modifications (PTMs) by labeling or altering protein properties.

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10:51

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Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

Area of Science:

  • Proteomics
  • Biochemistry
  • Molecular Biology

Background:

  • Difference gel electrophoresis (DIGE) is a common technique for quantifying relative protein expression levels in complex biological samples.
  • Protein activity is influenced not only by expression levels but also by post-translational modifications (PTMs).
  • Common PTMs include phosphorylation, ubiquitination, palmitoylation, and oxidation, which can significantly alter protein function.

Purpose of the Study:

  • To describe the adaptation of DIGE for the specific detection of post-translational modifications (PTMs).
  • To highlight how DIGE can provide insights into protein activity beyond mere expression level changes.

Main Methods:

  • Utilizing Difference gel electrophoresis (DIGE) with specific labeling strategies.
  • Introducing modifications to protein isoelectric point (pI) and/or molecular weight to distinguish PTMs.
  • Analyzing complex protein samples to identify changes indicative of specific PTMs.

Main Results:

  • Demonstration of DIGE's capability to identify specific PTMs within protein samples.
  • Validation of DIGE as a tool to infer changes in protein activity influenced by PTMs.
  • Successful application of DIGE for PTM analysis in complex biological contexts.

Conclusions:

  • DIGE can be effectively employed to detect and characterize specific post-translational modifications.
  • This adapted DIGE methodology expands the scope of proteomic analysis beyond expression profiling.
  • Understanding PTMs through DIGE offers a more comprehensive view of protein function and regulation.