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Related Concept Videos

Two-dimensional Gel Electrophoresis01:22

Two-dimensional Gel Electrophoresis

Two-dimensional gel electrophoresis is a high-resolution protein separation method first introduced by O' Farrell and Klose in 1975. This method involves protein separation by two dimensions, mass and charge, making it more accurate than one-dimensional gel electrophoresis.
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as  cells...
SDS-PAGE01:27

SDS-PAGE

Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed  polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
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...
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...

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Related Experiment Video

Updated: May 21, 2026

Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting
10:51

Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting

Published on: April 10, 2014

Differential proteome analysis using 2D-DIGE.

Caroline May1, Frederic Brosseron, Piotr Chartowski

  • 1Department of Medical Proteomics/Bionalaytics, Medizinisches Proteom-Center, Ruhr-Universität Bochum, Bochum, Germany. caroline.may@rub.de

Methods in Molecular Biology (Clifton, N.J.)
|June 6, 2012
PubMed
Summary
This summary is machine-generated.

Difference in-gel electrophoresis (DIGE) enhances proteome analysis using fluorescent labeling for improved sensitivity and quantitation. This method allows multiplexing up to three samples per gel, offering significant advantages over traditional 2D-PAGE.

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Proteomic Profiling of Macrophages by 2D Electrophoresis
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Two-dimensional Gel Electrophoresis Coupled with Mass Spectrometry Methods for an Analysis of Human Pituitary Adenoma Tissue Proteome
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Two-dimensional Gel Electrophoresis Coupled with Mass Spectrometry Methods for an Analysis of Human Pituitary Adenoma Tissue Proteome

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Last Updated: May 21, 2026

Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting
10:51

Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting

Published on: April 10, 2014

Proteomic Profiling of Macrophages by 2D Electrophoresis
07:53

Proteomic Profiling of Macrophages by 2D Electrophoresis

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Two-dimensional Gel Electrophoresis Coupled with Mass Spectrometry Methods for an Analysis of Human Pituitary Adenoma Tissue Proteome
12:34

Two-dimensional Gel Electrophoresis Coupled with Mass Spectrometry Methods for an Analysis of Human Pituitary Adenoma Tissue Proteome

Published on: April 2, 2018

Area of Science:

  • Proteomics
  • Biochemistry
  • Analytical Chemistry

Background:

  • Classical 2D-PAGE enables proteome comparison and quantitation via gel staining and image analysis.
  • Fluorescent labeling techniques have advanced proteomic analysis capabilities.

Purpose of the Study:

  • To provide detailed protocols for 2D-DIGE.
  • To highlight the advantages of 2D-DIGE over traditional 2D-PAGE.

Main Methods:

  • Two-dimensional polyacrylamide gel electrophoresis (2D-PAGE)
  • Difference in-gel electrophoresis (DIGE) utilizing fluorescent reagents
  • Minimal and saturation labeling protocols

Main Results:

  • 2D-DIGE offers higher sensitivity than standard protein staining methods.
  • 2D-DIGE provides a wider linear range for accurate protein quantitation.
  • The technique allows for multiplexing of up to three samples on a single gel.

Conclusions:

  • 2D-DIGE represents a substantial improvement for proteome analysis.
  • Detailed protocols facilitate the implementation of 2D-DIGE for researchers.
  • Fluorescent labeling enhances the precision and scope of gel-based proteomic studies.