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Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling
Published on: July 1, 2014
Quantitative proteomics by stable isotope labeling and mass spectrometry
1Institute for System Biology, Seattle, WA, USA.
Methods in Molecular Biology (Clifton, N.J.)
|December 23, 2006
Summary
Quantitative proteomics uses stable isotope labeling with mass spectrometry (MS) to measure protein changes. This chapter reviews key methods for introducing mass tags for accurate protein quantification.
Area of Science:
- Biochemistry and Molecular Biology
- Analytical Chemistry
Background:
- Quantitative proteomics aims to systematically analyze protein profiles under different conditions.
- Mass spectrometry (MS)-based methods are crucial for high-throughput protein analysis.
- Stable isotope labeling is a common technique for accurate protein quantification in MS.
Purpose of the Study:
- To review and discuss various methods for introducing mass tags in proteins and peptides for MS-based quantitative proteomics.
- To provide an overview of established and emerging stable isotope labeling strategies.
Main Methods:
- Isotope-coded affinity tags (ICAT)
- Stable isotope labeling by amino acids in cell culture (SILAC)
- Global internal standard technology
- Mass-coded abundance tagging (MCAT)
Main Results:
- These methods enable the introduction of mass tags for distinguishing and quantifying peptides/proteins from different samples using MS.
- Each technique offers specific advantages for different experimental designs and sample types.
Conclusions:
- Stable isotope labeling is fundamental to modern quantitative proteomics.
- A variety of mass tagging strategies are available to researchers for precise protein quantification via MS.
