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Related Experiment Video

Updated: Apr 26, 2026

Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling

Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling

Published on: July 1, 2014

Quantitative proteomics using reductive dimethylation for stable isotope labeling.

Andrew C Tolonen¹, Wilhelm Haas²

¹CEA, DSV, IG, Genoscope; CNRS-UMR8030, Évry, France; Université d'Évry Val d'Essonne; atolonen@genoscope.cns.fr.

Journal of Visualized Experiments : Jove

|July 22, 2014

Summary

This summary is machine-generated.

Stable isotope labeling of peptides by reductive dimethylation (ReDi labeling) enables accurate protein quantification. This robust protocol offers a fast, inexpensive, and precise method for comparing complex protein mixtures using mass spectrometry.

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Last Updated: Apr 26, 2026

Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling

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Published on: July 1, 2014

Enhanced Sample Multiplexing of Tissues Using Combined Precursor Isotopic Labeling and Isobaric Tagging cPILOT

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Sample Preparation and Relative Quantitation using Reductive Methylation of Amines for Peptidomics Studies

Sample Preparation and Relative Quantitation using Reductive Methylation of Amines for Peptidomics Studies

Published on: November 4, 2021

Area of Science:

Proteomics
Analytical Chemistry
Biochemistry

Background:

Quantitative proteomics is crucial for understanding biological processes.
Accurate protein expression profiling requires reliable labeling techniques.
Stable isotope labeling methods are essential for comparative proteomics.

Purpose of the Study:

To present a robust protocol for reductive dimethylation (ReDi) labeling of peptides.
To demonstrate the accurate quantitative comparison of complex protein mixtures.
To highlight novel applications of ReDi labeling in proteomics.

Main Methods:

Peptide preparation via reversed-phase solid-phase extraction.
On-column ReDi labeling using light or heavy stable isotopes.
Peptide fractionation using basic pH reversed-phase (BPRP) chromatography.
StageTip purification and LC-MS/MS analysis.

Main Results:

Successful implementation of a robust ReDi labeling protocol.
Accurate quantification of relative protein abundances by comparing labeled peptide ion chromatogram peak areas.
Demonstration of ReDi labeling for complex protein mixture analysis.

Conclusions:

ReDi labeling provides a fast, inexpensive, and accurate method for protein quantification.
The protocol is applicable to a wide range of biological samples.
This technique advances comparative proteomics and biomarker discovery.