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Proteomics

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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Related Experiment Video

Updated: Jun 1, 2026

Protease- and Acid-catalyzed Labeling Workflows Employing 18O-enriched Water

Protease- and Acid-catalyzed Labeling Workflows Employing ¹⁸O-enriched Water

Published on: February 20, 2013

Trypsin-catalyzed oxygen-18 labeling for quantitative proteomics.

Wei-Jun Qian¹, Brianne O Petritis, Carrie D Nicora

¹Biological Sciences Division, Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA 99352, USA.

Methods in Molecular Biology (Clifton, N.J.)

|May 24, 2011

Summary

Oxygen-18 labeling is a simple and cost-effective method for quantitative proteomics. This technique enables accurate and reproducible measurements by creating a universal labeled reference sample for peptide abundance analysis.

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Last Updated: Jun 1, 2026

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Published on: February 20, 2013

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

Published on: May 1, 2017

Area of Science:

Proteomics
Analytical Chemistry
Biochemistry

Background:

Stable isotope labeling is crucial for quantitative proteomics.
Relative peptide/protein abundance measurements are commonly used.
Oxygen-18 labeling offers advantages in simplicity and cost-effectiveness.

Purpose of the Study:

To highlight the utility of trypsin-catalyzed oxygen-18 labeling in quantitative proteomics.
To explain the mechanism and benefits of (18)O labeling for peptide quantification.
To position (18)O labeling as an ideal method for creating universal reference samples.

Main Methods:

Enzymatic exchange of C-terminal carboxyl group atoms of tryptic peptides with (18)O.
Utilizing a 4 Da mass shift between (18)O-labeled and (16)O-labeled peptides.
Application in generating a labeled universal reference sample for discovery proteomics.

Main Results:

(18)O labeling provides universal labeling of peptides.
High sample recovery is achieved with this method.
The 4 Da mass shift allows for accurate quantification.

Conclusions:

Trypsin-catalyzed (18)O labeling is a simple, cost-effective, and efficient method for quantitative proteomics.
(18)O labeling facilitates the generation of universal reference samples.
This approach enables accurate and reproducible quantitative measurements across numerous samples.