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Related Concept Videos

Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
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: Jun 13, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Quantitative analysis of mTRAQ-labeled proteome using full MS scans.

Un-Beom Kang1, Jeonghun Yeom, Hoguen Kim

  • 1Life Sciences Division, Korea Institute of Science and Technology, Seoul 136-791, Korea.

Journal of Proteome Research
|May 15, 2010
PubMed
Summary

This study introduces mTRAQ, a mass tag method for quantitative proteomics. mTRAQ improves peptide identification and enables wider proteome coverage, alone or with ICAT, for comparative profiling.

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Comprehensive Workflow of Mass Spectrometry-based Shotgun Proteomics of Tissue Samples
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Comprehensive Workflow of Mass Spectrometry-based Shotgun Proteomics of Tissue Samples

Published on: November 13, 2021

Related Experiment Videos

Last Updated: Jun 13, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Comprehensive Workflow of Mass Spectrometry-based Shotgun Proteomics of Tissue Samples
14:51

Comprehensive Workflow of Mass Spectrometry-based Shotgun Proteomics of Tissue Samples

Published on: November 13, 2021

Area of Science:

  • Proteomics
  • Mass Spectrometry
  • Biochemistry

Background:

  • Quantitative proteomics is crucial for comparing biological states like disease.
  • Mass spectrometry-based quantification often utilizes mass tags with stable isotopes.
  • Accurate quantification of proteome differences remains a significant challenge.

Purpose of the Study:

  • To introduce and validate mTRAQ for quantitative proteomics using full MS scans.
  • To assess the utility of mTRAQ for MS1-based relative quantification.
  • To compare mTRAQ with existing methods like ICAT for proteome profiling.

Main Methods:

  • Utilized mTRAQ reagent for labeling peptides in standard protein mixtures and human blood plasma.
  • Performed MS1-based relative quantification.
  • Combined mTRAQ with Isotope-Coded Affinity Tag (ICAT) for colon cancer tissue analysis.
  • Analyzed data using SEQUEST search.

Main Results:

  • mTRAQ-labeled peptides yielded higher quality MS2 spectra with improved XCorr values compared to unlabeled peptides.
  • mTRAQ demonstrated utility for MS1-based relative quantification.
  • Combining mTRAQ and ICAT identified and quantified 3,320 proteins in colon cancer tissues.
  • mTRAQ exhibited broader proteome coverage than ICAT, with only 1053 proteins overlapping.

Conclusions:

  • mTRAQ is effective for quantitative proteomics, particularly for MS1-based relative quantification.
  • mTRAQ enhances peptide spectral quality, aiding in protein identification.
  • mTRAQ, alone or combined with ICAT, offers a valuable approach for comparative proteome profiling.