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Related Concept Videos

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...
MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...

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Related Experiment Video

Updated: Jul 6, 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 protein profiling by mass spectrometry using isotope-coded affinity tags.

Arsalan S Haqqani1, John F Kelly, Danica B Stanimirovic

  • 1Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada.

Methods in Molecular Biology (Clifton, N.J.)
|March 29, 2008
PubMed
Summary
This summary is machine-generated.

Quantifying protein changes is crucial in proteomics. Isotope-coded affinity tagging (ICAT) coupled with mass spectrometry (MS) offers a sensitive method to measure relative protein levels, overcoming limitations of traditional gel electrophoresis.

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Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
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Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry

Published on: July 31, 2011

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Last Updated: Jul 6, 2026

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

Published on: November 15, 2017

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
06:09

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry

Published on: July 31, 2011

Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biochemistry

Background:

  • Quantifying protein expression changes in biological samples is essential for understanding cellular processes.
  • Traditional 2D gel electrophoresis (2-DE) has limitations in detecting low-abundance or insoluble proteins and is labor-intensive.

Purpose of the Study:

  • To present a detailed protocol for Isotope-Coded Affinity Tagging (ICAT) for quantitative proteomics.
  • To demonstrate the advantages of ICAT-mass spectrometry (MS) over 2-DE for protein quantification.
  • To highlight a targeted MS/MS approach for identifying differentially expressed proteins.

Main Methods:

  • Sample preparation and ICAT labeling of proteins from different biological conditions.
  • Fractionation and purification of labeled peptides.
  • Quantitative analysis using MS and targeted tandem MS (MS/MS) for protein identification.
  • Data analysis, statistical assessment, and protein database searching.

Main Results:

  • The ICAT method enables sensitive quantification of relative protein abundance in complex mixtures.
  • A targeted MS/MS approach provides more biologically relevant data compared to data-dependent analysis.
  • The protocol covers comprehensive steps from sample handling to data interpretation.

Conclusions:

  • ICAT-based quantitative proteomics is a powerful strategy to overcome limitations of 2-DE.
  • The described protocol facilitates accurate and sensitive measurement of protein expression changes.
  • Targeted MS/MS analysis enhances the biological relevance of proteomic studies.