Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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...
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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Conditional Fragment Ion Probabilities Improve Database Searching for Nonmonoisotopic Precursors.

Journal of proteome research·2022
Same author

Increased <i>AR</i> expression in castration-resistant prostate cancer rapidly induces AR signaling reprogramming with the collaboration of EZH2.

Frontiers in oncology·2022
Same author

A multi-purpose, regenerable, proteome-scale, human phosphoserine resource for phosphoproteomics.

Nature methods·2022
Same author

Assessing interference in isobaric tag-based sample multiplexing using an 18-plex interference standard.

Proteomics·2021
Same author

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

Cell·2021
Same author

Improved Monoisotopic Mass Estimation for Deeper Proteome Coverage.

Journal of proteome research·2020

Related Experiment Video

Updated: May 28, 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

MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics.

Lily Ting1, Ramin Rad, Steven P Gygi

  • 1Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA.

Nature Methods
|October 4, 2011
PubMed
Summary
This summary is machine-generated.

Triple-stage mass spectrometry (MS3) effectively minimizes protein quantification interference in multiplexed proteome analysis. This advancement improves the accuracy of quantitative proteomics, especially when analyzing complex biological samples.

More Related Videos

Enhanced Sample Multiplexing of Tissues Using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)
09:06

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

Published on: May 1, 2017

Related Experiment Videos

Last Updated: May 28, 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

Enhanced Sample Multiplexing of Tissues Using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)
09:06

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

Published on: May 1, 2017

Area of Science:

  • Proteomics
  • Mass Spectrometry
  • Analytical Chemistry

Background:

  • Quantitative mass spectrometry is a powerful proteomics tool but lacks easy multiplexing capabilities.
  • Isobaric labeling enables multiplexed proteome quantification but suffers from ratio distortion due to interference.
  • Protein quantification interference is a significant challenge in multiplexed mass spectrometry-based proteomics.

Purpose of the Study:

  • To investigate and quantify the interference effect in a sixplex isobaric labeling system.
  • To evaluate the efficacy of triple-stage mass spectrometry (MS3) in mitigating interference.
  • To establish a robust method for accurate multiplexed proteome quantification.

Main Methods:

  • Development of a two-proteome model using a mixture of human and yeast proteins.
  • Application of a sixplex isobaric labeling strategy for sample preparation.
  • Utilizing triple-stage mass spectrometry (MS3) for enhanced data acquisition.

Main Results:

  • The study successfully documented the interference effect in a sixplex isobaric labeling system.
  • Triple-stage mass spectrometry (MS3) was found to almost completely eliminate the observed interference.
  • Accurate proteome quantification was achieved by mitigating ratio distortion.

Conclusions:

  • Triple-stage mass spectrometry (MS3) is a highly effective solution for overcoming protein quantification interference in isobaric labeling-based proteomics.
  • This method significantly enhances the reliability and accuracy of multiplexed proteome quantification.
  • The findings pave the way for more precise and comprehensive proteomic analyses.