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

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...

You might also read

Related Articles

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

Sort by
Same author

Digital Revitalization of a Legacy Linear Ion Trap System.

Analytical chemistry·2026
Same author

Optimized Low-Field Differential Ion Mobility Separations with High-Resolution Mass Spectrometry for Top-Down Proteomics.

Analytical chemistry·2026
Same author

Improving the Quadrupole to Ion Mobility Region in a Digital Quadrupole/Ion Mobility/Orbitrap Mass Spectrometer.

Journal of the American Society for Mass Spectrometry·2025
Same author

Superior Differential Ion Mobility Spectrometry of Pendular Macromolecules Using Low-Frequency Rectangular Waveforms.

Analytical chemistry·2025
Same author

Experimental Evaluation of Higher Order Stability Zones Using a Digitally Operated Quadrupole Mass Filter.

Journal of the American Society for Mass Spectrometry·2024
Same author

Increasing Isolation Efficiency Using a Segmented Quadrupole Mass Filter Operated with Rectangular Waveforms.

Journal of the American Society for Mass Spectrometry·2024
Same journal

Deep Plasma Proteomics-Based Diagnostic Panel for Early Detection of Amnestic Mild Cognitive Impairment.

Journal of proteome research·2026
Same journal

Proteomic and Phosphoproteomic Characterization of Disease-Associated Alterations in Nerve Terminals and Protein Inclusions of Alzheimer's Disease Patients.

Journal of proteome research·2026
Same journal

Proteomic Profiling of Endothelial Cells Under Laminar Shear Stress Confirms the Importance of KLF4 in the Regulation of Membrane Protein Expression Compared to Oscillatory Flow.

Journal of proteome research·2026
Same journal

Identification of Age-Associated Circulating Proteins and Lipids in 3800 Comorbidity-Enriched Older Adults from Japan-Based Cohorts Using Olink Assays and MRM Mass Spectrometry.

Journal of proteome research·2026
Same journal

Molecular Solution to the Paradox of Ancient Brain Preservation.

Journal of proteome research·2026
Same journal

From Method-Defined Signals to Reference Measurement Procedures: Two Decades of Mass Spectrometry-Based ProGRP Quantification.

Journal of proteome research·2026
See all related articles

Related Experiment Video

Updated: Jun 6, 2026

Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling
11:53

Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling

Published on: July 1, 2014

UNiquant, a program for quantitative proteomics analysis using stable isotope labeling.

Xin Huang1, Aleksey V Tolmachev, Yulei Shen

  • 1Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska 68198, USA.

Journal of Proteome Research
|December 17, 2010
PubMed
Summary
This summary is machine-generated.

A new program, UNiquant, enhances quantitative proteomics by accurately measuring protein abundance differences using stable isotope labeling (SIL). It outperforms existing tools, especially for complex samples, simplifying data analysis.

More Related Videos

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

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
11:54

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

Related Experiment Videos

Last Updated: Jun 6, 2026

Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling
11:53

Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling

Published on: July 1, 2014

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

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
11:54

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biochemistry

Background:

  • Stable isotope labeling (SIL) coupled with mass spectrometry is vital for comparative proteomics.
  • Accurate identification and quantification of peptides are crucial for reliable proteomic analysis.
  • Existing software for SIL-based quantitative proteomics requires further optimization for sensitivity and accuracy.

Purpose of the Study:

  • To develop and evaluate UNiquant, a novel software tool for analyzing quantitative proteomics data obtained via stable isotope labeling.
  • To assess the performance of UNiquant in comparison to established programs like MaxQuant and Mascot Distiller.
  • To determine UNiquant's ability to accurately quantify relative peptide and protein abundance.

Main Methods:

  • Utilized nanoscale liquid chromatography and high-resolution tandem mass spectrometry for proteomic analysis.
  • Employed SILAC (Stable Isotope Labeling by Amino acids in Cell culture) labeling on complex proteome mixtures.
  • Compared UNiquant's performance against MaxQuant and Mascot Distiller using Jeko-1 cell proteome digests with varying heavy/light ratios.

Main Results:

  • UNiquant identified a comparable number of peptide pairs to MaxQuant for low heavy/light ratios (1:1, 1:5).
  • UNiquant quantified significantly more peptides than MaxQuant and Mascot Distiller for a high heavy/light ratio (1:10).
  • UNiquant accurately measured relative peptide/protein abundance without requiring post-measurement normalization.

Conclusions:

  • UNiquant offers improved sensitivity and accuracy for quantitative proteomics using stable isotope labeling.
  • The software simplifies data analysis by eliminating the need for ratio normalization.
  • UNiquant represents a valuable advancement for proteome-wide difference analysis in biological samples.