Related Experiment Video
Updated: Sep 7, 2025
10:37
Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
Published on: November 15, 2017
12.1K
Advances in stable isotope labeling: dynamic labeling for spatial and temporal proteomic analysis
Nicole C Beller1, Amanda B Hummon1,2
1Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA, 43210. hummon.1@osu.edu.
Molecular Omics
|June 20, 2022
Summary
Stable isotope labeling in cell culture (SILAC) offers advanced quantitative proteomics. Pulsed SILAC (pSILAC) enables temporal analysis by tracking protein label incorporation over time, revealing dynamic proteomic changes.
Area of Science:
- Proteomics
- Biochemistry
- Analytical Chemistry
Background:
- Proteomics requires advanced quantitative methods.
- Stable isotope labeling in cell culture (SILAC) is a metabolic labeling technique.
- Traditional SILAC differentiates labeled and unlabeled cells using mass spectrometry.
Purpose of the Study:
- To review the evolution of SILAC and pulsed SILAC (pSILAC).
- To introduce advances in SILAC labeling techniques.
- To propose future perspectives in SILAC-based proteomics.
Main Methods:
- Stable isotope labeling in cell culture (SILAC) incorporates isotopically labeled amino acids.
- Pulsed SILAC (pSILAC) assesses the rate of protein label incorporation over time.
- Variations include super SILAC, spike-in SILAC, and spatial SILAC.
Main Results:
- Pulsed SILAC enables temporal analysis of proteomic changes.
- Heavy SILAC followed by unlabeled medium mimics pulse-chase experiments.
- pSILAC monitors initial label incorporation for rate assessment.
Conclusions:
- SILAC and its pulsed applications have expanded quantitative proteomics.
- Innovative SILAC techniques facilitate temporal and spatial proteomic studies.
- The field of SILAC-based proteomics continues to evolve with new applications.
