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Protein Dynamics in Living Cells

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Related Experiment Video

Updated: Jul 2, 2026

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

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

Published on: November 15, 2017

A high-temporal resolution technology for dynamic proteomic analysis based on 35S labeling.

Zhao Zhang¹, Jian Chen, Fuzheng Guo

¹Universities' Confederated Institute of Proteomics, Key laboratory for Cell Proliferation and Regulation Biology Ministry of Education, Beijing Normal University, Beijing, People's Republic of China.

|August 21, 2008

Summary

A new method, Sulfur-35 in vivo Labeling Analysis for Dynamic Proteomics (SiLAD), offers high-resolution analysis of dynamic proteome changes in cells and tissues. This technique accurately quantifies protein expression rates for better biological process characterization.

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TMT Sample Preparation for Proteomics Facility Submission and Subsequent Data Analysis

TMT Sample Preparation for Proteomics Facility Submission and Subsequent Data Analysis

Published on: June 8, 2020

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Last Updated: Jul 2, 2026

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

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

Published on: November 15, 2017

TMT Sample Preparation for Proteomics Facility Submission and Subsequent Data Analysis

TMT Sample Preparation for Proteomics Facility Submission and Subsequent Data Analysis

Published on: June 8, 2020

Area of Science:

Proteomics
Cellular Biology
Biochemistry

Background:

Dynamic and differential proteomics require high-throughput, high-temporal-resolution methods.
Understanding dynamic proteome changes is crucial for analyzing cellular processes.

Purpose of the Study:

To design and validate a novel method for dynamic proteomics.
To assess the SiLAD technique's sensitivity, temporal resolution, and quantification capabilities.

Main Methods:

Development of Sulfur-35 in vivo Labeling Analysis for Dynamic Proteomics (SiLAD).
Application of SiLAD combined with 2-Dimensional Electrophoresis.
Analysis of synchronized A549 cells and rat liver partial hepatectomy models.

Main Results:

SiLAD demonstrated high sensitivity and a good signal-to-noise ratio for analyzing endogenous protein dynamics.
The technique effectively identified and re-categorized differential proteins.
SiLAD accurately quantified protein expression rates, reflecting cellular physiological shifts.

Conclusions:

SiLAD is a sensitive and effective method for studying dynamic proteome changes with high temporal resolution.
The technique allows for quantification of protein expression rates, offering deeper insights into biological processes.
SiLAD-derived proteome patterns can serve as unique markers for different stages of biological processes.