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Related Concept Videos

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
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...

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Related Experiment Video

Updated: May 13, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
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QuaNCAT: quantitating proteome dynamics in primary cells.

Andrew J M Howden1, Vincent Geoghegan, Kristin Katsch

  • 1Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.

Nature Methods
|March 12, 2013
PubMed
Summary
This summary is machine-generated.

This study quantifies protein changes in primary T cells using bio-orthogonal noncanonical amino acid tagging (BONCAT) and stable-isotope labeling (SILAC). The new quantitative noncanonical amino acid tagging (QuaNCAT) method tracked over 600 early protein expression changes after activation stimuli.

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Last Updated: May 13, 2026

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Area of Science:

  • Proteomics
  • Cellular Biology
  • Biochemistry

Background:

  • Understanding dynamic proteome changes in primary cells is crucial for immunology and disease research.
  • Existing methods for quantifying protein expression changes can be limited in scope or sensitivity.

Purpose of the Study:

  • To develop and validate a novel method for quantifying stimuli-induced proteome dynamics in primary cells.
  • To monitor early protein expression changes in activated T cells.

Main Methods:

  • Combined bio-orthogonal noncanonical amino acid tagging (BONCAT) with stable-isotope labeling of amino acids in cell culture (SILAC).
  • Utilized nanoscale liquid chromatography-tandem mass spectrometry (nanoLC-MS/MS).
  • Developed quantitative noncanonical amino acid tagging (QuaNCAT) for proteome analysis.

Main Results:

  • Successfully quantified proteome dynamics in primary resting T cells upon activation.
  • Monitored early expression changes of over 600 proteins.
  • Demonstrated the efficacy of the QuaNCAT method for sensitive proteomic analysis.

Conclusions:

  • The QuaNCAT method provides a powerful approach for studying dynamic proteome changes in primary cells.
  • This technique enables the monitoring of early cellular responses to stimuli at the proteome level.
  • The findings offer new insights into T cell activation pathways.