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Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics
12:53

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

Published on: July 6, 2014

Proteome-wide quantitation by SILAC.

Kristoffer T G Rigbolt1, Blagoy Blagoev

  • 1Center for Experimental BioInformatics, Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.

Methods in Molecular Biology (Clifton, N.J.)
|September 15, 2010
PubMed
Summary
This summary is machine-generated.

Stable isotope labeling by amino acids in cell culture (SILAC) enables quantitative proteome-wide analysis using mass spectrometry. This method facilitates accurate measurement of protein expression differences in various cell lines.

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Area of Science:

  • Proteomics
  • Biochemistry
  • Analytical Chemistry

Background:

  • Advancements in LC-MS/MS increase proteome coverage.
  • Quantitative assessment of proteome-wide differences is crucial.
  • Stable isotope labeling by amino acids in cell culture (SILAC) is a key technique.

Purpose of the Study:

  • To provide a detailed protocol for SILAC-based proteome-wide quantitation.
  • To offer guidance on optimizing SILAC labeling.
  • To present recent developments in SILAC methodology.

Main Methods:

  • Utilizes cellular metabolism for incorporating isotopically labeled amino acids.
  • Combines labeled and unlabeled proteomes for comparative analysis.
  • Employs mass spectrometry for quantifying protein abundance differences.

Main Results:

  • SILAC allows for accurate and versatile proteome-wide quantitation.
  • The technique has been successfully applied across diverse cell lines.
  • Optimization protocols enhance the efficiency of SILAC labeling.

Conclusions:

  • SILAC is a powerful tool for quantitative proteomic studies.
  • The chapter provides a comprehensive guide to SILAC implementation.
  • Ongoing developments continue to expand SILAC's applications.