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Related Concept Videos

Proteomics01:33

Proteomics

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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...
10.0K

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

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Quantitative Proteomics Using SILAC.

Kian Kani1

  • 1USC Center for Applied Molecular Medicine, USC Keck School of Medicine, 2250 Alcazar St. CSC-240, Los Angeles, CA, 90089, USA. kani@usc.edu.

Methods in Molecular Biology (Clifton, N.J.)
|February 12, 2017
PubMed
Summary

Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) enables quantitative proteomics by comparing isotopically labeled and unlabeled cells. This method allows precise measurement of protein levels without affecting cell physiology.

Keywords:
AMTMultiplexProteomicsQuantitativeSILAC

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Area of Science:

  • Proteomics
  • Cellular Biology
  • Biochemistry

Background:

  • Quantitative proteomics enables differential protein measurements, crucial for understanding cellular processes.
  • Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) is a leading technique for relative protein quantitation.
  • SILAC has become a preferred method for proteome-wide analysis using mass spectrometry.

Purpose of the Study:

  • To provide a detailed protocol for performing SILAC experiments.
  • To enable accurate proteome-wide quantitation of proteins.
  • To highlight the applications of quantitative proteomics.

Main Methods:

  • Metabolic incorporation of isotopically enriched amino acids into cellular proteomes.
  • Comparison of 'light' (unlabeled) and 'heavy' (labeled) cell proteomes.
  • Distinguishing labeled and unlabeled peptides using mass spectrometry.

Main Results:

  • SILAC allows for precise differential protein quantitation.
  • The technique is applicable to various applications, including protein turnover and co-immunoprecipitation.
  • Cellular uptake of labeled amino acids does not impact cell physiology.

Conclusions:

  • SILAC is a robust and widely adopted method for quantitative proteomics.
  • The provided protocol facilitates the implementation of SILAC experiments.
  • Quantitative proteomics offers powerful insights into cellular mechanisms.