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Related Experiment Video

Updated: May 13, 2026

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

Identifying specific protein-DNA interactions using SILAC-based quantitative proteomics.

Cornelia G Spruijt1, H Irem Baymaz, Michiel Vermeulen

  • 1Department of Molecular Cancer Research, University Medical Center Utrecht, Utrecht, The Netherlands.

Methods in Molecular Biology (Clifton, N.J.)
|February 26, 2013
PubMed
Summary

Identifying protein-DNA interactions is challenging. This study introduces a SILAC-based method for unbiased identification of these crucial molecular interactions in various organisms.

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A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation

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Related Experiment Videos

Last Updated: May 13, 2026

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

Identification of protein complexes with quantitative proteomics in S. cerevisiae
11:12

Identification of protein complexes with quantitative proteomics in S. cerevisiae

Published on: March 4, 2009

A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation
14:44

A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation

Published on: September 24, 2012

Area of Science:

  • Molecular Biology
  • Genomics
  • Biochemistry

Background:

  • Understanding protein-DNA interactions is vital for cellular processes like transcription and replication.
  • Current methods for identifying these interactions face significant technical challenges.
  • These interactions are fundamental in both prokaryotic and eukaryotic systems.

Purpose of the Study:

  • To present a novel method for identifying protein-DNA interactions.
  • To overcome the limitations of existing techniques in this field.
  • To enable unbiased characterization of protein-DNA binding partners.

Main Methods:

  • Utilized Stable Isotope Labeling by Amino acids in Cell culture (SILAC) technology.
  • Developed a DNA affinity purification strategy.
  • Integrated SILAC with DNA affinity purification for quantitative analysis.

Main Results:

  • Successfully identified specific protein-DNA interactions.
  • Demonstrated the method's applicability in an unbiased manner.
  • Provided a robust approach for studying these interactions.

Conclusions:

  • The presented SILAC-based DNA affinity purification method is effective for identifying protein-DNA interactions.
  • This technique offers a powerful tool for advancing research in molecular biology and genomics.
  • It facilitates a deeper understanding of gene regulation and DNA replication mechanisms.