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Related Experiment Video

Updated: Mar 7, 2026

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Profiling Cell Lines Nuclear Sub-proteome.

Aline Poersch1,2, Andrea G Maria3, Camila S Palma1,2

  • 1Department of Biochemistry and Immunology, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, SP, Brazil.

Methods in Molecular Biology (Clifton, N.J.)
|February 12, 2017
PubMed
Summary
This summary is machine-generated.

This study details a protocol for isolating and quantifying nuclear proteins using cell fractionation and mass spectrometry. This method aids in understanding protein localization critical for cell function and disease.

Keywords:
Cell LineMass spectrometryNuclear fractionationProtein localizationSubcellular proteomics

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Area of Science:

  • Cell Biology
  • Proteomics

Background:

  • Protein localization and trafficking are vital for cellular function.
  • Aberrant protein localization can cause disease.
  • Cellular fractionation combined with mass spectrometry enables protein localization and quantification.

Purpose of the Study:

  • To present a detailed protocol for nuclear proteome enrichment, identification, and quantitation.
  • To combine differential centrifugation with high-throughput proteomics for nuclear subproteome analysis.

Main Methods:

  • Differential centrifugation for nuclear subproteome enrichment.
  • High-throughput proteomics for identification and quantitation.
  • Application in cell lines.

Main Results:

  • A detailed protocol for nuclear proteome analysis was established.
  • The method allows for enrichment, identification, and quantitation of nuclear proteins.
  • Facilitates study of protein localization within cellular compartments.

Conclusions:

  • The presented protocol enables comprehensive analysis of the nuclear proteome.
  • This technique is valuable for studying protein localization in health and disease.
  • Advances the understanding of subcellular protein dynamics.