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Related Experiment Video

Updated: Jul 2, 2026

Glycopeptide Capture for Cell Surface Proteomics
10:11

Glycopeptide Capture for Cell Surface Proteomics

Published on: May 9, 2014

Sample preparation method for plasma membrane proteome analysis.

Seung-Ah Park1, Mi-Ryung Kim, Pan-Kyeom Kim

  • 1School of Life Sciences and Biotechnology, Korea University, 1, 5-ga Anam-dong, Sungbuk-ku, Seoul 136-701, Republic of Korea.

Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences
|August 12, 2008
PubMed
Summary

Preparing plasma membrane (PM) proteome samples is challenging. A new method using Ultracentrifugation with Percoll and aqueous two-phase extraction offers a rapid, high-purity, and high-yield solution for PM proteome studies.

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Area of Science:

  • Proteomics
  • Cell Biology
  • Biochemistry

Background:

  • Plasma membrane (PM) protein isolation is crucial for cell biology research.
  • PM proteins are hydrophobic and low in abundance, making sample preparation difficult and time-consuming.

Purpose of the Study:

  • To develop an efficient, rapid, and high-purity method for plasma membrane proteome sample preparation.
  • To facilitate downstream analyses such as 2D gel electrophoresis.

Main Methods:

  • Ultracentrifugation with Percoll combined with aqueous two-phase extraction.
  • Optimization of sample preparation for plasma membrane proteins.

Main Results:

  • Achieved a rapid sample preparation time of 3 hours.

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Last Updated: Jul 2, 2026

Glycopeptide Capture for Cell Surface Proteomics
10:11

Glycopeptide Capture for Cell Surface Proteomics

Published on: May 9, 2014

"Cell Surface Capture" Workflow for Label-Free Quantification of the Cell Surface Proteome
06:31

"Cell Surface Capture" Workflow for Label-Free Quantification of the Cell Surface Proteome

Published on: March 24, 2023

  • Obtained high purity, with a 26-fold enrichment compared to cell lysate.
  • Secured a high yield, representing 2.6% of whole cell lysate proteins.
  • Conclusions:

    • The developed method provides an efficient and effective approach for plasma membrane proteome analysis.
    • This technique is particularly beneficial for studies utilizing 2D gel electrophoresis.
    • The method addresses the challenges of hydrophobicity and low abundance in PM protein isolation.