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Related Experiment Video

Updated: Jan 5, 2026

Determining Cell-surface Expression and Endocytic Rate of Proteins in Primary Astrocyte Cultures Using Biotinylation
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Determining Cell-surface Expression and Endocytic Rate of Proteins in Primary Astrocyte Cultures Using Biotinylation

Published on: July 3, 2017

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Studying Purinoceptor Cell-Surface Expression by Protein Biotinylation.

Mark T Young1

  • 1School of Biosciences, Cardiff University, Cardiff, UK. youngmt@cardiff.ac.uk.

Methods in Molecular Biology (Clifton, N.J.)
|October 25, 2019
PubMed
Summary

This study details a biotinylation method to quantify cell-surface protein expression. The technique measures how mutations affect cell-surface P2X2 receptor levels in mammalian cells.

Keywords:
BiotinylationCell-surfaceCrosslinkingMembrane proteinP2XProtein expressionWestern blot

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Biotinylation is a key technique for capturing and analyzing proteins.
  • It is essential for studying cell-surface membrane proteins, protein trafficking, and mutation effects.

Purpose of the Study:

  • To describe a procedure for biotinylation and capture of cell-surface rat P2X2 receptors.
  • To outline data analysis for measuring cell-surface protein expression of mutants relative to wild-type.

Main Methods:

  • Covalent labeling of cell-surface proteins with biotin.
  • Capture of biotinylated proteins using streptavidin-coated beads.
  • Analysis of protein levels to quantify cell-surface expression.

Main Results:

  • A detailed protocol for biotinylation and capture of rat P2X2 receptors is provided.
  • The method allows for the quantification of cell-surface expressed protein.
  • The proportion of cell-surface expressed protein for single point mutants can be measured relative to wild-type.

Conclusions:

  • This biotinylation method is effective for analyzing cell-surface protein expression.
  • It is particularly useful for studying the impact of mutations on membrane protein localization.
  • The described procedure facilitates the study of protein trafficking and function.