A set of homo-oligomeric standards allows accurate protein counting.

Angew Chem Int Ed Engl

Single Molecule Biophysics, Institute for Physical and Theoretical Chemistry, Goethe-University Frankfurt, Max-von-Laue-Strasse 7, 60438 Frankfurt am Main (Germany).

Published: October 2015

AI Article Synopsis

  • Researchers are turning to fluorescence microscopy techniques for counting proteins in cells, but there's a lack of accurate standards for validation.
  • A new set of bacterial homo-oligomers with 10-24 subunits has been created for testing the accuracy of these counting methods in mammalian cells.
  • These standards helped confirm that nuclear pores have 32 copies of the Nup107 complex, showcasing their practical application.

Article Abstract

Techniques based on fluorescence microscopy are increasingly used to count proteins in cells, but few stoichiometrically well-defined standards are available to test their accuracy. A selection of bacterial homo-oligomers were developed that contain 10-24 subunits and fully assemble when expressed in mammalian cells, and they can be used to easily validate/calibrate molecular counting methods. The utility of these standards was demonstrated by showing that nuclear pores contain 32 copies of the Nup107 complex.

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Source
http://dx.doi.org/10.1002/anie.201505664DOI Listing

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