Volume 127, Issue 41 pp. 12217-12220
Zuschrift

A Set of Homo-Oligomeric Standards Allows Accurate Protein Counting

Dr. Kieran Finan

Corresponding Author

Dr. Kieran Finan

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

Current address: UCL Medical School, Gower St., London (UK)

Single Molecule Biophysics, Institute for Physical and Theoretical Chemistry, Goethe-University Frankfurt, Max-von-Laue-Strasse 7, 60438 Frankfurt am Main (Germany)Search for more papers by this author
Anika Raulf

Anika Raulf

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

Search for more papers by this author
Prof. Dr. Mike Heilemann

Corresponding Author

Prof. Dr. Mike Heilemann

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

Single Molecule Biophysics, Institute for Physical and Theoretical Chemistry, Goethe-University Frankfurt, Max-von-Laue-Strasse 7, 60438 Frankfurt am Main (Germany)Search for more papers by this author
First published: 20 August 2015

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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