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A set of homo-oligomeric standards allows accurate protein counting.
Finan, Kieran; Raulf, Anika; Heilemann, Mike.
Afiliación
  • Finan K; Single Molecule Biophysics, Institute for Physical and Theoretical Chemistry, Goethe-University Frankfurt, Max-von-Laue-Strasse 7, 60438 Frankfurt am Main (Germany). kieran.finan.13@ucl.ac.uk.
  • Raulf A; Current address: UCL Medical School, Gower St., London (UK). kieran.finan.13@ucl.ac.uk.
  • Heilemann M; Single Molecule Biophysics, Institute for Physical and Theoretical Chemistry, Goethe-University Frankfurt, Max-von-Laue-Strasse 7, 60438 Frankfurt am Main (Germany).
Angew Chem Int Ed Engl ; 54(41): 12049-52, 2015 Oct 05.
Article en En | MEDLINE | ID: mdl-26289028
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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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Poro Nuclear / Proteínas de Complejo Poro Nuclear / Synechococcus / Escherichia coli / Microscopía Fluorescente Límite: Humans Idioma: En Revista: Angew Chem Int Ed Engl Año: 2015 Tipo del documento: Article

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Poro Nuclear / Proteínas de Complejo Poro Nuclear / Synechococcus / Escherichia coli / Microscopía Fluorescente Límite: Humans Idioma: En Revista: Angew Chem Int Ed Engl Año: 2015 Tipo del documento: Article