A Set of Homo-Oligomeric Standards Allows Accurate Protein Counting

被引：32

作者：

Finan, Kieran ^{[1
]}

Raulf, Anika ^{[1
]}

Heilemann, Mike ^{[1
]}

机构：

[1] Goethe Univ Frankfurt, Inst Phys & Theoret Chem, Single Mol Biophys, D-60438 Frankfurt, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2015年 / 54卷 / 41期

关键词：

fluorescence microscopy; nuclear pores; proteins; protein counting; super-resolution imaging; NUCLEAR-PORE COMPLEX; ESCHERICHIA-COLI; FLUORESCENT PROTEIN; CRYSTAL-STRUCTURE; SINGLE; MICROSCOPY; MOLECULES; TURNOVER;

D O I：

10.1002/anie.201505664

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

页码：12049 / 12052

页数：4

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