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Journal Article

Two-Dimensional Blue Native Polyacrylamide Gel Electrophoresis


Schamel,  Wolfgang W. A.
Research Group and Chair of Molecular Immunology of the University of Freiburg, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Schamel, W. W. A. (2008). Two-Dimensional Blue Native Polyacrylamide Gel Electrophoresis. Current Protocols in Cell Biology, 38, 6.10.1-6.10.21.

Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-900D-D
Multiprotein complexes play crucial roles in nearly all cell biological processes. Blue Native Polyacrylamide Gel Electrophoresis (BN-PAGE) is a powerful method to study these complexes. It is a native protein separation method that relies on the dye Coomassie blue to confer negative charge for separation. It has a higher resolution than gel filtration or sucrose density ultracentrifugation and can be used for protein complexes from 10 kDa to 10 MDa. If a second-dimension SDS-PAGE is applied (two-dimensional BN/SDS-PAGE), the size, subunit composition, and relative abundance of the different multiprotein complexes can be studied. In recent years, there has been a large increase in the number of publications where BN-PAGE was used to study protein-protein interactions. Here, we give detailed protocols for the separation of multiprotein complexes by two-dimensional BN/SDS-PAGE and for a related technique to determine the stoichiometry of these complexes.