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We show that in conventional, competition-based bioluminescence resonance energy transfer (BRET) assays of membrane protein stoichiometry, the presence of competitors can alter tagged-protein density and artifactually reduce energy transfer efficiency. A well-characterized monomeric type I membrane protein, CD86, and two G protein-coupled receptors β2AR and mCannR2, all of which behave as dimers in these conventional assays, exhibit monomeric behavior in an improved competition-based type-3 BRET assay designed to circumvent such artifacts.

Original publication

DOI

10.1016/j.bpj.2014.04.061

Type

Journal article

Journal

Biophys J

Publication Date

17/06/2014

Volume

106

Pages

L41 - L43

Keywords

Animals, Energy Transfer, Luminescent Measurements, Membrane Proteins, Mice, Receptors, G-Protein-Coupled