| Literature DB >> 24940791 |
James H Felce1, Rachel G Knox2, Simon J Davis2.
Abstract
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.Entities:
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Year: 2014 PMID: 24940791 PMCID: PMC4070276 DOI: 10.1016/j.bpj.2014.04.061
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033