New Promega NanoBRET™ Technology Enables Real-Time Monitoring of Protein Interactions in Live Cells
Traditional methods for studying interactions between proteins are commonly performed in vitro using only protein fragments and do not provide data in the context of the cellular environment. With NanoBRET Protein Interaction Assays, researchers can study both induction and inhibition of protein interactions in real time using full-length proteins expressed at physiologically relevant levels.
Conventional BRET measures the interaction of proteins using a bioluminescent donor fused to a protein of interest and a fluorescent acceptor fused to its binding partner; the donor does not excite the fluorophore using light, but transfers resonance energy through dipole-dipole coupling. The optimized NanoBRET Protein Interaction Assays use NanoLuc® Luciferase as the energy donor and HaloTag® protein as the energy acceptor. NanoBRET Technology has improved spectral overlap, increased signal, and lower background, providing researchers with a reproducible method for monitoring and screening protein interactions. In addition, the brighter light output from NanoLuc enables use of NanoBRET even at low expression levels, while still providing efficient energy transfer.