Related Experiment Video
Updated: Mar 20, 2026
Investigating Protein-protein Interactions in Live Cells Using Bioluminescence Resonance Energy Transfer
Published on: May 26, 2014
Measuring NLR Oligomerization III: Detection of NLRP3 Complex by Bioluminescence Resonance Energy Transfer
Fátima Martín-Sánchez1, Vincent Compan2,3, Pablo Pelegrín4
1Inflammation and Experimental Surgery Unit,, Institute for Bio-Health Research of Murcia (IMIB-Arrixaca), Carretera Buenavista, s/n., El Palmar, Murcia, 30120, Spain. fatima.martin@ffis.es.
Abstract:
Bioluminescent resonance energy transfer (BRET) is a natural phenomenon resulting from a non-radiative energy transfer between a bioluminescent donor (Renilla luciferase) and a fluorescent protein acceptor. BRET signal is dependent on the distance and the orientation between the donor and the acceptor and could be used to study protein-protein interactions and conformational changes within proteins in real time in living cells. This protocol describes the use of BRET technique to study NLRP3 oligomerization in living cells before and during NLRP3 inflammasome activation.
More Related Videos
05:28Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay
Published on: September 10, 2020
06:44Author Spotlight: Integrating BRET-Based Assays and Rare Mutation Analysis to Decipher RAF Kinase Regulation in Live Cells
Published on: March 1, 2024