NanoBRET BRD4/Histone H3.3 Interaction Assay

Bromodomain (BRD)-containing proteins are critical components of nuclear protein complexes involved in the recruitment of chromatin-modifying enzymes and transcriptional regulation of acetylated chromatin. The protein:protein interaction (PPI) of the BRD-containing proteins with acetylated histones is an important method of epigenetic regulation critical for cell health and development and is of great interest for drug targeting because dysfunction in BRD modulation has been implicated as a critical event in disease formation. The NanoBRET Bromodomain BRD4/Histone Interaction Assays enable interaction studies of BRD-containing proteins with full-length histones in the context of natural chromatin. In addition to the full-length BRD protein, the BRD fragment alone is also included for users that may want to understand the interaction of this isolated domain. NanoBRET assay technology is dependent upon energy transfer from a luminescent donor (NanoLuc luciferase) to a fluorescent acceptor (HaloTag NanoBRET 618 Ligand). NanoLuc luciferase and HaloTag protein are fused to the target proteins of interest and fusion proteins expressed at low cellular levels, enabling monitoring and screening studies of protein interactions that reflect true cellular physiology. The NanoBRET assay is fully reversible, enabling studies of both induction and inhibition of protein interactions. For more details on NanoBRET Technology and a full list of available NanoBRET Bromodomain Interaction Assays visit the NanoBRET Technology for Protein Interactions page.