Home / Application Notes / Protein-induced fluorescence enhancement detects protein-nucleic acid interactions in microplates

Protein-induced fluorescence enhancement detects protein-nucleic acid interactions in microplates

312 Protein-induced fluorescence enhancement detects protein-nucleic acid interactions in microplates
Fulneček J., Valuchová S., Petrov A.P., Tripsianes K., Říha K. Research group Molecular Biology of Plants, Central European Institute of Technology, Masaryk University, Brno, Czech Republic 10/2017

Various biological processes depend on the interaction of proteins with nucleic acids. These comprise packaging of DNA, transcriptional regulation, DNA replication and DNA repair. The binding of proteins to nucleic acids are hitherto detected by electrophoretic mobility shift assays (EMSAs), fluorescence polarization (FP) assays or chromatin immunoprecipitations (ChIP).

However, these methods are either laborious (EMSA, ChIP) or limited to specific targets (EMSA, FP, ChIP). A novel fluorescence assay detects interactions of nucleic acids with proteins to identify binding, sequence and structure specificities or dissociation constants. The microplate assay is a quick and cost-effective alternative and can be read on a fluorescence reader with the capability to scan wells such as the FLUOstar® Omega…

Applicable Products

The following BMG Labtech microplate reader products are applicable.