Related Experiment Video
Updated: Aug 8, 2026

Quantitative FRET (Förster Resonance Energy Transfer) Analysis for SENP1 Protease Kinetics Determination
Published on: February 21, 2013
Using fluorescence resonance energy transfer (FRET) for measuring 2-5A analogues ability to activate RNase L
H Cramer1, D A Geselowitz, P F Torrence
1Section of Biomedical Chemistry, NIDDK, NIH, Bethesda, MD 20892, USA.
Abstract:
The development of a method for measuring the ability of 2-5A analogues to activate the cleavage of an oligoribonucleotide substrate by RNase L is described. This method is based on fluorescence resonance energy transfer. The method is easily performed with 96-well plates, allowing for quantitative high-throughput analyses of 2-5A analogues under different reaction conditions.
More Related Videos
06:10A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases
Published on: December 23, 2013
04:55Assessment of DNase Activity by Ratiometric Fluorescence Resonance Energy Transfer
Published on: July 25, 2025