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Updated: Jul 20, 2025

Use of Recombinant Fusion Proteins in a Fluorescent Protease Assay Platform and Their In-gel Renaturation
Published on: January 16, 2019
TEV protease cleavage in generation of artificial substrate proteins bearing neo-N-termini
Lioba Inken Winckler1, Nico Dissmeyer1
1Department of Plant Physiology and Protein Metabolism Laboratory, University of Osnabruck, Osnabruck, Germany; CellNanOs-Center of Cellular Nanoanalytics, University of Osnabruck, Osnabruck, Germany; Faculty of Biology, University of Osnabruck, Osnabruck, Germany.
Abstract:
The tobacco etch virus (TEV) protease is widely used in in vitro and in vivo approaches for the removal of affinity tags from fusion proteins or the generation of proteins with a desired N-terminal amino acid. Processing of fusion proteins by the TEV protease can either be achieved by encoding the TEV protease and its recognition site on one construct (self-cleavage) or on two different constructs (co-expression). Here, we compare the efficiency of the self-splitting approach to the co-expression approach.
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