Introduction of a TEV cleavage site between the catalytic and the... | Download Scientific Diagram
TEV Protease | NEB
TEVプロテアーゼ | リコンビナント融合タンパク質からタグを切断 | コスモ・バイオ株式会社
TEV Protease (Glycerol free)
Recombinant EN-TEV Protease (mutated S219N) protein (Tagged-His Tag) (ab134877)
TEV (Tobacco Etch Virus) Protease, Active Tobacco Etch Virus (TEV) Protease, Active
Directed evolution improves the catalytic efficiency of TEV protease | Nature Methods
A TEV Protease Compatible with Inhibitory Compounds from Protein Purification
Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production | PLOS ONE
TEV Protease, His | Z03030
YESS 2.0, a Tunable Platform for Enzyme Evolution, Yields Highly Active TEV Protease Variants | ACS Synthetic Biology
TEV Protease - an overview | ScienceDirect Topics
TEV Protease Activity Assay Kit (Fluorometric) (ab211109) | Abcam
TEV Protease
Exploring the Mutations on Improving Oxidative Stability of Tobacco Etch Virus Protease for Tag- removal in Refolding of Two Dis
YESS 2.0, a Tunable Platform for Enzyme Evolution, Yields Highly Active TEV Protease Variants | ACS Synthetic Biology
NumaTEV Protease - Numaferm
주)펩진
Tobacco etch virus (TEV) protease with multiple mutations to improve solubility and reduce self‐cleavage exhibits enhanced enzymatic activity - Nam - 2020 - FEBS Open Bio - Wiley Online Library
SNAC-tag cleavage in fusion proteins a, TEV protease cleavage of... | Download Scientific Diagram
Activity of the Human Rhinovirus 3C Protease Studied in Various Buffers, Additives and Detergents Solutions for Recombinant Protein Production | PLOS ONE
Purification of His-TEV
The Xenopus laevis Atg4B Protease: Insights into Substrate Recognition and Application for Tag Removal from Proteins Expressed in Pro- and Eukaryotic Hosts | PLOS ONE
Comparison of the protease efficiency of TEV and C3. A) The Trx-EYFP... | Download Scientific Diagram
Mechanism-based traps enable protease and hydrolase substrate discovery | Nature
