Production of Circularly Permuted Caspase-2 for Affinity Fusion-Tag Removal: Cloning, Expression in <i>Escherichia coli</i>, Purification, and Characterization

Production of Circularly Permuted Caspase-2 for Affinity Fusion-Tag Removal: Cloning, Expression in <i>Escherichia coli</i>, Purification, and Characterization

Caspase-2 is the most specific protease of all caspases and therefore highly suitable as tag removal enzyme creating an authentic N-terminus of overexpressed tagged proteins of interest. The wild type human caspase-2 is a dimer of heterodimers generated by autocatalytic processing which is required...

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Bibliographic Details
Main Authors: Monika Cserjan-Puschmann, Nico Lingg, Petra Engele, Christina Kröß, Julian Loibl, Andreas Fischer, Florian Bacher, Anna-Carina Frank, Christoph Öhlknecht, Cécile Brocard, Chris Oostenbrink, Matthias Berkemeyer, Rainer Schneider, Gerald Striedner, Alois Jungbauer
Format: Article
Language:English
Published: MDPI AG 2020-11-01
Series:Biomolecules
Subjects:
affinity tag removal
fusion protein
proteases
recombinant protein
solubility enhancing tag
His-tag
Online Access:https://www.mdpi.com/2218-273X/10/12/1592

Internet

https://www.mdpi.com/2218-273X/10/12/1592

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