Dear Elias,
we routinely produce a C-terminally His6-tagged catalytic domain of bovine enterokinase in E. coli. The protease is expressed into inclusion bodies and subsequently folded in vitro. Considering the high activity of our enterokinase construct, one refolding batch allows us to cleave several grams of target proteins.
If you're interested in our expression system, just send me an email.
best wishes,
Wolfgang Skala
--
Structural Biology Group / Department of Molecular Biology
University of Salzburg
Billrothstraße 11
5020 Salzburg
Austria
Email: [log in to unmask]
Phone: +43 662 8044 7278
http://www.uni-salzburg.at/xray
|