Making the production cost lower compared to use of mammalian systems, and allows us to offer selenoproteins at competitive prices compared to selenoproteins purified from native sources.
Our edge-cutting technology results from 30+ years of extensive research at Karolinska Institutet in Stockholm, Sweden, now making selenoproteins available for academic research and the global Pharma and R&D sectors.
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Overexpression of Recombinant Selenoproteins in E. coli
Cheng Q and Arnér ESJ.
Methods Mol Biol 2018.
Tagging recombinant proteins with a Sel-tag for purification, labeling with electrophilic compounds or radiolabeling with 11C
Cheng Q, et al.
Nat Protoc 2006.
Exploiting the 21st amino acid – purifying and labeling proteins by selenolate targeting
Johansson L, et al.
Nat Methods 2004.
Scheme of reactions catalyzed by mammalian TrxR or parasite TGR selenoproteins
Model of the selenoenzyme TrxR architecture, with its C-terminal arm containing Sec
From Zhong L, Arnér ES, Holmgren A. Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. Proc Natl Acad Sci U S A. 2000;97:5854-5
Scheme of quinone interactions with the Sec-containing active site of TrxR
From Cenas N, Nivinskas H, Anusevicius Z, Sarlauskas J, Lederer F, Arnér ES. Interactions of quinones with thioredoxin reductase: a challenge to the antioxidant role of the mammalian selenoprotein. J Biol Chem. 2004;279:2583-2592.
Coomassie-stained SDS-PAGE with pure GPX1 made by Dr. Qing Cheng, CTO at SeLENOZYME