Technology

We are the sole producer of active recombinant selenoproteins

And with our technology we could theoretically produce any of the 800+ natural selenoproteins yet identified in nature, or any synthetic selenocysteine-containing proteins on demand.

Our recombinant production system uses bacteria

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.

The use in our selenoprotein production technology of E. coli strains lacking RF1 and any endogenous use of TAG/UAG codons is enabled under a license agreement with Harvard College.

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Key References

Overexpression of Production and purification of homogenous recombinant human selenoproteins reveals a unique codon skipping event in E. coli and GPX4-specific affinity to bromosulfophthalein
Cheng Q and Arnér ESJ.
Redox Biology 2021.

Overexpression of Recombinant Selenoproteins in E. coli
Cheng Q and Arnér ESJ.
Methods Mol Biol 2018.

Selenocysteine Insertion at a Predefined UAG Codon in a Release Factor 1 (RF1)-depleted Escherichia coli Host Strain Bypasses Species Barriers in Recombinant Selenoprotein
Cheng Q and Arnér ES.
J Biol Chem 2017.

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

Scheme of reactions catalyzed by mammalian TrxR or parasite TGR selenoproteins

From Arnér ES. Focus on mammalian thioredoxin reductases–important selenoproteins with versatile functions. Biochim Biophys Acta. 2009;1790:495-526.

Model of the selenoenzyme TrxR architecture, with its C-terminal arm containing Sec

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

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

Coomassie-stained SDS-PAGE with pure GPX1 made by Dr. Qing Cheng, CTO at SeLENOZYME

In-house photo

Model of the C-terminal Sec-containing site of TrxR1

Model of the C-terminal Sec-containing site of TrxR1 as based on the crystal structure

From Cheng Q, Sandalova T, Lindqvist Y, Arnér ES. Crystal structure and catalysis of the selenoprotein thioredoxin reductase 1. J Biol Chem. 2009;284:3998-4008

Scheme of a Sel-tag in reduced selenolthiol

Scheme of a Sel-tag in reduced selenolthiol as well as oxidized selenenylsulfide forms

From Johansson, L., Chen, C., Thorell, J. et al. Exploiting the 21st amino acid—purifying and labeling proteins by selenolate targeting. Nat Methods 1, 61–66 (2004)

Sel-tagged proteins

Principle of making Sel-tagged proteins

From Cheng, Q., Stone-Elander, S. & Arnér, E. Tagging recombinant proteins with a Sel-tag for purification, labeling with electrophilic compounds or radiolabeling with 11C. Nat Protoc 1, 604–613 (2006)