Products
We are the world’s first producer of high quality and genuine sec-containing selenoproteins. Our recombinant selenoproteins have a specific activity very close to that of native enzymes purified from tissues.
We have the capacity to produce virtually any selenoprotein on demand by our customers, using a confidential
work-for-hire contract. Order directly from us or from any of our trusted distributors.
We offer in stock recombinant selenoproteins for rapid delivery and tailored production of unique selenoproteins available upon request
All our products are genuine selenocysteine containing selenoproteins, according to the specifications given below. Several other commercial vendors of recombinant selenoproteins incorrectly label them as selenoproteins, while they are typically sold as Sec-to-Cys or Sec-to-Ser substituted variants.
HUMAN TRXR1
The human TrxR1 selenoprotein is encoded by the TXNRD1 gene and exerts a wide range of functions in cytosolic redox control and antioxidant systems.
Other specific isoforms of TrxR1 can be made to order.
HUMAN TRXR2
The human TrxR2 selenoprotein is encoded by the TXNRD2 gene and exerts a wide range of functions in mitochondrial redox control and antioxidant systems.
We provide the main mitochondrial isoform of the human TrxR2 enzyme with more than 90% Sec contents and more than 95% purity in aliquots at amounts from 5 units to 50 units. The recombinant TrxR2 selenoprotein has a specific activity very close to that of native enzyme purified from tissues.
Other specific isoforms of TrxR2 can be made to order.
C. ELEGANS TRXR1
The TrxR enzyme in C. elegans is the single selenoprotein in this organism, exerting a wide range of functions in redox control and for antioxidant systems. It is also together with glutathione reductase essential for the molting process.
We provide the main isoform of the C. elegans TrxR enzyme with more than 90% Sec contents and more than 95% purity in aliquots at amounts from 5 units to 50 units. The recombinant C. elegans has a specific activity very close to that of native enzyme purified from tissues.
HUMAN GPX1
The human GPX1 selenoprotein is encoded by the GPX1 gene and has potent hydrogen peroxide reducing activity using glutathione.
We provide the human GPX1 enzyme with approx. 20% Sec contents, mixed with inactive forms containing Sec-to-Lys and Sec-to-Gln substitutions, at more than 95% purity in aliquots at amounts from 0.5 units to 5 units. The recombinant GPX1 has a substrate specificity very close to that of native enzyme purified from tissues, with a turnover assumed to be approx. 20% of native enzyme due to the ca. 20% Sec contents.
HUMAN GPX2
The human GPX2 selenoprotein is encoded by the GPX2 gene and has potent hydrogen peroxide reducing activity using glutathione.
We provide the human GPX2 enzyme with approx. 20% Sec contents, mixed with inactive forms containing Sec-to-Lys and Sec-to-Gln substitutions, at more than 95% purity in aliquots at amounts from 0.5 units to 5 units. The recombinant GPX2 has a substrate specificity very close to that of native enzyme purified from tissues, with a turnover assumed to be approx. 20% of native enzyme due to the ca. 20% Sec contents.
HUMAN GPX3
The human GPX3 selenoprotein is encoded by the GPX3 gene and has potent hydrogen peroxide reducing activity using glutathione.
We provide the human GPX3 enzyme with approx. 20% Sec contents, mixed with inactive forms containing Sec-to-Lys and Sec-to-Gln substitutions, at more than 95% purity in aliquots at amounts from 0.5 units to 5 units. The recombinant GPX3 has a substrate specificity very close to that of native enzyme purified from tissues, with a turnover assumed to be approx. 20% of native enzyme due to the ca. 20% Sec contents.
HUMAN GPX4
The human GPX4 selenoprotein is encoded by the GPX4 gene and has hydrogen peroxide and lipid hydroperoxide reducing activity using glutathione, protecting cells from ferroptosis.
We provide the human GPX4 enzyme with approx. 20% Sec contents, mixed with inactive forms containing Sec-to-Lys and Sec-to-Gln substitutions, at more than 95% purity in aliquots at amounts from 0.5 units to 5 units. The recombinant GPX4 has a substrate specificity very close to that of native enzyme purified from tissues, with a turnover assumed to be approx. 20% of native enzyme due to the ca. 20% Sec contents.
We also offer a recombinant high specific activity human GPX4 which is purified to yield close to 100% selenocysteine content. This product is offered on demand at amounts ranging from 2.5 units to 25 units.
For more information about this product, please see prof. Arnér’s and dr. Cheng’s article from 2021 listed under key references.
MOUSE GPX3
The mouse GPX3 selenoprotein is encoded by the GPX3 gene and has hydrogen peroxide reducing activity using glutathione. It is a secreted form of GPX that can be found in plasma.
We provide the mouse GPX3 enzyme with approx. 20% Sec contents, mixed with inactive forms containing Sec-to-Lys and Sec-to-Gln substitutions, at more than 95% purity in aliquots at amounts from 0.5 units to 5 units. The recombinant GPX3 has a substrate specificity very close to that of native enzyme purified from tissues, with a turnover assumed to be approx. 20% of native enzyme due to the ca. 20% Sec contents.
For more information about the production method resulting in this product, please see prof. Arnér’s and dr. Cheng’s article from 2021 listed under key references.
HUMAN DIO2
The human DIO2 selenocprotein is encoded by the DIO2 gene and catalyzes the conversion of prohormone thyroxine (3,5,3′,5′-tetraiodothyronine, T4) to the bioactive thyroid hormone (3,5,3′-triiodothyronine, T3) by outer ring 5′-deiodination.
We provide the human DIO2 enzyme with approx. 20% Sec contents, mixed with inactive forms containing Sec-to-Lys and Sec-to-Gln substitutions, at more than 95% purity in aliquots at amounts from 50 µg to 500 µg.
HUMAN DIO3
The human DIO3 selenoprotein is encoded by the DIO3 gene and catalyzes the inactivation of thyroid hormone by inner ring deiodination of the prohormone thyroxine (T4) and the bioactive hormone 3,3′,5-triiodothyronine (T3) to inactive metabolites, 3,3′,5′- triiodothyronine (RT3) and 3,3′-diiodothyronine (T2), respectively.
We provide the human DIO3 enzyme with approx. 20% Sec contents, mixed with inactive forms containing Sec-to-Lys and Sec-to-Gln substitutions, at more than 95% purity in aliquots at amounts from 50 µg to 500 µg.
RAT TRXR1
RAT TRXR2
The rat TrxR2 selenoprotein is encoded by the rat Txnrd2 gene and exerts a wide range of functions in mitochondrial redox control and antioxidant systems.
We provide the main mitochondrial isoform of the rat TrxR2 enzyme with more than 90% Sec contents and more than 95% purity in aliquots at amounts from 5 units to 50 units. The recombinant TrxR2 has a specific activity very close to that of native enzyme purified from tissues.
Other specific isoforms of TrxR2 can be made to order.
SHISTOSOMA MANSONI TGR
The TGR selenoprotein of Schistosoma mansoni is the only major reductive cytosolic flavoprotein of this parasite, taking over the combined role of TrxR1 and glutathione reductase. It is thereby exerting a wide range of functions in redox control and antioxidant systems and being a promising drug target for treatment of schistosomiasis.
We provide the main the Schistosoma mansoni TGR enzyme with more than 90% Sec contents and more than 95% purity in aliquots at amounts from 5 units to 50 units. The recombinant Shistosama mansoni TGR has a specific activity very close to that of native enzyme purified from tissues.
SEL-TAGGED SYNTHETIC SELENOPROTEINS
The C-terminal tetrapeptide motif of TrxRs (-Gly-Cys-Sec-Gly) can be utilized as a C- terminal “Sel-tag” of any recombinant protein of choice. It thereby enables purification of PAO-Sepharose and Sec-specific modifications using covalent targeting with electrophilic moieties, eg. for fluorescence labeling or radiolabeling. We are happy to make Sel-tagged proteins to order. For further information on the Sel-tag technology, see the following publications:
Preclinical PET imaging of EGFR levels: pairing a targeting with a non-targeting Sel-tagged Affibody-based tracer to estimate the specific uptake.
Cheng Q, Wållberg H, Grafström J, Lu L, Thorell JO, Hägg Olofsson M, Linder S, Johansson K, Tegnebratt T, Arnér ES, Stone-Elander S, Ahlzén HS, Ståhl S; Sel-tag imaging project. EJNMMI Res. 2016 Dec;6(1):58.
Site-specifically 11C-labeled Sel-tagged annexin A5 and a size-matched control for dynamic in vivo PET imaging of protein distribution in tissues prior to and after induced cell death.
Cheng Q, Lu L, Grafström J, Olofsson MH, Thorell JO, Samén E, Johansson K, Ahlzén HS, Linder S, Arnér ES, Stone-Elander S. Biochim Biophys Acta. 2013 Mar;1830(3):2562-73.
HER2-positive tumors imaged within 1 hour using a site-specifically 11C-labeled Sel-tagged affibody molecule.
Wållberg H, Grafström J, Cheng Q, Lu L, Martinsson Ahlzén HS, Samén E, Thorell JO, Johansson K, Dunås F, Olofsson MH, Stone-Elander S, Arnér ES, Ståhl S. J Nucl Med. 2012 Sep;53(9):1446-53.
Combining [11C]-AnxA5 PET imaging with serum biomarkers for improved detection in live mice of modest cell death in human solid tumor xenografts.
Cheng Q, Lu L, Grafström J, Olofsson MH, Thorell JO, Samén E, Johansson K, Ahlzén HS, Stone-Elander S, Linder S, Arnér ES; Sel-tag Imaging Project. PLoS One. 2012;7(8):e42151.
Tagging recombinant proteins with a Sel-tag for purification, labeling with electrophilic compounds or radiolabeling with 11C.
Cheng Q, Stone-Elander S, Arnér ES. Nat Protoc. 2006;1(2):604-13.
Selenolthiol and dithiol C-terminal tetrapeptide motifs for one-step purification and labeling of recombinant proteins produced in E. coli.
Cheng Q, Johansson L, Thorell JO, Fredriksson A, Samén E, Stone-Elander S, Arnér ES. Chembiochem. 2006 Dec;7(12):1976-81.
A mouse model for in vivo tracking of the major dust mite allergen Der p 2 after inhalation.
Johansson L, Svensson L, Bergström U, Jacobsson-Ekman G, Arnér ES, van Hage M, Bucht A, Gafvelin G. FEBS J. 2005 Jul;272(13):3449-60.
Exploiting the 21st amino acid-purifying and labeling proteins by selenolate targeting.
Johansson L, Chen C, Thorell JO, Fredriksson A, Stone-Elander S, Gafvelin G, Arnér ES. Nat Methods. 2004 Oct;1(1):61-6.
Learn more about our recombinant production system for sec-containing selenoproteins on our technology page.
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Please don’t hesitate to contact us and discuss it with our selenoprotein experts.
