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Immunogen sequence: MHQAALLGGL IQDAPNYGWE VAQPVPHDWR KMAEAVQNHV KSLNWGHRVQ LQDRKVKYFN IKASFVDEHT VCGVAKGGKE ILLSADHIII ATGGRPRYPT HIEGALEYGI TSDDIFWLKE SPGKTLVVGA SYVALECAGF LTGIGLDTTI MMRSIPLRGF DQQMSSMVIE HMASHGTRFL RGCAPSRVRR LPDGQLRVTW EDSTTGKEDT GTFDTVLWAI GRVPDTRSLN LEKAGVDTSP DTQKILVDSR EATSVPHIYA IGDVVEGRPE LTPIAIMAGR LLVQRLFGGS SDLMDYDNVP TTVFTPLEYG CVGLSEEEAV ARHGQEHVEV YHAHYKPLEF TVAGRDASQC YVKMVCLREP PQLVLGLHFL GPNAGEVTQG FALGIKCGAS YAQVMRTVGI HPTCSEEVVK LRISKRSGLD PTVTGC*G
The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxidoreductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence (-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55-58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Selenoprotein Z; SelZ; Thioredoxin reductase 2, mitochondrial; thioredoxin reductase 3; thioredoxin reductase beta; Thioredoxin reductase TR3; TR-beta
Gene Aliases: KIAA1652; SELZ; TR; TR-BETA; TR3; TRXR2; TXNRD2
UniProt ID: (Human) Q9NNW7
Entrez Gene ID: (Human) 10587
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