Immunogen sequence: AALLGGLIQD APNYGWEVAQ PVPHDWRKMA EAVQNHVKSL NWGHRVQLQD RKVKYFNIKA SFVDEHTVCG VAKGGKEILL SADHIIIATG GRPRYPTHIE GALEYGITSD DIFWLKESPG KTLVVGASYV ALECAGFLTG IGLDTTIMMR SIPLRGFDQQ MSSMVIEHMA SHGTRFLRGC APSRVRRLPD GQLQVTWEDS TTGKEDTGTF D; Positive Samples: 293T, HepG2, Mouse spleen; Cellular Location: Mitochondrion
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.
蛋白别名: Selenoprotein Z; SelZ; Thioredoxin reductase 2, mitochondrial; thioredoxin reductase 3; thioredoxin reductase beta; Thioredoxin reductase TR3; TR beta; TR-beta
基因别名: AA118373; ESTM573010; KIAA1652; SELZ; TGR; TR; TR-BETA; TR3; TRXR2; Trxrd2; TXNRD2