Anti-TXNRD1 polyclonal antibody

Antibody Isotype

IgG

Species Reactivity

Human

Immunogen

Recombinant human protein purified from E.coli.

Conjugate

Alternative Names

TXNRD1; thioredoxin reductase 1; TRXR1; TR; TR1; TXNR; GRIM-12; MGC9145; thioredoxin reductase 1, cytoplasmic; oxidoreductase; thioredoxin reductase TR1; thioredoxin reductase GRIM-12; KM-102-derived reductase-like factor; Gene associated with retinoic an

Entrez Gene ID

UniProt ID

Antigen Description

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.

Pathway

Fatty acid, triacylglycerol; Metabolism; Metabolism of lipids and lipoproteins; Metabolism of nucleotides; Pyrimidine metabolism; Regulation of Lipid Metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha); Selenium Metabolism; Selenium Pathway; Selenocompound metabolism; Synthesis and interconversion of nucleotide di- and triphosphates; selenium