Thioredoxin 1 (clone 3A1), anti-human antibody
€355.00
In stock
SKU
AC-ABV11159-100
Catalog Number: AC-ABV11159-100
Size: 100 µl
Host: Mouse IgG
Applications: WB, E, IP
Datasheet
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Size: 100 µl
Host: Mouse IgG
Applications: WB, E, IP
Datasheet
Request Information
Background:
The mammalian thioredoxin reductases (TrxRs) are a family of seleno-cysteine containing pyridine nucleotide-disulfide oxido-reductases. 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 seleno-cysteine (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 kDa 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. TrxR1 plays a central role as a glucosyl donor in cellular metabolic pathways.
Other Names:
TXN, TRX, TRX1.
Primary Accession: O43396
Gene Name: TXNL1
Concentration (mg/ml): 1 mg/ml
The mammalian thioredoxin reductases (TrxRs) are a family of seleno-cysteine containing pyridine nucleotide-disulfide oxido-reductases. 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 seleno-cysteine (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 kDa 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. TrxR1 plays a central role as a glucosyl donor in cellular metabolic pathways.
Other Names:
TXN, TRX, TRX1.
Primary Accession: O43396
Gene Name: TXNL1
Concentration (mg/ml): 1 mg/ml
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