protein

TRXR1/TXNRD1 Protein, Human (His)

HY-P77258

5 μg;10 μg;50 μg

50;85;240 USD

TRXR1/TXNRD1 Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg

50;85;240 USD

The homodimeric flavoprotein TRXR1/TXNRD1 plays a key role in cellular redox regulation, growth and differentiation. It reduces the disulfide protein thioredoxin (Trx) to its dithiol-containing form and exhibits reductase activity towards hydrogen peroxide (H2O2). TRXR1/TXNRD1 Protein, Human (His) is the recombinant human-derived TRXR1/TXNRD1 protein, expressed by E. coli , with N-His labeled tag. The total length of TRXR1/TXNRD1 Protein, Human (His) is 487 a.a., with molecular weight of ~55 kDa.

Human

The TRXR1/TXNRD1 protein functions as a homodimeric flavoprotein crucial for the regulation of cellular redox reactions, growth, and differentiation by reducing disulfideprotein thioredoxin (Trx) to its dithiol-containing form. This protein, containing a selenocysteine residue at the C-terminal active site essential for catalysis, exhibits reductase activity on hydrogen peroxide (H2O2). Beyond its redox regulatory role, TRXR1/TXNRD1 also induces actin and tubulin polymerization, contributing to the formation of cell membrane protrusions. These multifaceted activities underscore its significance in cellular processes, highlighting its involvement in maintaining redox homeostasis and influencing key aspects of cellular morphology and signaling.

Thioredoxin reductase 1, cytoplasmic; GRIM-12; Thioredoxin reductase TR1; TR; KDRF

Greater than 90% as determined by reducing SDS-PAGE

Supplied as a 0.22 μm filtered solution of PBS, pH 7.4.

Shipping with dry ice.