PRDX5/Peroxiredoxin-5 Protein, Human (His)

The PRDX5 protein (or Peroxiredoxin-5) plays a critical role as a thiol-specific peroxidase that reduces hydrogen peroxide and organic hydroperoxides. This enzyme activity is essential for cells to defend against oxidative stress and detoxify peroxides. PRDX5/Peroxiredoxin-5 Protein, Human (His) is the recombinant human-derived PRDX5/Peroxiredoxin-5 protein, expressed by E. coli , with N-His labeled tag. The total length of PRDX5/Peroxiredoxin-5 Protein, Human (His) is 162 a.a., with molecular weight of ~18.5 kDa.

PRDX5, also known as Peroxiredoxin-5, serves as a thiol-specific peroxidase, facilitating the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. This enzymatic activity is integral to the cellular defense against oxidative stress, functioning as a protective mechanism by detoxifying peroxides. Beyond its role in peroxide reduction, PRDX5 acts as a sensor for hydrogen peroxide-mediated signaling events, highlighting its involvement in cellular signaling pathways associated with oxidative stress responses. The multifaceted functions of PRDX5 underscore its significance in maintaining cellular homeostasis and orchestrating adaptive responses to oxidative challenges.

Human

E. coli

N-His

P30044-2 (M53-L214)

25824  [NCBI]

Approximately 18.5 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.