The recombinant mouse Peroxiredoxin-1 protein is typically expressed with a C-terminal polyhistidine tag, which facilitates its purification. The protein consists of 199 amino acids and has a molecular weight of approximately 23.2 kDa . It is expressed in various host systems, including baculovirus and E. coli .
Peroxiredoxin-1 functions as a thioredoxin peroxidase, reducing peroxides through a conserved cysteine residue in its active site. This reduction process is essential for maintaining cellular redox balance and protecting cells from oxidative stress . The enzyme’s activity is defined by its ability to reduce hydroperoxides, with a specific activity greater than 2,500 pmol/min/µg .
Peroxiredoxin-1 is constitutively expressed in most human cells and is upregulated upon serum stimulation in both untransformed and transformed cells . It plays a significant role in the antiviral activity of CD8+ T-cells and may contribute to cancer development and progression due to its proliferative effects . Overexpression of Peroxiredoxin-1 has been associated with poor prognosis in several types of human cancers .