PRDX2 Rat

Peroxiredoxin-2 is known for its ability to react rapidly with hydrogen peroxide, with a rate constant greater than (10^7 , \text{M}^{-1} , \text{s}^{-1}) . It primarily exists in the cytosol as non-covalent dimers but can also form higher-order structures such as doughnut-like decamers and other oligomers . The protein’s primary function is to reduce hydrogen peroxide, lipid peroxides, and other peroxides, thereby protecting cells from oxidative stress .

The catalytic cycle of Prdx2 involves the oxidation of its peroxidatic cysteine residue to cysteine sulfenic acid by peroxides. This intermediate can then form a disulfide bond with a resolving cysteine residue from another Prdx2 molecule, which is subsequently reduced by thioredoxin . This cycle allows Prdx2 to continuously detoxify peroxides in the cell.

Prdx2 undergoes various post-translational modifications that can affect its activity. These modifications include phosphorylation, nitration, and acetylation . Such modifications can enhance the protein’s antioxidant activity and its ability to act as a chaperone for hemoglobin and other erythrocyte membrane proteins .

The extent of Prdx2 oxidation is often increased in various diseases, making it a potential biomarker for oxidative stress . Its ability to reduce peroxides and protect cells from oxidative damage underscores its importance in maintaining cellular health and preventing disease progression.

Recombinant Rat Peroxiredoxin-2 is typically expressed in Escherichia coli and purified to high levels of purity, making it suitable for various biochemical assays and research applications . This recombinant protein retains the functional properties of the native protein, allowing researchers to study its structure, function, and role in oxidative stress in a controlled environment .