HRP Anti-Peroxiredoxin 2/PRP antibody [EPR5154]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Peroxiredoxin 2 (also known as PRP or PRDX2) is an antioxidant enzyme that plays an important role in reducing peroxides and protecting cells from oxidative damage. The target consisting of approximately 22kDa mass is expressed heavily in erythrocytes but can also be found in other tissues like the heart and liver. PRDX2 belongs to the peroxiredoxin family and its redox activity contributes significantly to cellular homeostasis and defense against oxidative stress.

Biological function summary

Peroxiredoxins like PRDX2 function by breaking down hydrogen peroxide and organic hydroperoxides safeguarding cells from oxidative harm. PRDX2 often forms homodimers or higher-order oligomers which influence its catalytic efficiency and chaperone activity. Within the cell it not only acts independently but also associates with other cellular components reflecting its participation in important cellular processes including cell proliferation and apoptosis.

Pathways

PRDX2 engages significantly within antioxidant defense systems specifically the thioredoxin pathway. It interacts with thioredoxin reductase and thioredoxin to facilitate the reduction of peroxides maintaining the cell’s redox balance. Furthermore PRDX2 intersects with cellular signaling pathways associated with inflammation and the regulation of cell death where proteins like NRF2 and KEAP1 play important roles in managing oxidant-inducible gene expression.

Associated diseases and disorders

Disruptions in PRDX2 function connect to conditions like cancer and cardiovascular diseases. In cancer altered peroxiredoxin 2 expression correlates to tumor progression and resistance to chemotherapy implicating its interaction with proteins like NF-κB in enhancing cell survival. In cardiovascular diseases oxidative stress mediated by PRDX2 imbalance can lead to myocardial infarction and heart failure linking it to proteins such as SOD2 involved in mitochondrial defense.