PRDX4 Human

Prx4 is ubiquitously expressed and is localized primarily in the endoplasmic reticulum (ER) and extracellular space . It is also found in various tissues, with the highest expression levels in the pancreas, liver, and heart, and the lowest in blood leukocytes and the brain .

Prx4 functions as an antioxidant enzyme, reducing hydrogen peroxide to water in a thiol-dependent catalytic cycle . This activity is vital for maintaining cellular redox balance and protecting cells from oxidative damage. Additionally, Prx4 has been linked to the regulation of the pro-inflammatory transcription factor, nuclear factor kappa B (NF-κB) .

Prx4 can switch between peroxidase and chaperone activities through redox-dependent and reversible conversion from disulfide-linked homodimers to higher-order multimers . This versatility allows Prx4 to interact with various binding partners, including stress-responsive kinases, membrane proteins, and immune modulators, thereby fine-tuning hydrogen peroxide signaling .

Recombinant human Peroxiredoxin-4 is produced using Escherichia coli expression systems and is typically purified to over 90% purity . This recombinant protein retains its biological activity and is used in various research applications, including SDS-PAGE and functional studies .

Prx4 has emerged as a potential biomarker for various diseases due to its differential expression in healthy individuals and patients with acute or chronic conditions . It has been linked to morbidity and mortality in patients with sepsis and non-specific complaints in emergency departments . The measurement of Prx4 levels, redox state, oligomerization, and nitro-oxidative modifications can provide valuable insights into the oxidative state of patients and the progression of diseases .