+ +

•  

   

     Western blot analysis of Thymidine Kinase 1 in K562, Hela lysates using Thymidine Kinase antibody.    

  
  

Peroxiredoxin-2 (PRDX2) is a member of the peroxiredoxin family of antioxidant enzymes that play critical roles in regulating intracellular reactive oxygen species (ROS) levels by catalyzing the reduction of peroxides. PRDX2 is ubiquitously expressed in various tissues, particularly in erythrocytes, where it protects cellular components from oxidative damage. Structurally, PRDX2 functions as a homodimer and participates in redox signaling, cell proliferation, apoptosis, and inflammation regulation. Its dysregulation has been linked to multiple pathologies, including cancer, neurodegenerative disorders, and cardiovascular diseases, making it a potential biomarker or therapeutic target.

Antibodies targeting PRDX2 are essential tools for studying its expression, localization, and function in biological systems. These antibodies are widely used in techniques such as Western blotting, immunohistochemistry (IHC), immunofluorescence (IF), and enzyme-linked immunosorbent assays (ELISA). High-quality PRDX2 antibodies exhibit specificity for distinct epitopes, enabling the differentiation of PRDX2 from other peroxiredoxin isoforms. Researchers often validate these antibodies using knockout or knockdown models to confirm target specificity. Commercial PRDX2 antibodies may vary in clonality (monoclonal or polyclonal), host species, and conjugation formats, allowing flexibility in experimental design. However, batch-to-batch consistency and cross-reactivity remain critical considerations. By enabling precise detection of PRDX2. these antibodies contribute to advancing research on oxidative stress-related mechanisms and disease pathogenesis.