Peroxiredoxin5抗体;Peroxiredoxin5 Antibody—艾普蒂 新品

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     Western blot analysis of Peroxiredoxin 5 expression in HepG2 cell lysate.    

  
  

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     All lanes use the Antibody at 1:2K dilution for 1 hour at room temperature.    

  
  

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     All lanes use the Antibody at 1:2K dilution for 1 hour at room temperature.    

  
  

Peroxiredoxin 5 (PRDX5) is a member of the peroxiredoxin family, a group of evolutionarily conserved antioxidant enzymes critical for regulating cellular redox homeostasis. PRDX5 plays a key role in detoxifying reactive oxygen species (ROS), particularly hydrogen peroxide and peroxynitrite, through its peroxidase activity. Unlike other peroxiredoxins, PRDX5 exhibits a unique structural flexibility, allowing it to localize to multiple subcellular compartments, including mitochondria, cytoplasm, nucleus, and peroxisomes. This broad distribution underscores its involvement in diverse physiological processes, such as cell proliferation, apoptosis, inflammation, and DNA damage repair. Dysregulation of PRDX5 has been linked to oxidative stress-related pathologies, including cancer, neurodegenerative disorders, and cardiovascular diseases.

Antibodies targeting PRDX5 are essential tools for studying its expression, localization, and function in both normal and diseased states. These antibodies enable techniques like Western blotting, immunohistochemistry, and immunofluorescence to quantify protein levels, assess tissue-specific distribution, and investigate interactions with signaling pathways. High-quality PRDX5 antibodies are validated for specificity, often using knockout cell lines or siRNA-mediated knockdown to confirm target selectivity. Researchers also utilize them to explore PRDX5’s role as a potential biomarker or therapeutic target, particularly in conditions driven by oxidative damage. Commercial PRDX5 antibodies are typically raised against conserved epitopes, ensuring cross-reactivity across human, mouse, and rat samples, which facilitates translational and comparative studies. Proper validation remains critical to avoid off-target effects, given the structural similarities among peroxiredoxin family members.