SuperoxideDismutase3抗体;SuperoxideDismutase3 Antibody—艾普蒂 新品

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     Western blot analysis of Superoxide Dismutase 3 expression in human fetal heart lysate.    

  
  

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

  
  

Superoxide Dismutase 3 (SOD3), also known as extracellular superoxide dismutase (EC-SOD), is a member of the SOD family of antioxidant enzymes that catalyze the dismutation of superoxide radicals into oxygen and hydrogen peroxide, thereby protecting cells from oxidative damage. SOD3 is distinct from other SOD isoforms (SOD1 and SOD2) due to its extracellular localization, heparin-binding domain, and tetrameric structure. Encoded by the *SOD3* gene in humans, it is primarily secreted by smooth muscle cells, fibroblasts, and macrophages, and is abundantly found in extracellular matrices, including blood vessels, lungs, and kidneys.

SOD3 plays a critical role in maintaining redox balance in extracellular environments, modulating inflammatory responses, and protecting tissues from oxidative stress-related damage. Its dysregulation has been implicated in various pathologies, such as chronic obstructive pulmonary disease (COPD), atherosclerosis, and neurodegenerative disorders.

Antibodies targeting SOD3 are essential tools for studying its expression, localization, and function. These antibodies are widely used in techniques like Western blotting, immunohistochemistry, and ELISA to quantify SOD3 levels in biological samples or visualize its distribution in tissues. Commercial SOD3 antibodies are typically raised against specific epitopes, such as the N-terminal or heparin-binding domains, and require validation via knockout controls or enzymatic activity assays to ensure specificity. Researchers utilize these antibodies to explore SOD3's role in oxidative stress mechanisms, disease progression, and potential therapeutic applications.