SOD3 (EC) Antibody, Clone 4GG11G6: PerCP

Superoxide dismutases (SODs) are essential antioxidant enzymes that protect cells from oxidative stress by catalyzing the dismutation of superoxide radicals (O₂⁻) into molecular oxygen (O₂) and hydrogen peroxide (H₂O₂), which are further detoxified by catalase and glutathione peroxidase. Among the three mammalian isoforms—SOD1 (cytoplasmic), SOD2 (mitochondrial), and SOD3 (extracellular) —SOD3 (extracellular superoxide dismutase, EC-SOD) plays a unique and increasingly recognized role in the central nervous system (CNS) . SOD3 is a copper- and zinc-containing homotetramer (~30 kDa) localized exclusively in the extracellular matrix, where it binds to heparan sulfate proteoglycans. This localization enables SOD3 to modulate redox signaling and protect neurons and glial cells from extracellular oxidative insults—key contributors to neuroinflammation and neurodegeneration. Emerging evidence links dysregulation of SOD3 expression and activity to the pathogenesis of neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, and amyotrophic lateral sclerosis (ALS) . Its extracellular positioning makes SOD3 a promising biomarker and therapeutic target for modulating oxidative stress in the brain. Understanding the distinct biochemical properties and neuroprotective functions of SOD3 is critical for advancing antioxidant-based strategies in neuroscience and neurodegenerative disease research.

SOD3, EC SOD, EC-SOD, Extracellular superoxide dismutase [Cu Zn], Extracellular superoxide dismutase [Cu-Zn], Extracellular superoxide dismutase, Extracellular superoxide dismutase precursor, MGC20077, SOD 3, SODE_HUMAN, Superoxide dismutase 3 extracellular

Cancer | Oxidative Stress | Cancer | Cancer Metabolism | Response to Hypoxia | Cell Signaling | Metabolism | Metabolism processes | Hypoxia | Cell Signaling | Metabolism | Redox Metabolism

1 µg/ml of SMC-167 was sufficient for detection of EC-SOD in 20 µg of human cartilage lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

1. Adachi T., et al. (1992) Clin Chim Acta. 212: 89-102. 2. Barrister J.V., et al. (1987). Crit. Rev. Biochem. 22:111-180. 3. FurukawaY., and O'Halloran T. (2006) Antioxidants & Redo Signaling. 8(5): 6. 4. Gao B., et al. (2003) Am J Physiol Lung Cell Mol Physiol 284: L917-L925. 5. Hassan H.M. (1988) Free Radical Biol. Med. 5: 377-385. 6. Wispe J.R., et al. (1989) BBA. 994: 30-36. 7. Regan, E. et al. (2005) Arthritis & Rheumatism 52(11): 3479–3491

1. Adachi T., et al. (1992) Clin Chim Acta. 212: 89-102. 2. Barrister J.V., et al. (1987) . Crit. Rev. Biochem. 22:111-180. 3. FurukawaY., and O'Halloran T. (2006) Antioxidants & Redo Signaling. 8 (5) : 6. 4. Gao B., et al. (2003) Am J Physiol Lung Cell Mol Physiol 284: L917-L925. 5. Hassan H.M. (1988) Free Radical Biol. Med. 5: 377-385. 6. Wispe J.R., et al. (1989) BBA. 994: 30-36. 7. Regan, E. et al. (2005) Arthritis & Rheumatism 52 (11) : 3479–3491