SOD2 (Mn) Antibody: RPE

Superoxide dismutase 2 (SOD2), a manganese-dependent enzyme localized in the mitochondrial matrix, is a critical component of the cellular antioxidant defense system. It catalyzes the dismutation of superoxide radicals (O₂⁻), a byproduct of mitochondrial respiration, into hydrogen peroxide (H₂O₂) and molecular oxygen (O₂) . This reaction is essential for mitigating oxidative stress, particularly in neurons, which are highly susceptible to mitochondrial dysfunction and reactive oxygen species (ROS) accumulation. Among the three mammalian SOD isoforms—SOD1 (Cu/Zn, cytosolic), SOD2 (Mn, mitochondrial), and SOD3 (Cu/Zn, extracellular) —SOD2 is uniquely positioned to protect mitochondrial integrity. Its tetrameric structure and localization enable it to neutralize ROS at their primary source, making it a focal point in studies of neurodegenerative diseases such as Alzheimer's, Parkinson's, and amyotrophic lateral sclerosis (ALS) . Deficiencies or mutations in SOD2 have been linked to increased oxidative damage, mitochondrial impairment, and neuronal cell death. As a result, SOD2 is not only a biomarker of oxidative stress but also a promising therapeutic target in neuroscience. Enhancing SOD2 activity or expression is a growing area of interest in the development of neuroprotective strategies. Understanding the role of SOD2 in redox homeostasis is essential for advancing treatments for neurodegenerative disorders and improving mitochondrial health in aging and disease.

0.5 µg/ml of SPC-117 was sufficient for detection of Mn SOD in 20 µg of rat brain tissue extract by colorimetric immunoblot analysis using Goat anti-rabbit IgG:AP as the secondary antibody.

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