SOD1 (Cu/Zn) Antibody: PerCP

Superoxide dismutase 1 (SOD1) is a copper- and zinc-dependent antioxidant enzyme that plays a vital role in cellular defense against oxidative stress. Present in nearly all mammalian cells, SOD1 catalyzes the dismutation of superoxide radicals (O₂⁻) into hydrogen peroxide (H₂O₂) and molecular oxygen (O₂) . These reactive oxygen species are subsequently detoxified by catalase and glutathione peroxidase, maintaining redox balance and protecting cells from oxidative damage. SOD1 functions as a 32 kDa homodimer, with each 16 kDa subunit stabilized by an intra-subunit disulfide bridge and a conserved β-barrel structure. It is primarily localized in the cytoplasm but also found in the nucleus and mitochondrial intermembrane space. Its structural integrity and metal-binding capacity are essential for enzymatic activity and cellular protection. In neuroscience and neurodegenerative disease research, SOD1 has gained prominence due to its association with amyotrophic lateral sclerosis (ALS) . Mutations in the SOD1 gene can lead to protein misfolding, aggregation, and toxic gain-of-function effects, contributing to motor neuron degeneration. These pathological forms of SOD1 are key biomarkers and therapeutic targets in ALS and related disorders. Understanding the structure-function relationship of SOD1, particularly its metal coordination and dimerization, is critical for developing targeted interventions in oxidative stress-related neurodegeneration.

0.2 µg/ml of SPC-116 was sufficient for detection of Cu/Zn SOD in 20 µg of HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:AP as the secondary antibody.

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