SOD1 (EDI) Antibody

Superoxide dismutase 1 (SOD1) is a cytosolic antioxidant enzyme that catalyzes the dismutation of superoxide radicals (O₂⁻) into hydrogen peroxide (H₂O₂) and molecular oxygen (O₂), playing a vital role in cellular redox homeostasis. Structurally, SOD1 is a 32 kDa homodimer, with each 16 kDa subunit stabilized by copper and zinc ions, an intra-subunit disulfide bridge, and a tightly packed β-barrel fold. In neurodegenerative disease research—particularly amyotrophic lateral sclerosis (ALS) —SOD1 misfolding and aggregation are key pathological features. One critical conformational change involves the exposure of the dimer interface (EDI), a normally buried region essential for SOD1 stability and enzymatic function. This structural disruption is associated with toxic gain-of-function mechanisms and neuronal degeneration. Conformation-specific antibodies such as SOD1 (EDI) are designed to selectively recognize this exposed dimer interface, enabling researchers to detect early misfolding events in ALS-affected tissues. When used in combination with antibodies like SOD1 (UβB) (catalog# SPC-205), which targets the unfolded β-barrel region, these tools provide a powerful means of mapping SOD1 conformational states and tracking disease progression. Targeting the exposed dimer interface of SOD1 offers a promising strategy for understanding ALS pathogenesis and developing precision diagnostics and therapeutics in neurodegenerative disease research.

SOD1, Superoxide dismutase [Cu-Zn], Cu/Zn superoxide dismutase, SODC_HUMAN, ALS1, SOD1 EDI, SEDI, SOD1 exposed dimer interface, Conformationally altered SOD1, Misfolded SOD1, Apo-SOD1, Superoxide dismutase 1, SOD

1µg/ml of SPC-206 was sufficient for detection of the exposed dimer interface of SOD1 by colorimetric dot blot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

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