SOD1 (UbetaB) Antibody: APC

Superoxide dismutase 1 (SOD1) is a copper- and zinc-binding antioxidant enzyme that catalyzes the dismutation of superoxide radicals (O₂⁻) into hydrogen peroxide (H₂O₂) and molecular oxygen (O₂), thereby mitigating oxidative stress in the cytoplasm. Structurally, SOD1 functions as a 32 kDa homodimer, with each 16 kDa subunit stabilized by an intra-subunit disulfide bond and a β-barrel fold critical for its enzymatic activity and structural integrity. In neurodegenerative disease research—particularly amyotrophic lateral sclerosis (ALS) —SOD1 has emerged as a central player. Mutations in the SOD1 gene can lead to protein misfolding, aggregation, and toxic gain-of-function effects. A key pathological hallmark involves the exposure of normally buried regions of the β-barrel, including the unfolded β-barrel domain, which is implicated in early misfolding events. Conformation-specific antibodies such as Anti-SOD1 (UbetaB), which selectively binds the unfolded β-barrel region, are powerful tools for detecting misfolded SOD1 in affected tissues. When used alongside antibodies like Anti-SOD1 (EDI) (catalog# SPC-206), which targets the exposed dimer interface, researchers can map conformational states of SOD1 and track disease progression at the molecular level. Understanding and detecting these structural transitions in SOD1 is essential for advancing ALS diagnostics and developing targeted therapeutics in neurodegenerative disease research.

SOD1 (UbetaB), SOD1, Superoxide dismutase [Cu-Zn], Cu/Zn superoxide dismutase, SODC_HUMAN, ALS1, USOD, SOD1 unfolded beta barrel region, Misfolded SOD1, Conformationally altered SOD1, Apo-SOD1, Superoxide dismutase 1, SOD

1µg/ml of SPC-205 was sufficient for detection of the unfolded beta barrel of SOD1 by colorimetric dot blot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

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