Anti-Superoxide Dismutase 1 antibody [2F5]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Superoxide Dismutase 1 (SOD1) also known as Cu/Zn SOD or simply dismutase is an enzyme important for the detoxification of superoxide radicals. SOD1 catalyzes the conversion of two superoxide molecules into oxygen and hydrogen peroxide maintaining cellular redox balance. This enzyme typically exhibits a mass of approximately 32 kDa. SOD1 is expressed in the cytoplasm of cells throughout the body including tissues like liver kidney and brain.

Biological function summary

The enzyme functions as a homodimer with each subunit containing a copper and zinc ion. These metal ions are essential for the catalytic activity of SOD1 as the copper ion participates in electron transfer while the zinc ion provides structural stability. The enzyme protects cells from oxidative stress by neutralizing excess reactive oxygen species ensuring cellular health and functioning.

Pathways

SOD1 plays an important role in the cellular antioxidant defense system and is a part of the reactive oxygen species (ROS) metabolic pathway. It works in conjunction with catalase and glutathione peroxidase to limit oxidative damage within cells. The close interaction between these enzymes highlights the interdependence within the antioxidant defense network emphasizing their role in maintaining cellular homeostasis.

Associated diseases and disorders

Mutations in the SOD1 gene are linked to familial Amyotrophic Lateral Sclerosis (ALS) a neurodegenerative condition. In ALS aberrant SOD1 proteins may lead to increased oxidative stress and motor neuron damage. Research also connects SOD1 to the pathogenesis of Alzheimer's disease where oxidative stress is a contributing factor. These associations underline SOD1's significance in neurodegenerative diseases highlighting potential therapeutic targets for interventions focused on oxidative stress management.