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Superoxide dismutase (Cu-Zn) (SOD1)

UniProt Number: P00441
Alternate Names: SOD1, hSOD1,
Structure and Function: SOD1 or Superoxide dismutase [Cu-Zn] is an enzyme that binds copper and zinc ions and is one of three superoxide dismutases responsible for destroying free superoxide radicals in the body. SOD1 is a soluble protein locates in cytoplasmic and mitochondrial intermembrane space. It acts as a homodimer to convert superoxide radicals, which are naturally produced but toxic to biological systems, within the cells to molecular oxygen and hydrogen peroxide.

The SOD family has 3 members, two of which are Cu-Zn type -cytoplasmic SOD1 and the extracellular. The other member is the mitochondrial Mn type SOD2.

Disease Associations: Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:105400]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms. Mice lacking SOD1 have increased age-related muscle mass loss (sarcopenia), early development of cataracts, macular degeneration, thymic involution, hepatocellular carcinoma, and shortened lifespan.

Protein Quantity Assays
Cat. No. Name Reactivity Amount
ab174440 Superoxide Dismutase 1 (SOD1) Human ELISA Kit Human 96 Tests

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