SOD2 Human

SOD2 is a mitochondrial enzyme that forms a homotetramer, with each subunit binding one manganese ion . The manganese ion is essential for the enzyme’s catalytic activity, as it facilitates the conversion of superoxide radicals into less harmful molecules . The enzyme’s active site consists of a network of side chains that form hydrogen bonds, which are crucial for its function .

Mutations in the SOD2 gene have been linked to various health conditions, including idiopathic cardiomyopathy, premature aging, sporadic motor neuron disease, and cancer . Additionally, a missense variant in SOD2 (valine to alanine at position 16) is present in 45% of people with African ancestry and is associated with increased complications in sickle cell disease .

Recombinant human SOD2 is produced using E. coli as a host organism. This recombinant form is a homodimer consisting of two identical 154-amino acid chains . It is purified using proprietary chromatographic methods to ensure its efficacy and safety . Recombinant SOD2 is used in various research and therapeutic applications due to its ability to mitigate oxidative stress and its potential role in treating diseases associated with oxidative damage .

SOD2 is an essential component of the body’s defense against oxidative stress. In diseases like sickle cell disease, the antioxidant defense system is significantly diminished, leading to increased oxidative stress and associated complications . Enhancing SOD2 activity through recombinant forms or other therapeutic strategies holds promise for mitigating oxidative damage and improving health outcomes in such conditions .