SOD2 Mouse

Superoxide Dismutase-2 (SOD2), also known as manganese-dependent superoxide dismutase (MnSOD), is a crucial mitochondrial enzyme that plays a significant role in protecting cells from oxidative stress. This enzyme is encoded by the SOD2 gene and is a member of the iron/manganese superoxide dismutase family .

SOD2 is a mitochondrial protein that forms a homotetramer, with each subunit binding one manganese ion. The enzyme’s active site contains a manganese ion that participates in the dismutation of superoxide radicals into hydrogen peroxide and molecular oxygen . This process is vital for mitigating the damaging effects of reactive oxygen species (ROS) produced during cellular respiration.

The SOD2 gene contains five exons and four introns, with a GC-rich promoter region that lacks the typical TATA or CAAT boxes. The proximal promoter region includes binding sites for various transcription factors, such as specific-1 (Sp1), activator protein 2 (AP-2), and early growth response 1 (Egr-1) .

SOD2 is essential for maintaining cellular homeostasis by converting superoxide radicals, which are byproducts of oxidative phosphorylation, into less harmful molecules. This conversion helps prevent oxidative damage to cellular components, including DNA, proteins, and lipids . The enzyme’s activity is particularly crucial in tissues with high metabolic rates, such as the heart, liver, and brain.

Recombinant SOD2, particularly from mouse models, is widely used in research to study oxidative stress-related diseases and potential therapeutic interventions. Studies have shown that SOD2 plays a role in various pathological conditions, including idiopathic cardiomyopathy, premature aging, sporadic motor neuron disease, and cancer . Additionally, SOD2 has been investigated for its potential in anti-tumor, anti-radiation, and anti-aging therapies .