Superoxide dismutase 1, soluble Adenovirus
The superoxide dismutase family is composed of three metalloenzymes (SOD-1, SOD-2 and SOD-3) that catalyze the oxido-reduction of reactive oxygen species (ROS) such as superoxide anion. Unlike SOD-1, which is a homodimeric cytosolic Cu-Zn enzyme, SOD-2 is a 22 kDa homotetrameric manganese enzyme (also known as MnSOD) that functions in the mitochondrion. SOD-1 activity depends on the delivery of copper cofactors by Copper chaperone for SOD-1 (CCS). CCS prevents copper ions from binding to intracellular scavengers, thus securing copper for SOD-1.
Ready-to-use Superoxide dismutase 1, soluble Adenovirus. Ad-SOD1, “Superoxide dismutase 1, soluble “, ALS, SOD, ALS1, IPOA, SOD1 adenovirus 1503
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Gene Reference Data
Related Citations
- Genetic modification of human mesenchymal stem cells helps to reduce adiposity and improve glucose tolerance in an obese diabetic mouse model. Sabyasachi Se, etc, (2015), Stem Cell Research & Therapy
- Anti-Inflammatory Effect of Targeted Delivery of SOD to Endothelium: Mechanism, Synergism with NO Donors and Protective Effects In Vitro and In Vivo. Shuvaev VV, etc, (2013), PLoS ONE
- Role of superoxide radical anion in the mechanism of apoB100 degradation induced by DHA in hepatic cells. Ursula A, etc, (2011), FASEB Journal
- Catalase and Superoxide Dismutase Conjugated with Platelet-Endothelial Cell Adhesion Molecule Antibody Distinctly Alleviate Abnormal Endothelial Permeability Caused by Exogenous Reactive Oxygen Species and Vascular Endothelial Growth Factor. Han J, etc, (2011), Journal of Pharmacology
