SOD3 (E8M3G) Rabbit mAb #24000

Superoxide dismutase 3 (SOD3, EC-SOD) is a copper-containing antioxidant enzyme that plays a critical role in redox homeostasis in extracellular spaces (1). SOD3 localizes to the extracellular matrix through its C-terminal heparin binding domain, which interacts with proteoglycan on the cell surface (2). The enzyme catalyzes the dismutation of the superoxide radical (O₂-) to hydrogen peroxide in the extracellular space, prevents oxidative fragmentation damage of the extracellular matrix under stress conditions (3), and protects against oxidant-mediated endothelial dysfunction and tissue inflammation (4,5). SOD3 antioxidative activity preserves the bioavailability of nitric oxide (NO), providing permissive signals through the normalization of tumor vasculature, leading to enhanced tumor infiltration by effector T cells (6,7). Downregulation of SOD3 provides a selective advantage for multiple cancer types (8). A SOD3 knockout animal model displays resistance to chemotherapy response, while overexpression of SOD3 increases the tumor response to chemotherapy (9).