|Detection of Human SOD3/EC‑SOD by Western Blot. Western blot shows lysates of human aorta tissue. PVDF membrane was probed with 0.1 µg/mL of Mouse Anti-Human SOD3/EC‑SOD Monoclonal Antibody (Catalog # MAB34201) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for SOD3/EC‑SOD at approximately 30 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Superoxide Dismutases (SODs), originally identified as Indophenoloxidase (IPO), are enzymes that catalyze the conversion of naturally-occuring, but harmful, superoxide radicals into molecular oxygen and hydrogen peroxide. Superoxide Dismutase 3 (SOD3) also known as extracellular (EC) SOD, is tetrameric glycoprotein with an apparent subunit molecular weight of about 30 kDa. Three isoenzymes of SOD have been identified and are functionally related but have very modest sequence homology. SOD3 shares 23% and 17% sequence identity with SOD1 and SOD2, respectively. Human SOD3 shares ~64% sequence homology with mouse and rat SOD3. Like SOD1, SOD3 binds one Cu2+ and Zn2+ ions per subunit but differs in sequence and tissue distribution. SOD3 is a secretory protein and is synthesized with a putative 18-amino acid signal peptide preceding the 222 amino acids in the mature SOD3. SOD3 is found in plasma, lymph, and synovial fluid as well as in tissues. SOD3 binds on the surface of endothelial cells through the heparan sulfate proteoglycan and eliminates the oxygen radicals from the NADP‑dependent oxidative system of neutrophils.
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