|Detection of Mouse SOD3/EC‑SOD by Western Blot. Western blot shows lysates of mouse lung and kidney tissue. PVDF membrane was probed with 1 µg/mL Goat Anti-Mouse SOD3/EC‑SOD Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4817) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). For additional reference, recombinant mouse SOD1, SOD2, and SOD3 (5 ng/lane) were included. A specific band for SOD3/EC-SOD was detected at approximately 30 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.|
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 Dismutases 3, SOD3, also known as extracellular (EC) SOD, is tetrameric glycoprotein with an apparent subunit molecular weight of about 30 kDa. Like SOD1, SOD3 binds one Cu2+ and Zn2+ ions per subunit but differs in sequence and tissue distribution. 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. Mouse SOD3 shares ~66% and 82% sequence homology with human and rat SOD3, respectively. SOD3 is a secretory protein and is synthesized with a putative 24-amino acid signal peptide preceding the 227 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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