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EC-SOD is the extracellular member of the superoxide dismutase family, encoded by SOD3. It is a secreted copper- and zinc-containing glycoprotein that removes superoxide in the extracellular space and binds to matrix components through a basic C-terminal region.
How does it differ from other superoxide dismutases?
The other family members act inside the cell, in the cytosol or mitochondria. EC-SOD is secreted, forms a tetramer, and carries a heparin-binding tail that anchors it to heparan sulfate proteoglycans and collagen in tissues.
What are the EC-SOD peptides used for?
They are defined segments of the mouse sequence, usually carrying an added cysteine for conjugation. Their main uses are immunogen preparation, antibody validation with blocking peptides, and epitope mapping rather than functional enzymatic work.
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