Superoxide dismutase (SOD) is a 152aa enzyme previously known as haemocuprein or erythrocuprein and belongs to the Cu-Zn superoxide dismutase family. In mammals, it was first described in bovine erythrocytes and is a homodimeric non-covalently bound protein where each monomer has one intrachain disulphide and one free sulfhydryl, and two Cu+2 atoms and two Zn+2 atoms. SOD catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen and thus plays an important role in the defense of cells against the toxic effects of oxygen radicals. It competes with nitric oxide (NO) for superoxide anion, thus promoting the activity of NO. SOD may also play a critical role in suppressing apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrite.
Suitable for use in Western Blot and Immunohistochemistry. Other applications not tested.
Western Blot: 0.025-0.1ug/ml
Immunohistochemistry (formalin fixed paraffin embedded): 5ug/ml
Optimal dilutions to be determined by the researcher.
Human, mouse or rat liver lysate
Storage and Stability:
May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.