*Optimal dilutions/concentrations should be determined by the researcher.
Not tested in other applications.
Shown to be specific by Western blotting and by gel diffusion techniques. Superoxide dismutases (SOD) arefound in all aerobic organisms, their physiological function appears to be to protect cells from free radicalsby scavenging superoxide anions. They catalyze the dismutation of superoxide anions to oxygen andhydrogen peroxide. SOD (Cu/Zn) is a cytosolic enzyme. SOD (Cu/Zn) is a dimer of two identical subunitsMW 16,000.
Glycine Buffered Saline pH 7.4, 0.099% sodium azide, 0.1% EACA, 0.01% Benzamidine, 1 mM EDTA
Store as concentrated solution. Centrifuge briefly prior to opening vial. Store at 4ºC.
33.50mg/ml(Please refer to the vial label for the specific concentration.)
Human SOD Cu/Zn purified from human erythrocytes.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
ALS1 Antibody , HSOD1 Antibody , SOD Antibody , IPOA Antibody , HOMODIMER Antibody , ALS Antibody
SOD (Cu/Zn) is a cytosolic enzyme.
The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene. [provided by RefSeq, Jul 2008]