Recombinant Human Superoxide Dismutase
Source : Escherichia Coli. Recombinant Human Cu/Zn Superoxide Dismutase produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 154 amino acids and having a total molecular mass of 31,608 Dalton. The Cu/Zn SOD is purified by proprietary chromatographic techniques. Human Cu/Zn Superoxide Dismutase (SOD1) catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. SOD1 binds copper and zinc ions and is 1 of 3 isozymes accountable for destroying free superoxide radicals in the body. The encoded protein neutralizes supercharged oxygen molecules, which can damage cells if their levels are not controlled. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis.
Product Specifications
Product Name Alternative
Superoxide dismutase [Cu-Zn]||EC 1.15.1.1||SOD1||SOD||ALS||ALS1||IPOA.
Purification
Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Components
Lyophilized from a 0.2μm filtered concentrated (1mg/mL) solution in PBS, pH 7.4.
Storage Conditions
Applications Notes
Amino Acids
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Thr-Lys-Ala-Val.
Explore Other Products
Discover premium biology products from our extensive collection of 20M+ items