ORDERING INFORMATION
Catalog nos.13001P-5 5ug13001P-25 25ug13001P-1000 1000ugFormulation: Sterile-filtered solution in 20mM Tris-HCl, pH 7.5 and 10% glycerol. Purified by proprietary chromatographic techniques.BACKGROUND
Cu/Zn Superoxide Dismutase (SOD1) catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. It protects a cell from dangerous levels of superoxide. SOD1 binds copper and zinc ions and is one of three isozymes responsible for destroying free superoxide radicals. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis (ALS).
DESCRIPTION
Recombinant Human Cu/Zn SOD1 produced in E. coli is a single monomeric non-glycosylated polypeptide chain containing 154 amino acids with a molecular weight of 15.9kDa.
SPECIFICATION SUMMARY
Source: Escherichia coliPurity: Greater than 95% as determined by SDS- PAGE and RP-HPLC.Accession number: P00441.2Amino acid sequence:MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN AGSRLACGVIGIAQ
BIOLOGICAL ACTIVITY
Specific activity is >90 units/mg in which one unit will inhibit the rate of reduction of cytochrome c by 50% in a coupled system using xanthine and xanthine oxidase at pH 7.8 at 25oC in a 1.5ml reaction volume.
STORAGE AND STABILITY
Store at 4oC if entire vial will be used within 2-4 weeks. Store at -20oC for longer periods of time. Addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid multiple freeze-thaw cycles.
For in vitro investigational use only. Not intended for use in therapeutic or diagnostic procedures.
