Catalogue number
PRO-648
Synonyms
Superoxide dismutase [Cu-Zn], EC 1.15.1.1, SOD1, SOD, ALS, ALS1, IPOA.
Introduction
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.
Description
Recombinant Human Cu/Zn Superoxide Dismutase produced in E.Coli is a single monomeric non-glycosylated polypeptide chain containing 154 amino acids and having a total molecular mass of 15.9 kDa.
The SOD1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered colorless solution.
Formulation
SOD1 filtered solution (1mg/ml) contains 20mM Tris-HCl pH-7.5 and 10% glycerol.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Amino acid sequence
MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN AGSRLACGVIGIAQ.
Biological Activity
Specific activity is > 500 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 25°C.
Safety Data Sheet
Usage
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
