Recombinant Human Superoxide Dismutase [Cu-Zn]/SOD1 is produced by our E. coli expression system. The target protein is expressed with sequence (Ala2-Gln154) of Human SOD1 fused with a 6His tag at the N-terminus.
Pureté
> 95 % as determined by reducing SDS-PAGE.
Stérilité
0.2 μm filtered
niveau d'endotoxine
Less than 0.1 ng/μg (1 IEU/μg) as determined by LAL test
SOD1
Origine: Poulet
Hôte: Escherichia coli (E. coli)
Recombinant
> 95 %
WB, SDS, Imm, PC
Restrictions
For Research Use only
Format
Liquid
Reconstitution
It is not recommended to reconstitute to a concentration less than 100 μg/mL. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Buffer
Supplied as a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.2.
Conseil sur la manipulation
Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
Stock
-80 °C
Stockage commentaire
Store at < -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles.
Superoxide Dismutase [Cu-Zn] (SOD1) is a soluble cytoplasmic and mitochondrial intermembrane space protein that belongs to the Cu-Zn superoxide dismutase family. SOD1 binds copper and zinc ions and is one of three isozymes responsible for destroying free superoxide radicals in the body. SOD1 neutralizes supercharged oxygen molecules, which can damage cells if their levels are not controlled. The enzyme protects the cell against dangerous levels of superoxide. Zinc binding promotes dimerization and stabilizes the native form. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis. Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) which is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Alternative Names: Superoxide Dismutase [Cu-Zn], Superoxide Dismutase 1, hSod1, SOD1