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10ug50ug500ug1mg
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Recombinant Human Superoxide Dismutase [Cu-Zn]/SOD1
Our PriceQuantity

10ug/$150

50ug/$440

500ug/$1540

1mg/$2200

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Catalog#CE19
SourceE. coli
DescriptionRecombinant 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.
NamesSuperoxide Dismutase [Cu-Zn], Superoxide Dismutase 1, hSod1, SOD1
Accession #P00441
FormulationSupplied as a 0.2 μM filtered solution of 20mM PB, 150mM NaCl, pH 7.2
ShippingThe product is shipped on dry ice/ice packs.
StorageStore at < -20°C, stable for 6 months after receipt.
Please minimize freeze-thaw cycles.
PurityGreater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.
EndotoxinLess than 0.1 ng/μg (1 IEU/μg).
Amino Acid Sequence
MGSSHHHHHHSSGLVPRGSHMATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHG FHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGD HCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
BackgroundSuperoxide 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.