Active Recombinant Human Superoxide Dismutase 1, Soluble, His-tagged

Cat.No. : SOD1-326H
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Species : Human
Source : E.coli
Tag : His
Description : Cu/Zn Superoxide Dismutase (Cu/Zn SOD) catalyzes the dismutation of superoxide radicals to molecular oxygen. It has been implicated in cellular aging due to its reduced activity in aging cells. Cu/Zn SOD plays a protective role in the pathogenesis of selective neuronal injury after brief ischemia and reduces the degree of necrotic and DNA fragmented neuronal death following global ischemia. Mutant forms of Cu/Zn SOD have been linked to neurodegenerative diseases such as amyotrophic lateral sclerosis.
Usage : For in vitro use only.
Form : Liquid. Supplied in 50 mM sodium citrate buffer pH 5.5, 1 mM DTT, 200 μM ZnSO4, and 200 μM CuSO4.
Activity : > 2.000 units/mg (One unit is defined as the amount of enzyme that will double the rate of autoxidation of 5, 6, 6a, 11b-tetrahydro- 3, 9,10-trihydroxybenzo-[c]- fluorene per minute at 37°C, pH 8.8).
Purity : > 90% by SDS-PAGE.
Storage : Quality guaranteed for 12 months, Store at -80°C. Avoid freeze / thaw cycles.
Gene Name SOD1 superoxide dismutase 1, soluble [ Homo sapiens ]
Synonyms SOD1; superoxide dismutase 1, soluble; ALS; SOD; ALS1; IPOA; homodimer; SOD, soluble; indophenoloxidase A; Cu/Zn superoxide dismutase; superoxide dismutase, cystolic; EC 1.15.1.1; Superoxide dismutase [Cu-Zn]
Gene ID 6647
mRNA Refseq NM_000454
Protein Refseq NP_000445
MIM 147450
UniProt ID P00441
Chromosome Location 21q22.11
Pathway Amyotrophic lateral sclerosis (ALS); Huntington"s disease; Prion diseases; Hemostasis
Function antioxidant activity; chaperone binding; copper ion binding; metal ion binding; protein homodimerization activity; protein phosphatase 2B binding; superoxide dismutase activity; zinc ion binding

Not For Human Consumption!

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