» Sign in / Register

Cu/Zn SODHis

Cu/Zn Superoxide Dismutase

human, recombinant, E. coli

Product Cat. No. Amount Price (EUR) Buy / Note
Cu/Zn SODHis PR-150 500 μg 103,50 Add to Basket/Quote Add to Notepad

For in vitro use only!

Shipping: shipped on dry ice

Storage Conditions: store at -80 °C
avoid freeze/thaw cycles

Shelf Life: 12 months

Accession number: X02317

Accession number: X02317

Purity: > 90 % (SDS-PAGE)

Form: liquid (Supplied in 50 mM sodium citrate buffer pH 5.5, 1 mM DTT, 200 μM ZnSO4 and 200 μM CuSO4)

pH: 5.5

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).

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.

Selected References:
Stasser et al. (2005) Cysteine-to-Serine Mutants of the Human Copper Chaperone for Superoxide Dismutase Reveal a Copper Cluster at a Domain III Dimer Interface. Biochemistry 44:3143.
Greenlund et al. (1995) Superoxide dismutase delays neuronal apoptosis: a role for reactive oxygen species in programmed neuronal death. Neuron 14:303.
Gurney et al. (1994) Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science 264:1772.
Nebot et al. (1993) Spectrophotometric assay of superoxide dismutase activity based on the activated autoxidation of tetracyclic catechol. Anal. Biochem. 214:442.
Deng et al. (1993) Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase. Science 261:986.