Extracellular superoxide dismutase [Cu-Zn] is an enzyme that in humans is encoded by the SOD3 gene. This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. Acroding to the report, in a weakly alkaline buffer solution (pH 8.2) with N-tris (hydroxymethyl) amino methane-HCl, pyrogallol can occur autoxidation in the air, then SOD can inhibit this reaction. Thus, we use this way to measure the activity of recombinant human SOD3. The reaction was performed in adding 30μl pyrogallol (50mmol/L) to 900μl Tris-HCl (50mmol/L) in 1.5 ml cuvette (1.0 cm light path), rapidly mixing at 25ºC, then read at 325nm (zero the spectrophotometer using 50 mmol/L Tris-HCl) , reacod the OD value every 30 second for 6 times. Control the pyrogallol autoxidation rate at 0.70 OD/min. After, adding various concentrations of recombinant of SOD3 to 900μl Tris-HCl (50 mmol/L), incubated for 20min at 25ºC, then adding 30μl pyrogallol (50 mmol/L) to each tube, rapidly mixing and read at 325nm, record the OD value every 30 second for 6 times. Under these conditions, the enzyme amount of 50% per minute inhibition of pyrogallol autooxidation is defined as a unit.
Reconstitute with 20mM Tris and 150mM NaCl (pH8.0) to a concentration of 0.1-1.0mg/ml. Do not vortex. Lyophilized from 20mM Tris (pH8.0), 150mM NaCl, 1mM EDTA, 1mM DTT, 0.01% SKL, 5% Trehalose.
For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, store at -20ºC or below. After reconstitution, keep as concentrated solution. Avoid freeze-thaw cycles.
N-terminal His-Tag; Trp19~Ala240 (NP_003093.2)
< 1 EU/μg
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
superoxide dismutase 3 , EC-SOD
This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the conversion of superoxide radicals into hydrogen peroxide and oxygen, which may protect the brain, lungs, and other tissues from oxidative stress. Proteolytic processing of the encoded protein results in the formation of two distinct homotetramers that differ in their ability to interact with the extracellular matrix (ECM). Homotetramers consisting of the intact protein, or type C subunit, exhibit high affinity for heparin and are anchored to the ECM. Homotetramers consisting of a proteolytically cleaved form of the protein, or type A subunit, exhibit low affinity for heparin and do not interact with the ECM. A mutation in this gene may be associated with increased heart disease risk. [provided by RefSeq, Oct 2015]