Superoxide Dismutase, Cu,Zn, Recombinant, Human (SOD Cu,Zn)

An oxidoreductase that catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide.\n\nRecombinant Human Cu/Zn Superoxide Dismutase is a homodimer, non-glycosylated polypeptide chain containing 2 x 154 amino acids and having a total molecular mass of 31,608D\n\nAA Sequence:\nThe sequence of the first five N-terminal amino acids was determined and was found to be Ala-Thr-Lys-Ala-Val.\n\nBiological Activity:\nThe potency per mg was tested by Pyrogallic Acid method and was found to be more than 10,000Units/mg.\n\nStorage and Stability: \nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile ddH2O to (same/more than)0.1mg/ml. Add a carrier protein (0.1% HSA or BSA) for long term storage. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

S8060-13

Size

100ug

Form

Supplied as a lyophilized powder from PBS, pH 7.4.\nReconstitute in sterile ddH2O to (same/more than)0.1mg/ml. Add 0.1% HSA or BSA for long term storage. This solution can then be diluted into other aqueous solutions.

Purity

(same/more than) 95% by RP-HPLC and SDS-PAGE. Chromatographically purified.

References

1. Superoxide dismutase versus ferricytochrome C: determining rate constants for the spin trapping of superoxide by cyclic nitrones. Weaver J, Tsai P, Rosen GM, J Org Chem 2004 Nov 26;69(24):8423-8 2. Physical and chemical stability of different formulations with superoxide dismutase. Di Mambro VM, Campos PM, Pharmazie 2004 Oct;59(10):786-90 3. Enhancement of collagen-induced arthritis in mice genetically deficient in extracellular superoxide dismutase. Ross AD, Banda NK, Arend WP, Arthritis Rheum 2004 Nov;50(11):3702-11 4. The effects of superoxide dismutase in gerbils with bacterial meningitis. Ge NN, Brodie SA, Brodie HA, Otolaryngol Head Neck Surg 2004 Nov;131(5):563-72 5. Folding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomers. Lindberg MJ, Normark J, Oliveberg M, Proc Natl Acad Sci U S A 2004 Nov 9;101(45):15893-8 6. The structure of rabbit extracellular superoxide dismutase differs from the human protein. Petersen SV, Due AV, Oury TD, Biochemistry 2004 Nov 9;43(44):14275-81.