Superoxide Dismutase 2, Recombinant, Human (SOD2, Superoxide Dismutase [Mn], Mitochondrial)

Superoxide dismutase comprises a family of metalloenzymes that catalyze the oxido-reduction of superoxide anion to H2O2. Manganese superoxide dismutase (SOD2) is encoded by nuclear chromatin, synthesized in the cytosol, and imported posttranslationally into the mitochondrial matrix. It has been shown that SOD2 activity in tumor cells is lower than that in their normal counterparts. results suggest that the reduced level of SOD2 activity observed in human tumor cells is not due to a defect in the primary structure of the SOD2 protein, a change in the dosage of the SOD2 gene, or a decrease in the stability of SOD2 mRNA in tumor cells but rather is due to a defect or defects in the expression of the gene. SOD2 is one of the major cellular defense enzymes that protects against toxic effects of superoxide radicals. Overexpression of human SOD2 has been shown to inhibit radiation-induced neoplastic transformation, suppress malignancy of cancer cells, and increase tolerance to various toxic agents.\n\nSource:\nRecombinant protein corresponding to aa25-222, from human Superoxide Dismutase 2, expressed in E. coli. (P04179)\n\nStorage and Stability:\nLyophilized powder may be stored at -70 degrees C. Stable for 12 months at -70 degrees C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -70 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.

Prices direct from United States Biological

Quick response times

Exclusive Biosave savings/discounts

SPECIFICATIONS

Catalog Number

S8060-10K8

Size

500ug

Form

Supplied as a lyophilized powder from 20mM HEPES, pH 7.5.

Purity

~95% (SDS-PAGE)

References

1. Kuninaka, S. et al. (2000) Br. J. Cancer. 83, 928-934. 2. Strange, R. W. et al. (2003) J. Mol. Biol. 328, 877-891. 3. Weisiger, R. A., and Fridovich, I. (1973) J. Biol. Chem. 248, 3582-3592. 4. Enghild, J. J. et al. (1999) Biochem J. 317, 51-57.