SOD2 Protein & Antibody

Superoxide Dismutase 2

SOD2 Products

SOD2 Protein, Recombinant

Molecule	Species	Description //For Detailed Info. and Price------CLICK!	Cat. No
SOD2	Human	SOD2 Protein, Recombinant, Native	12656-HNAE

SOD2 Antibody

Molecule	Application	Description //For Detailed Info. and Price------CLICK!	Cat. No
Human SOD2	WB, ELISA	SOD2 Antibody (Antigen Affinity Purified)	12656-RP02
Human SOD2	ELISA	SOD2 Antibody	12656-R001

SOD2 cDNA Clone

Molecule	Species	Description //For Detailed Info. and Price------CLICK!	Cat. No
SOD2	Human	Homo sapiens SOD2 cDNA Clone	HG12061-G

SOD2 Related Areas

Cancer>>Apoptosis>>Oxidative Stress>>SOD2

Enzyme>>Oxidoreductase>>SOD2

SOD2 Alternative Names

SOD2, RP1-56L9.2, IPOB, MNSOD, MVCD6 [Homo sapiens]

Sod2, MGC6144, MnSOD, Sod-2 [Mus musculus]

SOD2 Background

Superoxide dismutases (SOD) are important anti-oxidant enzymes that guard against superoxide toxicity. In humans, as in all mammals and most chordates, three forms of superoxide dismutase (SOD) are present: SOD1 is located in the cytoplasm, SOD2 in the mitochondria, and SOD3 is extracellular. Mitochondrial superoxide dismutase [SOD; manganese SOD (MnSOD) or SOD2] neutralizes highly reactive superoxide radical (O(*-)(2)), the first member in the plethora of mitochondrial reactive oxygen species. A polymorphism in the target sequence of MnSOD/SOD2 enzyme, Val(16)Ala, is known to disrupt proper targeting of the enzyme from cytosol to mitochondrial matrix where it acts on O(*-)(2) to dismutate it to hydrogen peroxide (H(2)O(2)). SOD2 can also bind iron in vivo, but is inactive with iron. Such metal ion mis-incorporation with SOD2 can become prevalent upon disruption of mitochondrial metal homeostasis. It is believed that oxidative stress plays an essential role in the development of breast cancer, while SOD2 is one of the primary enzymes that directly convert potential harmful oxidizing species to harmless metabolites. SOD2 Val16Ala polymorphism is not associated with breast cancer susceptibility.

SOD2 Related Studies

1. Culotta VC, et al. (2006) Activation of superoxide dismutases: putting the metal to the pedal. Biochim Biophys Acta. 1763(7): 747-58.
2. Bag A, et al. (2008) Target sequence polymorphism of human manganese superoxide dismutase gene and its association with cancer risk: a review. Cancer Epidemiol Biomarkers Prev. 17(12): 3298-305.
3. Diehl C, et al. (2009) The basis of topical superoxide dismutase antipruritic activity. Acta Dermatovenerol Croat. 17(1): 25-39.
4. Ma X, et al. (2010) No association between SOD2 Val16Ala polymorphism and breast cancer susceptibility: a meta-analysis based on 9,710 cases and 11,041 controls. Breast Cancer Res Treat. 122(2): 509-14.