SOD2 Antikörper (Antigen Affinität reinigt)

Verwandte Bereiche:

Proteine:

Antikörper:

Superoxide dismutases (SOD) are an ubiquitous family of enzymes that function to efficiently catalyze the dismutation of superoxide anions. Three unique and highly compartmentalized mammalian superoxide dismutases have been biochemically and molecularly characterized to date. SOD2, or Mn-SOD, exists as a tetramer and is initially synthesized containing a leader peptide, which targets this manganese-containing enzyme exclusively to the mitochondrial spaces. SOD2 is a member of the iron/manganese superoxide dismutase family. The SOD2 protein transforms toxic superoxide, a byproduct of the mitochondrial electron transport chain, into hydrogen peroxide and diatomic oxygen. In the case of mitochondrial MnSOD of eukaryotes (SOD2), metal insertion cannot occur post-translationally, but requires new synthesis and mitochondrial import of the SOD2 polypeptide. 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.

1. Zelko IN. et al., 2002, Free Radic Biol Med. 33 (3): 337-49.
2. Culotta VC. et al., 2006, Biochim Biophys Acta. 1763 (7): 747-58.
3. Ma X. et al., 2010, Breast Cancer Res Treat. 122 (2): 509-14.