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商品編號(hào)


YIF-LF-P0020



品牌


Adipogen



公司


Adipogen



公司分類


Proteins



Size

0.5 mg

商品信息


More Information



Product Details



Synonyms

CCS; Superoxide Dismutase Copper Chaperone; Copper Chaperone for Superoxide Dismutase



Product Type

Protein



Properties



Source/Host

E. coli



Crossreactivity

Human



Purity

≥95% (SDS-PAGE)



Formulation

Lyophilized from 20mM HEPES, pH 7.4.



Other Product Data

Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.



Declaration

Manufactured by AbFrontier



Shipping and Handling



Shipping

BLUE ICE



Short Term Storage

+4°C



Long Term Storage

-20°C



Handling Advice

Avoid freeze/thaw cycles.



Use/St
ABI
lity

After reconstitution, store at -80°C.



Documents



MSD
S

No



Product Specification Sheet



Datasheet


Download PDF





Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide r
ADI
cal anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu,Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.


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