Search Thermo Fisher Scientific
Disclaimer
Clicking the images or links will redirect you to a website hosted by BenchSci that provides third-party scientific content. Neither the content nor the BenchSci technology and processes for selection have been evaluated by us; we are providing them as-is and without warranty of any kind, including for use or application of the Thermo Fisher Scientific products presented.
Product Details
RP-104784
Applications
Tested Dilution
Publications
Product Specifications
Species
Human
Expression System
E. coli
Amino acid sequence
GQLQNLGAAVAILGGPGTVQGVVRFLQLTPERCLIEGTIDGLEPGLHGLHVHQYGDLTNNCNSCGNHFNPDGASHGGPQDSDRHR
Tag
His-ABP-tag
Class
Recombinant
Type
Protein
Purity
>80% by SDS-PAGE and Coomassie blue staining
Conjugate
Unconjugated
Form
Liquid
Concentration
≥5.0 mg/mL
Purification
purified
Storage buffer
PBS/1M urea, pH 7.4
Contains
no preservative
Storage conditions
-20°C, Avoid Freeze/Thaw Cycles
Shipping conditions
Wet ice
Product Specific Information
Highest antigen sequence indentity to the following orthologs: Mouse (86%), Rat (86%).
This recombinant protein control fragment may be used for blocking experiments with the corresponding antibody, PA5-83703. In IHC/ICC and WB experiments, we recommend a 100x molar excess of the protein fragment control based on the concentration and the molecular weight. Pre-incubate the antibody-protein control fragment mixture for 30 min at room temperature.
Target Information
Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical 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). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. 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. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
References (0)
Have you cited this product in a publication?
Let us know so we can reference it here.
Bioinformatics
Protein Aliases: Copper chaperone for superoxide dismutase; Superoxide dismutase copper chaperone
Gene Aliases: CCS
UniProt ID: (Human) O14618
Entrez Gene ID: (Human) 9973
We're here to help
Get expert recommendations for common problems or connect directly with an on staff expert for technical assistance related to applications, equipment and general product use.
Contact tech support