Superoxide Dismutase Cu,Zn, Bovine Active Protein | Sod active protein
Superoxide Dismutase Cu,Zn, Bovine (SOD)
Gene Names
Sod; CG11793; cSod; cSOD; Cu; Cu-Zn SOD; Cu/Zn sod; Cu/Zn SOD; Cu/Zn superoxide dismutase; Cu/ZnSOD; CuSOD; CuZn SOD; CuZn-SOD; CuZn-SOD1; CuZnSOD; Cu[2+]/Zn[2+]SOD; DmelCG11793; dSOD1; G; l(3)108; l(3)68Af'; l(3)G; Mn SOD; sod; SOD; Sod-1; SOD-1; sod1; Sod1;
Purity
Molecular Biology Grade
Synonyms
Superoxide Dismutase Cu; Zn; Bovine; Bovine (SOD); Sod active protein
Purity/Purification
Molecular Biology Grade
Activity
2500 units per mg dry weight
Isoelectric Point
4.95
Quality Control
SDS-PAGE
Solubility
Readily soluble in 0.05M potassium phosphate, 0.1M EDTA, pH 7.8, at 5mg/ml.
Extinction Coefficient (A259/A680): ~30. The protein does not show an absorption maximum at 280nm.
Extinction Coefficient (A259/A680): ~30. The protein does not show an absorption maximum at 280nm.
Unit Definition
1 unit causes a 50% inhibition in the rate of reduction of cytochrome C.
Preparation and Storage
-20 degree C
Stability: SOD is an unusually stable enzyme and retains its activity for up to a year at 5 degree C. The apoenzyme is very unstable.
Stability: SOD is an unusually stable enzyme and retains its activity for up to a year at 5 degree C. The apoenzyme is very unstable.
Related Product Information for Sod active protein
Superoxide dismutase (SOD) catalyzes the destruction of the O2- free radical, protecting oxygen-metabolizing cells against harmful effects of superoxide free-radicals.
SOD protects hyaluronate against depolymerization by free-radicals and indicated that exogenous SOD might have an anti-inflammatory effect. The O2-ion, which has been considered important in aging, lipid peroxidation and the peroxidative hemolysis of red blood cells, is formed by the univalent reduction of O2 during various enzymatic reactions or by ionizing radiation. There is also superoxide radical formation during leukocyte phagocytosis. SOD deficiency might lead to Heinz body hemolytic anemia.
SOD protects hyaluronate against depolymerization by free-radicals and indicated that exogenous SOD might have an anti-inflammatory effect. The O2-ion, which has been considered important in aging, lipid peroxidation and the peroxidative hemolysis of red blood cells, is formed by the univalent reduction of O2 during various enzymatic reactions or by ionizing radiation. There is also superoxide radical formation during leukocyte phagocytosis. SOD deficiency might lead to Heinz body hemolytic anemia.
Product Categories/Family for Sod active protein
NCBI and Uniprot Product Information
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
Molecular Weight
32.5kD
NCBI Official Full Name
superoxide dismutase, isoform D
NCBI Official Synonym Full Names
Superoxide dismutase
NCBI Official Symbol
Sod
NCBI Official Synonym Symbols
CG11793; cSod; cSOD; Cu; Cu-Zn SOD; Cu/Zn sod; Cu/Zn SOD; Cu/Zn superoxide dismutase; Cu/ZnSOD; CuSOD; CuZn SOD; CuZn-SOD; CuZn-SOD1; CuZnSOD; Cu[2+]/Zn[2+]SOD; DmelCG11793; dSOD1; G; l(3)108; l(3)68Af'; l(3)G; Mn SOD; sod; SOD; Sod-1; SOD-1; sod1; Sod1;
NCBI Protein Information
CG11793 gene product from transcript CG11793-RA; CG11793-PA; CG11793-PD; Cu, Zn superoxide dismutase; Cu-Zn superoxide dismutase; Cu/Zn superoxide dismutase; Cu/Zn-Superoxide dismutase; CuZn superoxide dismutase; CuZn-superoxide dismutase; CuZn-superoxide dismutase (SOD)1; CuZnSOD; Cu[2+] Zn[2+] superoxide dismutase; Cu[2+]Zn[2+] superoxide dismutase; Mn superoxide dismutase; Sod-PA; Sod-PD; complementation group G; copper and zinc SOD; copper-zinc superoxide; copper-zinc superoxide dismutase; cytoplasmic Cu/ZnSOD; super oxide dismutase; superoxidase dismutase; superoxide dismutase 1; superoxide dismutatase; superoxide-dismutase; superoxido dismutase; tetrazolium oxidase; tetrazolium oxidase-1
UniProt Protein Name
Superoxide dismutase [Cu-Zn]
Protein Family
UniProt Gene Name
Sod
UniProt Entry Name
SODC_DROME
Uniprot Description
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic activity: 2 superoxide + 2 H+ = O2 + H2O2.
Cofactor: Binds 1 copper ion per subunit.Binds 1 zinc ion per subunit.
Subunit structure: Homodimer.
Subcellular location: Cytoplasm.
Sequence similarities: Belongs to the Cu-Zn superoxide dismutase family.
Research Articles on Sod
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Product Notes
The Sod sod (Catalog #AAA635155) is an Active Protein and is intended for research purposes only. The product is available for immediate purchase. It is sometimes possible for the material contained within the vial of "Superoxide Dismutase Cu,Zn, Bovine, Active Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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