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Superoxide Dismutase from bovine erythrocytes

SIGMA/S7571 - lyophilized powder, ≥3,000 units/mg protein, Protein ≥95 % by biuret

Synonym: CU/ZN-SOD; Superoxide Dismutase 1 bovine; cytocuprein; erythrocuprein; hemocuprein; SOD; Superoxide: superoxide oxidoreductase

CAS Number: 9054-89-1
EC Number: 232-943-0
MDL Number: MFCD00132404
Product Type: Chemical

Catalog Number PKG Qty. Price Quantity
45-S7571-15KU 15000 units
$109.00
1/EA
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45-S7571-30KU 30000 units
$148.00
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45-S7571-75KU 75000 units
$247.00
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45-S7571-300KU 300000 units
$734.00
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SOD from bovine erythrocytes is a homodimeric non-covalently bound protein with two 16.3 kDa subunits of 151 amino acids. Each monomer has one intrachain disulfide and one free sulfhydryl, two copper atoms and two zinc atoms.
Multiple enzymatic scavengers are utilized by the cell to limit damage from reactive oxygen species. These scavengers include members of the superoxide dismutase (SOD) family, catalase, and glutathione peroxidase.
SOD catalyzes the conversion of superoxide radicals into hydrogen peroxide and molecular oxygen.
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: S7571-300KU
12 Principles of Green Chemistry: Principle 2—Atom Economy.  This product was designed to maximize the incorporation of all raw materials used in the manufacturing process.
12 Principles of Green Chemistry: Principle 7—A raw material or feedstock should be renewable rather than depleting whenever technically and economically practicable.

 

application(s) diagnostic assay manufacturing
biological source bovine
color blue-green
composition Protein, ≥95% biuret
form lyophilized powder
greener alternative category  , Re-engineered 
greener alternative product characteristics Atom Economy
Design for Energy Efficiency
Use of Renewable Feedstocks
Learn more about the Principles of Green Chemistry .
mol wt 32.5 kDa
pI  4.95
Quality Level 300 
solubility aqueous buffer, pH 7.5: soluble
  water: 20 mg/mL
specific activity ≥3,000 units/mg protein
storage condition (Store under nitrogen.
Tightly closed. Dry.)
storage temp. −20°C
sustainability Greener Alternative Product
technique(s) immunoblotting: suitable
  inhibition assay: suitable
UniProt accession no. P00442 
  P41976 
Application: Superoxide dismutase from bovine erythrocytes has been used:

•  in a study to assess a kinetic model of radiation-induced inactivation of superoxide dismutase in nitrous oxide-saturated solutions
•  in a study to investigate the possible participation of superoxide anion in the intestinal tryptophan 2,3-dioxygenase reaction
• to investigate its effect on the hemolysis rate of human RBCs and hemoglobin-nitric oxide complex (HbNO) stability in human erythrocytes
• in combination with catalase to study its effect on cell differentiation in vitro
• to quantify superoxide levels and study their effect on reactivity in mouse pulmonary arteries through chemiluminescence and cytochrome C reduction methods
Biochem/physiol Actions: Superoxide Dismutase from bovine erythrocytes catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. It serves as an antioxidant and plays a critical role in the defense of cells against the toxic effects of oxygen radicals. Competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice.
General description: Research area: Cell Signaling

Superoxide dismutase (SOD) is a redox-active metalloenzyme expressed in both aerobic and anaerobic living organisms. Bovine superoxide dismutase or CuZn SOD is a homodimer with each subunit containing one zinc and one copper ion.
Other Notes: One unit will inhibit reduction of cytochrome c by 50% in a coupled system with xanthine oxidase at pH 7.8 at 25 °C in a 3.0 ml reaction volume. Xanthine oxidase concentration should produce an initial ΔA550 of 0.025 ± 0.005 per min.
Packaging: 15000 units in glass bottle
Packaging: 30000, 75000, 300000 units in poly bottle
Physical form: Lyophilized powder, essentially salt-free
RIDADR NONH for all modes of transport
WGK Germany WGK 3
Flash Point(F) Not applicable
Flash Point(C) Not applicable
activity specific activity: ≥3,000 units/mg protein
Storage Temp. −20°C
Enzyme Commission (EC) Number 1.15.1.1   ( BRENDA  | IUBMB  )
UNSPSC 12352204

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