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Superoxide Dismutase from human erythrocytes

SIGMA/S9636 - essentially salt-free, lyophilized powder, ≥2,500 units/mg protein

Synonym: 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-S9636-1KU 1000 units
$225.00
1/EA
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45-S9636-3KU 3000 units
$658.00
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45-S9636-15KU 15000 units
$2250.00
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45-S9636-30KU 30000 units
$3720.00
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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.

 

application(s) life science and biopharma
assay >80% protein (biuret)
biological source human erythrocytes
color white to off-white
composition Protein, ≥80% biuret
form essentially salt-free, lyophilized powder
manufacturer/tradename Sigma-Aldrich
mol wt 32.0 kDa
pH 7.8
pH range 7.6—10.5
Quality Level 400 
specific activity ≥2,500 units/mg protein
storage temp. −20°C
suitability suitable for molecular biology
technique(s) activity assay: suitable
UniProt accession no. P00441 
  P04179 
  P08294 
Analysis Note: For assay method, see McCord, J.M. and Fridovich, I., J. Biol. Chem., 244, 6049 (1969).
Application: Superoxide Dismutase from human erythrocytes has been used:

• to test its effect on human neutrophils in reactive oxygen species (ROS) measurement studies involving Pseudomonas aeruginosa infection
• as an antioxidant to test its effect on ROS generation induced by atmospheric-pressure plasma jet (APPJ) in red blood cell (RBC) homogenates using optical spectroscopy studies
• to test its attenuating effect on hemoglobin (Hb)-induced nuclear factor-kappa B (NF- κB) and hypoxia-inducible factor (HIF) activity in human dermal microvascular endothelial cells (HMECs-1)
• as a reference antioxidant protein to examine its expression in human intestinal Caco-2 cells following treatment with dietary flavonoids
•  in combination with catalase to promote cell differentiation in vitro
Biochem/physiol Actions: Catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. 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.
Biochem/physiol Actions: Mutations in the SOD1 gene are implicated in Amyotrophic lateral sclerosis (ALS).
General description: Superoxide dismutases (SOD) are a group of low molecular weight metalloproteins present in all aerobic cells of plants, animals and micro-organisms. Three forms of SOD exist, based on the metal ions in the active site. These are Cu2+/Zn2+, Mn2+ and Fe2+ containing SOD. In vertebrate organisms, Cu/Zn-SOD is located in the cytoplasm as well as the mitochondrial intermembrane space, whereas Mn-SOD is located at the mitochondrial matrix space in prokaryotes. Fe-SOD is also found in prokaryotes and higher plants. Human erythrocyte SOD is a non-covalently bound homodimeric protein with two 16.3 kDa subunits containing 153 amino acids. Each dimer consists of two Cu2+ atoms and two Zn2+ atoms.
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.
RIDADR NONH for all modes of transport
WGK Germany WGK 3
Flash Point(F) Not applicable
Flash Point(C) Not applicable
Purity >80% protein (biuret)
activity specific activity: ≥2,500 units/mg protein
Storage Temp. −20°C
Enzyme Commission (EC) Number 1.15.1.1   ( BRENDA  | IUBMB  )
UNSPSC 12352204

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