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S9697 Sigma-Aldrich

Superoxide Dismutase bovine

recombinant, expressed in E. coli, lyophilized powder, ≥2500 units/mg protein, ≥90% (SDS-PAGE)

Synonym: CU/ZN-SOD, SOD1, SOD, Superoxide Dismutase 1 bovine, Superoxide: superoxide oxidoreductase

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Properties

Related Categories 1.15.x.x Acting on superoxide radicals, 1.x.x.x Oxidoreductases, Analytical and Industrial Enzymes, Application Index, Biochemicals and Reagents,
Quality Level   200
recombinant   expressed in E. coli
assay   ≥90% (SDS-PAGE)
form   lyophilized powder
specific activity   ≥2500 units/mg protein
optimum pH   7.8 (25 °C)
pH-range   7.6 - 10.5
pI    4.95
sequence note   MATKAVCVLKGDGPVQGTIHFEAKGDTVVVTGSITGLTEGDHGFHVHQFGDNTQGCTSAGPHFNPLSKKHGGPKDEERHVGDLGNVTADKNGVAIVDIVDPLISLSGEYSIIGRTMVVHEKPDDLGRGGNEESTKTGNAGSRLACGVIGIAK
NCBI accession no.   NM_174615
  NP_777040
storage temp.   −20°C

Description

General description

SOD from bovine erythrocytes was the first SOD to be found in mammalian tissues. Before its enzymatic activity was discovered the protein was known as haemocuprein or erythrocuprein. 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, one Cu+2 atoms and one Zn+2 atoms. There are three forms of SOD differentiated by the metal ions in the active site. These are Cu+2/Zn+2, Mn+2, and Fe+2 SOD. In vertebrate organisms Cu/Zn-SOD is found in the cytoplasm and the mitochondrial intermembrane space, while Mn-SOD is found in the mitochondrial matrix space. Fe-SOD is found in prokaryotes and some higher plants.

Application

Superoxide dismutase has been used in a study to investigate where lipoproteins may affect the L-arginine-nitric oxide pathway. Superoxide dismutase has also been used in a study to investigate the mass spectral evidence for carbonate-anion-radical-induced posttranslational modification of tryptophan to kynurenine in human Cu, Zn superoxide dismutase.

The product has been used to develop an SOD assay. This assay used dismutase-mediated inhibition of NADH-dependent nitroblue tetrazolium reduction.

Packaging

15000 units in glass bottle

30000, 75000, 300000 units in poly bottle

Biochem/physiol Actions

Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD 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 by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis.

Unit Definition

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.

Preparation Note

Produced using animal component-free materials.

Reconstitution

Reconstitute in 10 mM potassium phosphate, pH 7.4.

Analysis Note

Extinction coefficient: EmM= 10.3 (258 nM)
SOD has no significant absorbance peak at 280 nM because of the absence of tryptophan.

Other Notes

Inhibitors: cyanide, OH- (competitive), hydrogen peroxide

Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
WGK 3
Flash Point(F) 
Not applicable
Flash Point(C) 
Not applicable

Documents

Certificate of Analysis (COA)

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Certificate of Origin (COO)

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Protocols & Articles

Articles

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Mitochondrial Stress and ROS

Oxidative stress is implicated in the pathogenesis of lipotoxicity in both animal and human studies. Chronic oxidative stress is linked to insulin resistance in multiple tissues. Oxidative stress is ...
BioFiles 2011, 6.4, 22.
Keywords: Anti-inflammatory agents, Apoptosis, Cancer, Cell signaling, Cellular processes, Gene expression, Indicators, Metabolism, Oxidations, Respiratory

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Peer-Reviewed Papers
15

References

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