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S9697

Sigma-Aldrich

Superoxide Dismutase bovine

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

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Synonym(s):
Superoxide Dismutase 1 bovine, cytocuprein, erythrocuprein, hemocuprein, CU/ZN-SOD, SOD, SOD1, Superoxide: superoxide oxidoreductase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

biological source

bovine

Quality Level

recombinant

expressed in E. coli

assay

≥90% (SDS-PAGE)

form

lyophilized powder

specific activity

≥2500 units/mg protein

storage condition

(Tightly closed)

technique(s)

inhibition assay: suitable

color

white

optimum pH

7.8 (25 °C)

pH range

7.6-10.5

pI 

4.95

sequence note

MATKAVCVLKGDGPVQGTIHFEAKGDTVVVTGSITGLTEGDHGFHVHQFGDNTQGCTSAGPHFNPLSKKHGGPKDEERHVGDLGNVTADKNGVAIVDIVDPLISLSGEYSIIGRTMVVHEKPDDLGRGGNEESTKTGNAGSRLACGVIGIAK

NCBI accession no.

UniProt accession no.

storage temp.

−20°C

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S9697

Superoxide Dismutase bovine

biological source

bovine

biological source

bovine

biological source

-

biological source

-

specific activity

≥2500 units/mg protein

specific activity

≥3,000 units/mg protein

specific activity

2,000-6,000 units/mg protein (biuret)

specific activity

≥2,500 units/mg protein

assay

≥90% (SDS-PAGE)

assay

-

assay

-

assay

-

form

lyophilized powder

form

lyophilized powder

form

ammonium sulfate suspension

form

essentially salt-free, lyophilized powder

recombinant

expressed in E. coli

recombinant

-

recombinant

-

recombinant

-

General description

Research area: Cell Signaling

SOD from bovine erythrocytes was the first SOD to be found in mammalian tissues. 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 vertebrates, Cu/Zn-SOD is found in the cytoplasm, chloroplast, and may be in extracellular space, while Mn-SOD is found in the mitochondrial matrix space and peroxisome. Fe-SOD is found in the chloroplast of prokaryotes and some higher plants.

Application

Superoxide Dismutase bovine has been used:

  • to construct a calibration curve for the evaluation of superoxide dismutase (SOD) enzyme activities
  • in a study to investigate where lipoproteins may affect the L-arginine-nitric oxide pathway
  • 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

Biochem/physiol Actions

Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. This reaction in turn activates redox-sensitive kinases and inactivates specific phosphatases to regulate redox-sensitive signaling pathway, including hypertrophy, proliferation, and migration. SOD serves as a potent antioxidant and protects the cells against the toxic effects of oxygen radicals. SOD may also suppress apoptosis by competing with nitric oxide (NO) for superoxide anion, which reacts with NO to form peroxynitrite, 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

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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L Vergnani et al.
Circulation, 101(11), 1261-1266 (2000-03-22)
Native and oxidized LDLs (n-LDL and ox-LDL) are involved in the atherogenic process and affect endothelium-dependent vascular tone through their interaction with nitric oxide (NO). In this study we evaluated directly, by using a porphyrinic microsensor, the effect of increasing
Tohru Fukai et al.
Cardiovascular research, 55(2), 239-249 (2002-07-19)
Excessive production and/or inadequate removal of reactive oxygen species, especially superoxide anion (O(2)(*-)), have been implicated in the pathogenesis of many cardiovascular diseases, including atherosclerosis, hypertension, diabetes, and in endothelial dysfunction by decreasing nitric oxide (NO) bioactivity. Since the vascular
Olga Manzhulo et al.
Acta histochemica, 120(8), 741-747 (2018-09-02)
Docosahexaenoic acid (DHA, 22:6 (n-3)) leads to recovery of locomotor functions observed of spinal cord injury (SCI) in rats. In present study, we characterized the expression of iba-1, CD86, CD163 in microglia/macrophages, to assess activation state and M1 (pro-inflammatory)/M2 (anti-inflammatory)
Tohru Fukai et al.
Antioxidants & redox signaling, 15(6), 1583-1606 (2011-04-09)
Excessive reactive oxygen species Revised abstract, especially superoxide anion (O₂•-), play important roles in the pathogenesis of many cardiovascular diseases, including hypertension and atherosclerosis. Superoxide dismutases (SODs) are the major antioxidant defense systems against (O₂•-), which consist of three isoforms
Lingyan Wang et al.
Oxidative medicine and cellular longevity, 2015, 217670-217670 (2015-08-22)
A major source of reactive oxygen species (ROS) generation is the mitochondria. By using flow cytometry of the mitochondrial fluorescent probe, MitoSOX Red, western blot of mitochondrial ROS scavenger Peroxiredoxin (Prx) 3 and fluorescence immunostaining, ELISA of cleaved caspases 3

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Oxidative stress is mediated, in part, by reactive oxygen species produced by multiple cellular processes and controlled by cellular antioxidant mechanisms such as enzymatic scavengers or antioxidant modulators. Free radicals, such as reactive oxygen species, cause cellular damage via cellular.

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