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S7571

Sigma-Aldrich

Superoxide Dismutase from bovine erythrocytes

greener alternative

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

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

biological source

bovine

Quality Level

form

lyophilized powder

specific activity

≥3,000 units/mg protein

mol wt

32.5 kDa

composition

Protein, ≥95% biuret

storage condition

(Store under nitrogen.
Tightly closed. Dry.)

greener alternative product characteristics

Atom Economy
Design for Energy Efficiency
Use of Renewable Feedstocks
Learn more about the Principles of Green Chemistry.

technique(s)

immunoblotting: suitable
inhibition assay: suitable

color

blue-green

pI 

4.95

solubility

water: 20 mg/mL
aqueous buffer, pH 7.5: soluble

UniProt accession no.

application(s)

diagnostic assay manufacturing

greener alternative category

storage temp.

−20°C

Gene Information

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This Item
S5395S7446S9636
biological source

bovine

biological source

bovine erythrocytes

biological source

-

biological source

-

technique(s)

immunoblotting: suitable, inhibition assay: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

-

technique(s)

activity assay: suitable

Gene Information

cow ... SOD1(281495), SOD2(281496)

Gene Information

-

Gene Information

-

Gene Information

human ... SOD1(6647), SOD2(6648), SOD3(6649)

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

essentially salt-free, lyophilized powder

application(s)

diagnostic assay manufacturing

application(s)

-

application(s)

-

application(s)

-

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.

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.

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.

Physical form

Lyophilized powder, essentially salt-free

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Copper zinc superoxide dismutase (CuZnSOD) forms a crucial component of the cellular response to oxidative stress by catalyzing the dismutation of the superoxide radical to hydrogen peroxide and water. Mutations in human CuZnSOD are associated with the development of familial
Possible participation of superoxide anion in the intestinal tryptophan 2,3-dioxygenase reaction.
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The Journal of biological chemistry, 246(24), 7825-7826 (1971-12-25)

Articles

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.

Protocols

Enzymatic Assay of Superoxide Dismutase

Chromatograms

application for HPLC

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