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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

Synonym(s):

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

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine

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.

sustainability

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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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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

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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C A Chuaqui et al.
Biochimica et biophysica acta, 702(1), 112-116 (1982-03-18)
It has been reported that the inactivation yield of superoxide dismutase from bovine erythrocytes irradiated in N2O-saturated solutions increases exponentially with the initial enzyme concentration and that dose-response curves are non-exponential. The present work analyses these data using a kinetic
Superoxide dismutase and catalase significantly improve the osteogenic differentiation potential of osteogenetically compromised human adipose tissue-derived stromal cells in vitro
Sahlender B, et al.
Stem Cell Research (2022)
Superoxide-Mediated Upregulation of MMP9 Participates in BMPR2 Destabilization and Pulmonary Hypertension Development
Antioxidants, 12(11), 1961-1961 (2023)
Colleen M Hansel et al.
mBio, 10(2) (2019-03-14)
There is a growing appreciation within animal and plant physiology that the reactive oxygen species (ROS) superoxide is not only detrimental but also essential for life. Yet, despite widespread production of extracellular superoxide by healthy bacteria and phytoplankton, this molecule
Possible participation of superoxide anion in the intestinal tryptophan 2,3-dioxygenase reaction.
F Hirata et al.
The Journal of biological chemistry, 246(24), 7825-7826 (1971-12-25)

Articles

Cellular oxidative stress is countered by enzymatic scavengers and antioxidant modulators against reactive oxygen species damage.

Cellular oxidative stress is countered by enzymatic scavengers and antioxidant modulators against reactive oxygen species damage.

Cellular oxidative stress is countered by enzymatic scavengers and antioxidant modulators against reactive oxygen species damage.

Cellular oxidative stress is countered by enzymatic scavengers and antioxidant modulators against reactive oxygen species damage.

Protocols

Enzymatic Assay of Superoxide Dismutase

Chromatograms

application for HPLC

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