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S7446

Sigma-Aldrich

Superoxide Dismutase from bovine erythrocytes

BioUltra, lyophilized powder, ≥4,500 units/mg protein, ≥97% (SDS-PAGE)

Synonym(s):

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

product line

BioUltra

Quality Level

Assay

≥97% (SDS-PAGE)

form

lyophilized powder

specific activity

≥4,500 units/mg protein

mol wt

32.5 kDa

composition

Protein, ≥95% biuret

relevant disease(s)

arthritis

storage temp.

−20°C

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General description

Research area: Cell signaling. Superoxide Dismutase (SOD) is found in allaerobic cells of the animals, plants, and microorganisms. It is a low molecularweight protein that exists as three different forms such as manganese SOD,copper–zinc SOD, and extracellular SOD.

Application

Superoxide Dismutase from bovine erythrocytes has been used in a study to assess activity parameters in adjuvant-induced arthritis. Superoxide Dismutase from bovine erythrocytes has also been used in a study to simplify the process of purifying superoxide dismutases using charge-controlled hydrophobic chromatography on 10-carboxydecyl Sepharose. It has also been used as a standard in SOD assay in mice liver andkidney samples.

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.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

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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A García-González et al.
Archives of medical research, 30(2), 132-137 (1999-06-18)
The purpose of this work was to evaluate the effect of superoxide dismutase (SOD) on primary swelling, lipoperoxidation, body thymus, and spleen weight in the adjuvant-induced arthritis (AIA) model in rats. Orally and intraperitoneally administered SOD (100 U/kg) from bovine
Aloysia citrodora extract as a chemopreventive agent against HPV16-induced lesions: findings from K14-HPV16 mice
Medeiros F, et al.
Exploration of targeted anti-tumor therapy, 5, 416-433 (2024)
Karen E Butler et al.
Frontiers in chemistry, 9, 614595-614595 (2021-02-27)
Native mass spectrometry has emerged as a powerful tool for structural biology as it enables the evaluation of molecules as they occur in their physiological conditions. Ion mobility spectrometry-mass spectrometry (IMS-MS) has shown essential in these analyses as it allows
Lu Miao et al.
Free radical biology & medicine, 47(4), 344-356 (2009-05-30)
Numerous short-lived and highly reactive oxygen species (ROS) such as superoxide (O2(.-)), hydroxyl radical, and hydrogen peroxide are continuously generated in vivo. Depending upon concentration, location, and intracellular conditions, ROS can cause toxicity or act as signaling molecules. The cellular
Characterisation by EPR spectroscopy of the co-ordination environment of copper in superoxide dismutase from horseradish (Armoracia rusticana Gaertn.)
Palivan, CG and Palivan, H
Proceedings of the Royal Society of Edinburgh. Section B: Biology, 102, 273-277 (1994)

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