S9636
Superoxide Dismutase from human erythrocytes
essentially salt-free, lyophilized powder, ≥2,500 units/mg protein
Synonym(s):
SOD, Superoxide: superoxide oxidoreductase
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About This Item
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form
essentially salt-free, lyophilized powder
Quality Level
specific activity
≥2,500 units/mg protein
mol wt
32.0 kDa
composition
Protein, ≥80% biuret
technique(s)
activity assay: suitable
suitability
suitable for molecular biology
storage temp.
−20°C
Gene Information
human ... SOD1(6647) , SOD2(6648) , SOD3(6649)
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General description
Superoxide dismutases (SOD) are a group of low molecular weight metalloproteins present in all aerobic cells of plants, animals and micro-organisms. Three forms of SOD exist, based on the metal ions in the active site. These are Cu2+/Zn2+, Mn2+ and Fe2+ containing SOD. In vertebrate organisms, Cu/Zn-SOD is located in the cytoplasm as well as the mitochondrial intermembrane space, whereas Mn-SOD is located at the mitochondrial matrix space in prokaryotes. Fe-SOD is also found in prokaryotes and higher plants. Human erythrocyte SOD is a non-covalently bound homodimeric protein with two 16.3 kDa subunits containing 153 amino acids. Each dimer consists of two Cu2+ atoms and two Zn2+ atoms.
Application
Superoxide Dismutase from human erythrocytes has been used:
- to test its effect on human neutrophils in reactive oxygen species (ROS) measurement studies involving Pseudomonas aeruginosa infection
- as an antioxidant to test its effect on ROS generation induced by atmospheric-pressure plasma jet (APPJ) in red blood cell (RBC) homogenates using optical spectroscopy studies
- to test its attenuating effect on hemoglobin (Hb)-induced nuclear factor-kappa B (NF- κB) and hypoxia-inducible factor (HIF) activity in human dermal microvascular endothelial cells (HMECs-1)
- as a reference antioxidant protein to examine its expression in human intestinal Caco-2 cells following treatment with dietary flavonoids
- in combination with catalase to promote cell differentiation in vitro
Biochem/physiol Actions
Mutations in the SOD1 gene are implicated in Amyotrophic lateral sclerosis (ALS).
Catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. 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.
Analysis Note
For assay method, see McCord, J.M. and Fridovich, I., J. Biol. Chem., 244, 6049 (1969).
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
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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American journal of respiratory cell and molecular biology, 49(4), 619-626 (2013-05-30)
The release of hemoglobin (Hb) with hemolysis causes vascular dysfunction. New evidence implicates Hb-induced NF-κB and hypoxia inducible factor (HIF) activation, which may be under the control of a Toll-like receptor (TLR)-signaling pathway. Nearly all TLR-signaling pathways activate the myeloid
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Scientific reports, 9(1), 6724-6724 (2019-05-02)
Non-natively folded variants of superoxide dismutase 1 (SOD1) are thought to contribute to the pathogenesis of familial amyotrophic lateral sclerosis (ALS), however the relative toxicities of these variants are controversial. Here, we aimed to decipher the relationships between the different
J V Bannister et al.
CRC critical reviews in biochemistry, 22(2), 111-180 (1987-01-01)
The current status of superoxide dismutase (SOD) is that it is an enzyme with diverse ramifications. This review attempts an understanding of SOD as a structural, functional, and biological entity. Accordingly, the review is in three parts. The first part
L Guemouri et al.
Clinical chemistry, 37(11), 1932-1937 (1991-11-01)
We studied the biological variability of blood superoxide dismutase (SOD; EC 1.15.1.1), glutathione peroxidase (GPX; EC 1.11.1.9), and catalase (CAT; EC 1.11.1.6) in a sample of 1836 apparently health subjects, ages 4-97 years. SOD and GPX activities were assayed in
M Iu Eropkin et al.
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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
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