| Identification | Back Directory | [Name]
Superoxide dismutase | [CAS]
9054-89-1 | [Synonyms]
SOD
SOD1
SOD-3
hrSOD
EC-SOD
rh-SOD1
Cuprein
Ontosein
Ormetein
Palosein
ORGOTEIN
CU/ZN SOD
Dismutase
Sudismase
SOD、Fe-SOD
Paroxi-norn
SOD (CU/ZN)
EC 1.15.1.1
EC: 1.15.1.1
IUB: 1.15.1.1
Dismuzyme Plus
Peroxide dismutase
Superphycodismutase
Superoxide dismutase
Dismutase,superoxide
Super Oxide DlsMutase
superoxide dismutase F
Super Oxidase Dimutase
Super oxidase dismutase
SOD Superoxide Dismuyase
SUPEROXIDE OXIDOREDUCTASE
CU/ZN-SUPEROXIDE DISMUTASE
SUPEROXIDE DISMUTASE, HUMAN
SUPEROXIDE DISMUTASE(MN TYPE)
Superoxid dismutase, lyophil.
Superoxide Dismutase 1 bovine
Superoxide Distamuses EUK-189
SUPEROXIDE DISMUTASE, 20000u/mg
SUPEROXIDE DISMUTASE HUMAN (SOD)
Superoxide Dismutase(Cu.Zn-SOD)
Superoxide Dismutase bovine
SUPEROXIDE DISMUTASE BOVINE LIVER
Native Human Superoxide Dismutase
Native Plant Superoxide Dismutase
Native Canine Superoxide Dismutase
Native Bovine Superoxide Dismutase
Native Porcine Superoxide Dismutase
Superoxide Dismutase from pig blood
Superoxide DisMutase, Water Soluble
frombovineerythrocytescontact,sales
Superoxide diMutase (Mn-SOD, Fe-SOD)
Mn-Superoxide Dismutase, Recombinant
Cu/Zn- Superoxide Dismutase，Cu/Zn-SOD
SUPEROXIDE DISMUTASE FROM HORSERADISH
SUPEROXIDE: SUPEROXIDE OXIDOREDUCTASE
Recombinant Human Superoxide Dismutase
Recombinant Human SOD1 Protein, His Tag
Cu/Zn Superoxide Dismutase, Recombinant
Native Horseradish Superoxide Dismutase
superoxidedismutasef.bovineerythro-cytes
SUPEROXIDE DISMUTASE, CU/ZN SALT, HISTID
Extracellular superoxide dismutase [Cu-Zn]
SUPEROXIDE DISMUTASE FROM ESCHERICHIA*CO LI
SUPEROXIDE DISMUTASE FROM DOG*ERYTHROCYT ES
Native Escherichia coli Superoxide Dismutase
Superoxide Dismutase from Bovine, Recombinant
Recombinant Human Superoxide Dismutase(rhSOD)
superoxide dismutase from bovine*erythrocytes
Superoxide Dismutase, Human, Recomb., E. coli
ANTI-SOD3 (N-TERM) antibody produced in rabbit
Superoxide Dismutase copper-zinc salt human
Superoxide Dismutase Solution,Human,recombinant
superoxide dismutase microbial sources*from esche
Superoxide dismutase from Bovine Erythrocytes(SOD)
SUPEROXIDE DISMUTASE FROM BOVINE*ERYTHRO CYTES CELL
Native Silphium perfoliatum L. Superoxide Dismutase
SUPEROXIDE DISMUTASE MICROBIAL SOURCES*F ROM ESCHERI
Native Bacillus stearothermophilus Superoxide Dismutase
SUPEROXIDE DISMUTASE F. BOVINE ERYTHRO-C YTES, ~3000 U/MG
SUPEROXIDE DISMUTASE FROM BOVINE LIVER, LYOPH.,~1000 U/MG*
Superoxide Dismutase from Bacillus stearothermophilus
Superoxide dismutase, from bovine erythrocytes , 2500 units/mg
Superoxide Dismutase from bovine erythrocytes lyophilized powder
Superoxide dismutase from bovine erythrocytes ca. 3 000 units/mg
Superoxide dismutase from bovine erythrocytes min. 3 000 units/mg
Recombinant Human Copper, Zinc-Superoxide Dismutase (rhCu, Zn-SOD)
Superoxide disMutase froM bovine erythrocytes Min. 3 000 units/Mg lyophil.
Superoxide Dismutase from horseradish,SOD, Superoxide: superoxide oxidoreductase
Superoxide Dismutase from bovine liver,SOD, Superoxide: superoxide oxidoreductase
Superoxide Dismutase from Escherichia coli,SOD, Superoxide: superoxide oxidoreductase
Superoxide Dismutase from human erythrocytes,SOD, Superoxide: superoxide oxidoreductase
Superoxide Dismutase from bovine erythrocytes,SOD, Superoxide: superoxide oxidoreductase
Superoxide Dismutase from canine erythrocytes,SOD, Superoxide: superoxide oxidoreductase
Superoxide Dismutase from bovine erythrocytes BioReagent, >=3,000 units/mg protein, suitable for cell culture, lyophilized powder | [EINECS(EC#)]
232-943-0 | [Molecular Formula]
NULL | [MDL Number]
MFCD00132404 |
| Chemical Properties | Back Directory | [storage temp. ]
2-8°C
| [solubility ]
Dissolves readily at 5 mg/mL in 0.05 M potassium phosphate buffer, pH 7.8, containing 0.1 mM EDTA. | [form ]
powder
| [color ]
blue-gray
| [Uses]
superoxide dismutase (polyoxyalkylene-modified) is used in cosmetic preparations to prevent drying and aging of the skin without causing irritation. |
| Hazard Information | Back Directory | [Chemical Properties]
from bovine erythrocytes | [Definition]
Any of a type of antioxidant metalloenzymes that occur in aerobic and facultatitive bacteria and in eukarotes. They catalyze a reaction in which two molecules of the highly toxic, highly reactive, superoxide anion is converted into one molecule each of hydrogen peroxide and molecular oxygen.
| [Brand name]
Palosein Veterinary (Oxis). | [Description]
Superoxide dismutase is widely present in the human body, including the skin and its appendages. | [benefits]
Based on the metal cofactors present in the active sites, Superoxide dismutases (SODs) can be classified into four distinct groups: Copper-Zinc-SOD (Cu, Zn-SOD), Iron SOD (Fe-SOD), Manganese SOD (Mn-SOD), and Nickel SOD. The enzyme can serve as an anti-inflammatory agent and can also prevent precancerous cell changes. SOD is used in cosmetics and personal care products as an anti-aging ingredient and antioxidant due to its ability to reduce free radical damage to the skin, therefore preventing wrinkles, fine lines, and age spots, and it also helps with wound healing, softens scar tissue, protects against UV rays, and reduces other signs of aging. It has been reported that SOD has an important link in several human health problems including RBC-related disorders, cystic fibrosis (CF), postcholecystectomy pain syndrome, malignant breast disease, steroid-sensitive nephrotic syndrome, amyotrophic lateral sclerosis, neuronal apoptosis, AIDS, and cancer. In many animal models having myocardial ischemia-reperfusion injury, inflammation, cerebral ischemia-reperfusion injury, etc., SOD enzymes are found to be very effective. Furthermore, a strong association between the activity of SOD and Alzheimer's disease has been suggested by some researchers[1-2]. | [General Description]
Superoxide dismutases are a group of low molecular weight metalloproteins present in all aerobic cells of plants, animals and micro-organisms. They provide protection against damaging reactions with the superoxide radical anion (O2-) by catalyzing its disproportionation into oxygen and hydrogen peroxide. | [Biochem/physiol Actions]
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. | [Clinical Use]
Superoxide dismutase is widely studied and used for anti-inflammatory, anti-tumor, radiation protection and anti-aging applications. | [Purification Methods]
The dismutase is purified by DEAE-Sepharose and copper chelate affinity chromatography. The preparation is homogeneous by SDS-PAGE, by analytical gel filtration chromatography and by isoelectric focusing [Weselake et al. Anal Biochem 155 193 1986, Fridovich J Biol Chem 244 6049 1969]. | [References]
[1] Younus H. "Therapeutic potentials of superoxide dismutase" Int J Health Sci (Qassim)12(2018).
[2] Batinic-Haberle, Ines, et al. "Rational Design of Superoxide Dismutase (SOD) Mimics: The Evaluation of the Therapeutic Potential of New Cationic Mn Porphyrins with Linear and Cyclic Substituents." Inorganic Chemistry: A Research Journal that Includes Bioinorganic, Catalytic, Organometallic, Solid-State, and Synthetic Chemistry and Reaction Dynamics(2014). |
| Questions And Answer | Back Directory | [Distinct classes]
Three classes of SOD have evolved with distinct protein folds and different catalytic metal ions: Cu, ZnSODs, MnSOD/FeSODs, and NiSODs:
1. Cu, ZnSOD (also known as SOD1 and SOD3 in humans) occurs in eukaryotes and some prokaryotes, and point mutations in human Cu, ZnSOD are linked to the fatal neurodegenerative disease amyotrophic lateral sclerosis (ALS, also known as Lou Gehrig’s disease).
2. FeSOD and MnSOD (also referred to as SOD2 in humans) appear to have evolved from a common ancestral gene, with the FeSOD gene observed in primitive eukaryotes, the plastids of plants, and bacteria. Phylogenetic analysis of MnSOD indicates that it occurs in all the major domains of life, in the mitochondria of eukaryotes, and in the cytoplasm of many bacteria. FeSOD and MnSOD have diverged significantly from each other so that the two metals cannot functionally substitute for each other in Mn/FeSODs from most species.
3. The more recently discovered NiSOD has been found only in bacteria.
Common to all three classes of SOD is the disproportionation reaction, occurring through alternate oxidation and reduction of their catalytic metal ions, and rather remarkably, SOD catalysis takes place at rates close to diffusion limits. Although the protein architectures of the three SOD classes are distinct, all crucially provide electrostatic guidance for the superoxide substrate and alter the metal ion redox potential to a range suitable for superoxide disproportionation. These structures also provide for a suitable proton source and may control enzymatic activity through product inhibition[3]. |
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