dismutase

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Superoxide dismutase [Fe] Protein, Anabaena sp., Recombinant (His & KSI) is expressed in E. coli expression system with N-6xHis-KSI tag. The predicted molecular weight is 16.4 kDa and the accession number is P83157.

Destroys radicals which are normally produced within the cells and which are toxic to biological systems. SOD1 Protein, Mouse, Recombinant (E. coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 19.8 kDa and the accession number is P08228.

Destroys radicals which are normally produced within the cells and which are toxic to biological systems. May play a role in favoring mycobacterial survival in phagocytes. SodC Protein, Mycobacterium tuberculosis, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 28.1 kDa and the accession number is P9WGE8.

SOD1 Protein, Danio rerio, Recombinant (His & Myc & SUMO) is expressed in E. coli.

Superoxide Dismutase (SOD2) belongs to the iron manganese superoxide dismutase family. SOD2 is a mitochondrial matrix protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 transforms toxic superoxide, a byproduct of the mitochondrial electron transport chain into hydrogen peroxide and diatomic oxygen. It is reported that oxidative stress plays an essential role in the development of breast cancer, while SOD2 is one of the primary enzymes that directly convert potential harmful oxidizing species to harmless metabolites.

Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen. SOD3 Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 24.1 kDa and the accession number is P08294.

Superoxide Dismutase (SOD2) is a number of the iron manganese superoxide dismutase family. SOD2 is a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. The SOD2 protein transforms toxic superoxide and a byproduct of the mitochondrial electron transport chain into hydrogen peroxide and diatomic oxygen. Genetic variation in SOD2 is associated with microvascular complications of diabetes type 6 (MVCD6), idiopathic cardiomyopathy (IDC), sporadic motor neuron disease, and cancer. SOD2 destroys superoxide anion radicals which are usually produced within the cells and which are toxic to biological systems.

Chlorite dismutase (Cld) found in prokaryotic organisms, also known as Chlorite O2-lyase, is a b-type heme containing enzyme that catalyzes the reduction of chlorite into chloride plus dioxygen. The subunit of chlorite dismutase consists of a heme free N-terminal and a heme b containing C-terminal ferredoxin-like fold with high structural homology to the dye-decolorizing peroxidases (DyPs). The physiological role of Cld in prokaryote has been shown that some microorganisms can use perchlorate or chlorate as terminal electron acceptors for anaerobic respiration thereby producing chlorite that must be detoxified. This enzyme has gained attention because it can be used in the development of bioremediation processes, biosensors, and controlled dioxygen production.

Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen. SOD3 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 28.1 kDa and the accession number is P08294.

Destroys radicals which are normally produced within the cells and which are toxic to biological systems. SOD1 Protein, Mouse, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 17.8 kDa and the accession number is P08228.

Destroys radicals which are normally produced within the cells and which are toxic to biological systems. SOD1 Protein, Rat, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 17.3 kDa and the accession number is P07632.

SOD1 belongs to the Cu-Zn superoxide dismutase family. It binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene. SOD1 destroys radicals which are normally produced within the cells and which are toxic to biological systems. Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1). ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.

Superoxide dismutases (SOD) are important anti-oxidant enzymes that guard against superoxide toxicity. In humans, as in all mammals and most chordates, three forms of superoxide dismutase (SOD) are present: SOD1 is located in the cytoplasm, SOD2 in the mitochondria, and SOD3 is extracellular. Mitochondrial superoxide dismutase [SOD; manganese SOD (MnSOD) or SOD2] neutralizes highly reactive superoxide radical (O•-2), the first member in the plethora of mitochondrial reactive oxygen species.

Catalase is a ubiquitously expressed enzyme that catalyzes the decomposition of hydrogen peroxide to water and oxygen. It is a tetramer of four polypeptides chains containing four porphyrin heme groups that allow the enzyme to react with the hydrogen peroxide. The optimum PH of human catalase is approximately 7 and the optimum temperature is at 37 degree. Both the PH optimum and temperature for other catalases varies depending on the species. Catalase can be inhibited by a flux of O2-generated in situ by the aerobic xanthine oxidase reaction. This inhibition of catalase by O2-provides the basis for a synergism between superoxide dismutase and catalase.Such synergisms have been observed in vitro and may be significant in vivo. Catalase is used in the food industry for removing hydrogen peroxide from milk prior to cheese production. Another use is in food wrappers where it prevents food from oxidizing. Catalase is also used in the textile industry, removing hydrogen peroxide from fabrics to make sure the material is peroxide-free.