Human Superoxide dismutase, SOD Recombinant Protein (Active)
€0.00
In stock
SKU
BRP1088
Description: Recombinant human SOD protein with molecular weight 16 kDa.
Background:
Superoxide dismutases (SOD) are enzymes that catalyze the dismutation of superoxide into oxygen and hydrogen peroxide. Thus, they are an important antioxidant defense in nearly all cells exposed to oxygen. Several common forms of SOD exist: they are proteins cofactored with copper and zinc, or manganese, iron, or nickel. Thus, there are three major families of superoxide dismutase, depending on the metal cofactor: Cu/Zn (which binds both copper and zinc), Fe and Mn types (which bind either iron or manganese), and the Ni type, which binds nickel. Three forms of superoxide dismutase are present in humans, in all other mammals, and most chordates. SOD1 is located in the cytoplasm, SOD2 in the mitochondria, and SOD3 is extracellular. Mutations in the first SOD enzyme (SOD1) can cause familial amyotrophic lateral sclerosis (ALS, a form of motor neuron disease). The other two isoforms of SOD have not been linked to any human diseases, however, in mice inactivation of SOD2 causes perinatal lethality and inactivation of SOD1 causes hepatocellular carcinoma.
Synonyms:
Superoxide dismutase [Cu-Zn], SOD1, SOD
Purity: >95% by HPLC & SDS-PAGE
Endotoxin level: < 0.1 ng/μg (1 EU/μg) by LAL test
Reconstitution: Reconstitute with sterile 18MΩ-cm H2O.
Dimers: < 1% by SDS-PAGE
Storage buffer: Each vial contains 10 mM Phosphate bufferand 200 mM NaCl(pH7.0) without preservatives.
Storage and Expiration:
Ship at 4℃. Upon receipt, store at -20℃ or -80℃ for 2 years. After reconstituting, it can store at 4℃ for a week, it is recommended to add 0.1% HSA or BSA for long term. Avoid repeated freeze and thaw cycles.
Background:
Superoxide dismutases (SOD) are enzymes that catalyze the dismutation of superoxide into oxygen and hydrogen peroxide. Thus, they are an important antioxidant defense in nearly all cells exposed to oxygen. Several common forms of SOD exist: they are proteins cofactored with copper and zinc, or manganese, iron, or nickel. Thus, there are three major families of superoxide dismutase, depending on the metal cofactor: Cu/Zn (which binds both copper and zinc), Fe and Mn types (which bind either iron or manganese), and the Ni type, which binds nickel. Three forms of superoxide dismutase are present in humans, in all other mammals, and most chordates. SOD1 is located in the cytoplasm, SOD2 in the mitochondria, and SOD3 is extracellular. Mutations in the first SOD enzyme (SOD1) can cause familial amyotrophic lateral sclerosis (ALS, a form of motor neuron disease). The other two isoforms of SOD have not been linked to any human diseases, however, in mice inactivation of SOD2 causes perinatal lethality and inactivation of SOD1 causes hepatocellular carcinoma.
Synonyms:
Superoxide dismutase [Cu-Zn], SOD1, SOD
Purity: >95% by HPLC & SDS-PAGE
Endotoxin level: < 0.1 ng/μg (1 EU/μg) by LAL test
Reconstitution: Reconstitute with sterile 18MΩ-cm H2O.
Dimers: < 1% by SDS-PAGE
Storage buffer: Each vial contains 10 mM Phosphate bufferand 200 mM NaCl(pH7.0) without preservatives.
Storage and Expiration:
Ship at 4℃. Upon receipt, store at -20℃ or -80℃ for 2 years. After reconstituting, it can store at 4℃ for a week, it is recommended to add 0.1% HSA or BSA for long term. Avoid repeated freeze and thaw cycles.
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