Recombinant human Superoxide Dismutase 1 protein is a Human Full Length protein, in the 1 to 154 aa range, expressed in Escherichia coli, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS, HPLC.
M A T K A V C V L K G D G P V Q G I I N F E Q K E S N G P V K V W G S I K G L T E G L H G F H V H E F G D N T A G C T S A G P H F N P L S R K H G G P K D E E R H V G D L G N V T A D K D G V A D V S I E D S V I S L S G D H C I I G R T L V V H E K A D D L G K G G N E E S T K T G N A G S R L A C G V I G I A Q
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Application HPLC | Reactivity Reacts | Dilution info - | Notes - |
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Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Superoxide dismutase [Cu-Zn], Superoxide dismutase 1, hSod1, SOD1
Recombinant human Superoxide Dismutase 1 protein is a Human Full Length protein, in the 1 to 154 aa range, expressed in Escherichia coli, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS, HPLC.
The potency per mg was tested by Pyrogallic Acid method and was found to be more than 10,000Units/mg.
pH: 7.4
Constituents: 100% PBS
>95% by HPLC analysis.
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Belongs to the Cu-Zn superoxide dismutase family.
Unlike wild-type protein, the pathogenic variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 are polyubiquitinated by RNF19A leading to their proteasomal degradation. The pathogenic variants ALS1 Arg-86 and Ala-94 are ubiquitinated by MARCH5 leading to their proteasomal degradation.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Superoxide Dismutase 1 (SOD1) also known as Cu/Zn SOD or simply dismutase is an enzyme important for the detoxification of superoxide radicals. SOD1 catalyzes the conversion of two superoxide molecules into oxygen and hydrogen peroxide maintaining cellular redox balance. This enzyme typically exhibits a mass of approximately 32 kDa. SOD1 is expressed in the cytoplasm of cells throughout the body including tissues like liver kidney and brain.
The enzyme functions as a homodimer with each subunit containing a copper and zinc ion. These metal ions are essential for the catalytic activity of SOD1 as the copper ion participates in electron transfer while the zinc ion provides structural stability. The enzyme protects cells from oxidative stress by neutralizing excess reactive oxygen species ensuring cellular health and functioning.
SOD1 plays an important role in the cellular antioxidant defense system and is a part of the reactive oxygen species (ROS) metabolic pathway. It works in conjunction with catalase and glutathione peroxidase to limit oxidative damage within cells. The close interaction between these enzymes highlights the interdependence within the antioxidant defense network emphasizing their role in maintaining cellular homeostasis.
Mutations in the SOD1 gene are linked to familial Amyotrophic Lateral Sclerosis (ALS) a neurodegenerative condition. In ALS aberrant SOD1 proteins may lead to increased oxidative stress and motor neuron damage. Research also connects SOD1 to the pathogenesis of Alzheimer's disease where oxidative stress is a contributing factor. These associations underline SOD1's significance in neurodegenerative diseases highlighting potential therapeutic targets for interventions focused on oxidative stress management.
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