Analytical Data
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Gene name
SOD3
- Application
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Alternative Names
SOD3；Extracellular superoxide dismutase [Cu-Zn]
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08294
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Expression Region
19-240aa
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AA Sequence
WTGEDSAEPNSDSAEWIRDMYAKVTEIWQEVMQRRDDDGALHAACQVQPSATLDAAQPRVTGVVLFRQLAPRAKLDAFFALEGFPTEPNSSSRAIHVHQFGDLSQGCESTGPHYNPLAVPHPQHPGDFGNFAVRDGSLWRYRAGLAASLAGPHSIVGRAVVVHAGEDDLGRGGNQASVENGNAGRRLACCVVGVCGPGLWERQAREHSERKKRRRESECKAA
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Molecular Weight
28.1kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
SOD3, or superoxide dismutase 3, is a critical extracellular antioxidant enzyme that plays a vital role in protecting tissues from oxidative stress by catalyzing the dismutation of superoxide radicals into hydrogen peroxide and oxygen. Research on SOD3 has gained significant attention due to its potential therapeutic applications in various diseases associated with oxidative damage, such as cardiovascular diseases, neurodegenerative disorders, and inflammatory conditions. The enzyme is predominantly expressed in the extracellular matrix and is essential for maintaining redox homeostasis. Studies have shown that reduced SOD3 activity is linked to increased susceptibility to oxidative stress-related diseases. Therefore, recombinantly produced SOD3 has been explored for its potential in clinical therapies, allowing for detailed investigation into its structure-function relationship and mechanisms of action. The production of SOD3 as a recombinant protein facilitates large-scale studies, allowing researchers to examine its antioxidant properties, stability, and interactions with other biomolecules. Additionally, therapeutic approaches involving SOD3, such as gene therapy or the use of SOD3 mimetics, hold promise for enhancing the enzyme's protective effects in pathological conditions. Overall, the ongoing research on SOD3 recombinant protein underscores its significance in oxidative stress management and its potential as a target for novel therapeutic strategies.
