Analytical Data
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Gene name
SOD2
- Application
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Alternative Names
SOD2;Superoxide dismutase [Mn]. mitochondrial
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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
P04179
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Expression Region
25-222aa
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AA Sequence
KHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN NLNVTEEKYQ EALAKGDVTA QIALQPALKF NGGGHINHSI FWTNLSPNGG GEPKGELLEA IKRDFGSFDK FKEKLTAASV GVQGSGWGWL GFNKERGHLQ IAACPNQDPL QGTTGLIPLL GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVTERYMAC KK
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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
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Protein Description
SOD2, or superoxide dismutase 2, is a critical mitochondrial enzyme that protects cells from oxidative damage by catalyzing the dismutation of superoxide radicals into hydrogen peroxide and molecular oxygen. Its role in cellular defense mechanisms makes it a significant focus of research, particularly in the context of age-related diseases, neurodegenerative disorders, and cancer. Dysfunctional SOD2 has been linked to increased oxidative stress, which can lead to mitochondrial dysfunction and contribute to the pathogenesis of various diseases. Recombinant SOD2 protein has emerged as a valuable tool for both basic and applied research, enabling scientists to investigate its biochemical properties, role in oxidative stress response, and potential therapeutic applications. The production of SOD2 in recombinant systems facilitates the study of its structure-function relationships, the design of SOD2 mimetics, and the development of gene therapy strategies aimed at enhancing SOD2 expression in tissues with oxidative stress. By exploring the therapeutic benefits of SOD2, researchers aim to develop novel interventions to combat oxidative damage and improve health outcomes in conditions associated with elevated oxidative stress. Overall, the study of recombinant SOD2 protein serves as a pivotal foundation for understanding its biological significance and potential clinical applications.
