Analytical Data
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Gene name
SOD1
- Application
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Alternative Names
SOD1;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
P00441
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Expression Region
2-154aa
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AA Sequence
MGHHHHHHHH HHSSGHIEGR HMTYARAAAR QARALE+ATKA VCVLKGDGPV QGIINFEQKE SNGPVKVWGS IKGLTEGLHG FHVHEFGDNT AGCTSAGPHF NPLSRKHGGP KDEERHVGDL GNVTADKDGV ADVSIEDSVI SLSGDHCIIG RTLVVHEKAD DLGKGGNEES TKTGNAGSRL ACGVIGIAQ
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Molecular Weight
20 kDa
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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
The study of SOD1 (Superoxide Dismutase 1) recombinant protein is rooted in its critical role in oxidative stress management within cells. SOD1 is an essential enzyme that catalyzes the conversion of superoxide radicals into hydrogen peroxide and oxygen, thereby protecting cellular systems from oxidative damage. Mutations in the SOD1 gene have been linked to familial amyotrophic lateral sclerosis (fALS), a progressive neurodegenerative disease characterized by the degeneration of motor neurons. This connection has propelled extensive research into the structure and function of SOD1, particularly in understanding how specific mutations lead to aberrant protein folding, aggregation, and subsequent toxicity in neural tissues. Recombinant SOD1 proteins are produced to investigate these properties, enabling the study of mutant forms in vitro and in vivo, shedding light on the mechanistic pathways involved in oxidative stress and neurodegeneration. Additionally, the production of SOD1 as a recombinant protein allows for detailed biochemical analysis, high-throughput screening for therapeutic compounds, and the exploration of potential interventions to mitigate the effects of SOD1 mutations. The ongoing research holds promise for advancements in treatments for ALS and related disorders, emphasizing the importance of SOD1 in both cellular physiology and disease pathology.
