Analytical Data
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Gene name
sodC
- Application
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Alternative Names
sodC；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
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Protein Description
The study of sodC (superoxide dismutase C) recombinant protein is rooted in the broader understanding of oxidative stress and its implications for cellular health. Superoxide dismutases are pivotal enzymes that catalyze the dismutation of superoxide radicals into oxygen and hydrogen peroxide, thereby mitigating oxidative damage within cells. The sodC gene, which encodes a metal-independent superoxide dismutase, is predominantly found in bacteria and plays a crucial role in their defense mechanisms against oxidative damage caused by environmental stresses. Research into sodC recombinant protein involves the expression, purification, and characterization of the enzyme to better understand its functionality and significance in microbial pathogenesis. Enhanced oxidative stress resistance conferred by sodC may be implicated in bacterial survival in hostile environments, including the human immune response. By exploring the structural and biochemical properties of sodC, scientists aim to uncover its potential applications in biotechnology and medicine, such as the development of antioxidants or therapeutic agents targeting oxidative stress-related diseases. Increased knowledge of this enzyme not only contributes to fundamental microbiological research but also offers insights into potential novel strategies for combating bacterial infections and enhancing human health.
