Analytical Data
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Gene name
catA
- Application
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Alternative Names
1,2-CTD
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Species
Acinetobacter baylyi
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P07773
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Expression Region
1-311aa
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Molecular Weight
50.3 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 catA recombinant proteins has gained significant attention due to their potential applications in various biotechnological and therapeutic fields. CatA, or Catalase A, is an enzyme that plays a crucial role in protecting cells from oxidative stress by decomposing hydrogen peroxide into water and oxygen. This function is vital in both prokaryotic and eukaryotic organisms, as oxidative stress is linked to numerous diseases and cellular damage. The ability to produce catA recombinantly allows for large-scale production and detailed studies of its structure-function relationships. Furthermore, the recombinant form can be engineered to enhance its stability, catalytic efficiency, or specificity, which may lead to innovative solutions in treating oxidative stress-related conditions. Additionally, research into catA has implications in the fields of food preservation, as it can help in extending shelf life by inhibiting oxidative spoilage. The exploration of catA’s role in cellular pathways and its interactions with other biomolecules also opens avenues for understanding its broader biological significance. Overall, the investigation of catA recombinant proteins not only contributes to fundamental enzymology but also holds promise for practical applications in health, nutrition, and industry.
