Analytical Data
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Gene name
CAT
- Application
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Alternative Names
CAT；Catalase
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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
P46402
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Expression Region
24-167aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSQAMFFKEIEELKGYFNASNPDVADGGS LFVDILKNWKEESDKTIIQSQIVSFYLKMFENLKDDDQRIQRSMDTIKED MLDKLLNTSSSKRDDFLKLIQIPVNDLQVQRKAINELFKVMNDLSPRSNL RKRKRSQNLFRGRRASK
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Molecular Weight
19 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 Catalase-Peroxidase (CAT) recombinant proteins has garnered significant interest due to their crucial role in the detoxification of reactive oxygen species (ROS) and their implications in various biological and medical fields. CAT enzymes, known for their ability to catalyze the conversion of hydrogen peroxide to water and oxygen, are instrumental in cellular defense mechanisms against oxidative stress. The recombinant expression of CAT proteins allows for the production of large quantities of these enzymes for research and therapeutic applications, enabling scientists to investigate their structural and functional properties in greater detail. Additionally, the exploration of CAT recombinants facilitates the understanding of their evolutionary adaptations and potential biotechnological applications, including their use in food preservation, environmental bioremediation, and the development of antioxidant therapies. As oxidative stress is linked to numerous diseases, including cancer and neurodegenerative disorders, the insights gained from studying CAT recombinant proteins could lead to novel strategies for disease prevention and treatment. Furthermore, advancements in genetic engineering and protein purification techniques have made it increasingly feasible to design and optimize CAT variants with enhanced activity and stability, thereby expanding their utility in various scientific and industrial applications.
