Analytical Data
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Gene name
Cytosine deaminase/CodA
- Application
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Alternative Names
Cytosine aminohydrolaseIsoguanine deaminase1
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Species
Escherichia coli
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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
P25524
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Expression Region
2-427aa
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Molecular Weight
63.5 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
Cytosine deaminase (CDA), also known as CodA, is an enzyme that catalyzes the deamination of cytosine to uracil, playing a pivotal role in nucleic acid metabolism and the regulation of nucleotide pools in various organisms. The study of CDA has gained significance in the context of cancer therapy, particularly in the development of suicide gene therapies, where the enzyme converts a non-toxic prodrug into a toxic metabolite specifically within tumor cells. This targeted approach enhances the therapeutic efficacy while minimizing systemic toxicity. Additionally, CDA is of interest in synthetic biology, where its ability to manipulate nucleotides can be utilized for creating novel biosynthetic pathways and metabolic engineering. Researchers have focused on characterizing and optimizing CodA through recombinant protein expression techniques, enhancing its stability, activity, and substrate specificity. Such studies involve the cloning of the CDA gene, expression in suitable host organisms, and subsequent purification of the protein. Understanding the structure-function relationships of CDA not only facilitates its application in medical and biotechnological fields but also deepens our comprehension of evolutionary adaptation and enzyme mechanisms. The exploration of CDA and its recombinant forms opens avenues for innovative treatments and biotechnological applications, making it a key focus for ongoing research in enzymology and gene therapy.
