Analytical Data
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Gene name
Thymidylate
- Application
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Alternative Names
CDC8; TMPK; TYMK; Thymidylate Kinase; dTMP Kinase
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
D3ZUJ5
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Expression Region
Pro43~Glu190
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Molecular Weight
21kDa
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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
Thymidylate synthase (TS) is a vital enzyme involved in the de novo synthesis of thymidine, which is essential for DNA replication and repair. TS catalyzes the reductive methylation of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP) using tetrahydrofolate as a cofactor. Given its crucial role in the synthesis of DNA, TS has garnered significant attention in cancer research, particularly because its inhibition can lead to the depletion of nucleotide pools, thereby hindering tumor cell proliferation. Several chemotherapeutic agents, such as 5-fluorouracil, target TS, and understanding the structure and function of the enzyme can provide insights into drug resistance mechanisms and facilitate the design of novel therapeutic strategies. Moreover, recombinant TS proteins have been produced for detailed biochemical and structural studies, allowing researchers to uncover the enzyme's mechanism of action, substrate specificity, and interactions with inhibitors. These studies not only enhance the understanding of TS's role in cellular processes but also hold potential for developing targeted cancer therapies. The continuous exploration of TS and its recombinant forms stands as a cornerstone in the search for effective treatments against malignancies characterized by dysregulated DNA synthesis.
