Analytical Data
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Gene name
TYMS
- Application
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Alternative Names
TS; TMS; TSase; Thymidylate Synthase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04818
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Expression Region
Gln36~Val313
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Molecular Weight
36kDa
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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
TYMS (thymidylate synthase) is a critical enzyme involved in the de novo synthesis of thymidine, a nucleotide essential for DNA replication and repair. Its activity is central to cellular proliferation, making it a significant target in cancer therapy, particularly for tumors characterized by rapid cell division. The overexpression of TYMS has been linked to resistance against antifolate chemotherapeutic agents, such as 5-fluorouracil, which inhibit its function. Consequently, understanding the structure and function of TYMS is essential for developing more effective therapeutic strategies. Research into recombinant TYMS proteins has gained momentum as these studies can elucidate the enzyme's mechanisms, substrate specificity, and interactions with inhibitors. By using recombinant DNA technology, researchers can produce large quantities of TYMS protein for biochemical and structural analyses, facilitating drug design and discovery. Furthermore, the study of mutant forms of TYMS may reveal insights into the variations in drug response observed in different tumors, paving the way for personalized medicine approaches. Overall, the investigation of TYMS through recombinant protein technology holds promise for advancing our understanding of cancer biology and improving treatment outcomes.
