Analytical Data
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Gene name
TYMS
- Application
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Alternative Names
TYMS；TS；Thymidylate synthase
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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
P04818
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Expression Region
2-313aa
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AA Sequence
PVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGM QARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSL GFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCA WNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHIT GLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGY NPHPTIKMEMAV
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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
TYMS (thymidylate synthase) is a key enzyme involved in de novo pyrimidine biosynthesis, playing a crucial role in DNA synthesis and repair. Its function is vital for cellular proliferation, making it a significant target in cancer therapy, particularly in the treatment of solid tumors where rapid cell division occurs. Overexpression of TYMS has been linked to resistance against chemotherapeutic agents such as 5-fluorouracil (5-FU), a common drug used in cancer treatment. This has prompted extensive research into understanding the molecular mechanisms regulating TYMS expression and activity, as well as the development of TYMS inhibitors as novel therapeutic agents. Additionally, studying the structure and function of recombinant TYMS proteins can provide insights into its enzymatic mechanisms, interactions with ligands, and potential post-translational modifications. By employing techniques such as site-directed mutagenesis, X-ray crystallography, and recombinant DNA technology, researchers aim to elucidate the enzyme's role in cellular processes and its implications in oncogenesis. This research is crucial for improving existing cancer therapies and developing new strategies to circumvent drug resistance, ultimately aiding in more effective treatment modalities for cancer patients.
