Analytical Data
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Gene name
TYMP
- Application
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Alternative Names
TYMP；ECGF1；Thymidine phosphorylase
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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
P19971
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Expression Region
11-482aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMAPPAPGDFSGEGSQGLPDPSPEPKQLPEL IRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETS VLTQALAQSGQQLEWPEAWRQQLVDKHSTGGVGDKVSLVLAPALAACGCK VPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSE QLVPADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGA AVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPLGRCVGHALEVEE ALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSA LGRFERMLAAQGVDPGLARALCSGSPAERRQLLPRAREQEELLAPADGTV ELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRGTPWLR VHRDGPALSGPQSRALQEALVLSDRAPFAAPSPFAELVLPPQQ
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Molecular Weight
51 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
TYMP (thymidine phosphorylase) is an important enzyme involved in nucleoside metabolism, specifically catalyzing the phosphorylation of thymidine to produce deoxyribose-1-phosphate, which is a key component for DNA synthesis and repair. Dysregulation of TYMP has been implicated in various pathological conditions, including cancer, where it may promote tumor growth and angiogenesis by facilitating the availability of nucleotides. Additionally, TYMP has been associated with drug metabolism and resistance, particularly in the context of chemotherapeutic agents like gemcitabine. Given its significance in cellular processes, the study of TYMP as a recombinant protein has garnered attention for potential therapeutic applications, including drug design and targeted cancer therapies. The ability to produce and purify TYMP in a controlled environment allows researchers to explore its biochemical properties, substrate specificity, and interaction with other molecules. Understanding the functional mechanisms of TYMP can also provide insights into new strategies for overcoming drug resistance and enhancing the efficacy of existing treatments. By leveraging advances in recombinant DNA technology, researchers aim to generate modified versions of TYMP that may exhibit improved stability or altered enzymatic activity, potentially paving the way for innovative therapeutic approaches. Overall, research on TYMP recombinant protein is crucial for elucidating its role in metabolic pathways and its impact on human health, particularly in cancer pathophysiology and therapy.
