Analytical Data
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Gene name
DTYMK
- Application
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Alternative Names
DTYMK；CDC8；TMPK；TYMK;Thymidylate kinase
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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
P23919
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Expression Region
1-212aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MAARRGALIV LEGVDRAGKS TQSRKLVEAL CAAGHRAELL RFPERSTEIG KLLSSYLQKK SDVEDHSVHL LFSANRWEQV PLIKEKLSQG VTLVVDRYAF SGVAFTGAKE NFSLDWCKQP DVGLPKPDLV LFLQLQLADA AKRGAFGHER YENGAFQERA LRCFHQLMKD TTLNWKMVDA SKSIEAVHED IRVLSEDAIR TATEKPLGEL WK
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Molecular Weight
24 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
DTYMK, or Deoxythymidylate Kinase, is a crucial enzyme involved in the regulation of deoxyribonucleotide metabolism, playing a vital role in DNA synthesis and repair. As a key player in the salvage pathway of nucleotide metabolism, DTYMK catalyzes the phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), thus providing a direct source of deoxythymidine nucleotides necessary for DNA replication and cell division. Given its pivotal function, DTYMK has garnered attention in cancer research, as tumor cells often exhibit altered nucleotide metabolism to support their rapid proliferation. Additionally, the enzyme's structure and function make it a potential target for therapeutic intervention, as inhibiting DTYMK could disrupt tumor growth by depriving cancer cells of essential nucleotides. Advances in protein engineering and structural biology have facilitated the investigation of DTYMK’s properties, shedding light on its enzymatic mechanisms and paving the way for the development of novel inhibitors. Understanding the biochemical pathways involving DTYMK can help in designing targeted treatments for cancers characterized by dysregulated nucleotide metabolism, ultimately contributing to more effective cancer therapies. Thus, ongoing research into DTYMK not only enhances the fundamental knowledge of nucleotide biochemistry but also opens new avenues for drug discovery in oncology.
