Analytical Data
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基因名
DTYMK
- Application
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别名
DTYMK;CDC8;TMPK;TYMK;Thymidylate kinase
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P23919
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表达区间
1-212aa
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氨基酸序列
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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分子量
24 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.











