| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DTYMK |
| Uniprot No | P23919 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-212aa |
| 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 |
| 预测分子量 | 24 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于DTYMK(胸苷酸激酶)重组蛋白的模拟参考文献示例(注：以下内容为学术场景模拟，非真实文献)：
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1. **文献名称**: *Expression and purification of recombinant DTYMK in Escherichia coli for enzymatic studies*
**作者**: Chen L, Wang H, et al.
**摘要**: 本研究报道了通过大肠杆菌表达系统高效表达人源DTYMK重组蛋白的优化方法。通过亲和层析和凝胶过滤纯化获得高纯度蛋白，并验证其催化dTMP磷酸化为dTDP的酶活性，为后续药物筛选提供基础。
2. **文献名称**: *Structural insights into DTYMK's catalytic mechanism by X-ray crystallography*
**作者**: Kumar S, Zhang Y, et al.
**摘要**: 利用X射线晶体学解析了重组DTYMK蛋白的3D结构(分辨率2.1 Å)，揭示了其与底物dTMP和ATP结合的活性位点特征，阐明了其磷酸转移反应的分子机制。
3. **文献名称**: *Functional characterization of DTYMK mutations associated with mitochondrial disorders*
**作者**: Rossi M, Gonzalez F, et al.
**摘要**: 通过体外重组表达携带致病突变的DTYMK蛋白，发现部分突变体(如R189C)的酶活性显著降低，导致dTTP合成障碍，提示其与线粒体DNA复制缺陷疾病的关联。
4. **文献名称**: *DTYMK as a potential target for antiviral therapy: Inhibitor screening and validation*
**作者**: Lee J, Kim T, et al.
**摘要**: 基于重组DTYMK蛋白建立高通量抑制剂筛选平台，发现小分子化合物X可竞争性抑制酶活性(IC50=8.2 μM)，在细胞模型中有效抑制疱疹病毒复制。
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注：以上文献为模拟生成，实际引用时需检索PubMed、Web of Science等数据库获取真实文献。
**Background of DTYMK Recombinant Protein**
DTYMK (deoxythymidylate kinase), also known as thymidylate kinase (TYMK), is a key enzyme involved in nucleotide metabolism, specifically catalyzing the phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP). This reaction is a critical step in the synthesis of dTTP, an essential precursor for DNA replication and repair. As such, DTYMK plays a vital role in cell proliferation and genome stability, making it a focus in cancer research, antiviral drug development, and studies of genetic disorders linked to nucleotide imbalance.
The recombinant DTYMK protein is produced using genetic engineering techniques, where the *DTYMK* gene is cloned into expression vectors and expressed in host systems like *E. coli* or mammalian cells. This approach ensures high purity, scalability, and consistency compared to isolating the protein from native tissues. Recombinant DTYMK often includes affinity tags (e.g., His-tag) for simplified purification and detection.
Research applications of recombinant DTYMK span enzymology, structural biology, and drug screening. It serves as a tool to study enzyme kinetics, inhibitor interactions, and mutations affecting activity. In cancer biology, DTYMK overexpression is linked to tumor progression, highlighting its potential as a therapeutic target. Additionally, since many viruses rely on host nucleotide pathways for replication, DTYMK inhibitors are explored for antiviral strategies.
Overall, recombinant DTYMK provides a versatile platform for understanding nucleotide metabolism, disease mechanisms, and developing targeted therapies. Its role in DNA synthesis and cellular proliferation continues to drive interdisciplinary studies in biochemistry and medicine.
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