| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | dTMP |
| 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 | MAARRGALIVLEGVDRAGKSTQSRKLVEALCAAGHRAELLRFPERSTEIGKLLSSYLQKKSDVEDHSVHLLFSANRWEQVPLIKEKLSQGVTLVVDRYAFSGVAFTGAKENFSLDWCKQPDVGLPKPDLVLFLQLQLADAAKRGAFGHERYENGAFQERALRCFHQLMKDTTLNWKMVDASKSIEAVHEDIRVLSEDAIRTATEKPLGELWK |
| 预测分子量 | 50.7 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3篇关于dTMP相关重组蛋白研究的模拟参考文献示例(非真实文献，仅供格式参考)：
1. **《Recombinant thymidylate kinase from Escherichia coli: kinetic characterization and structural insights》**
- 作者：Smith J, et al.
- 摘要：研究通过重组技术在大肠杆菌中高效表达胸苷酸激酶(TMK)，分析其酶动力学特性及晶体结构，为开发核苷类似物抗病毒药物提供依据。
2. **《Functional expression of human thymidylate synthase in yeast for anticancer drug screening》**
- 作者：Chen L, et al.
- 摘要：构建人源胸苷酸合成酶(TS)重组酵母表达系统，验证其催化dUMP生成dTMP的活性，并用于高通量筛选TS抑制剂类抗癌化合物。
3. **《Engineering thermostable dTMP phosphorylase for industrial nucleotide biosynthesis》**
- 作者：Wang Y, et al.
- 摘要：通过定向进化技术改造重组dTMP磷酸化酶，提高其热稳定性和催化效率，优化酶法合成dTMP的工业化生产工艺。
4. **《A novel dTMP-binding protein in bacteriophage DNA replication: purification and functional analysis》**
- 作者：Kim S, et al.
- 摘要：鉴定并纯化噬菌体来源的新型dTMP结合重组蛋白，揭示其在病毒DNA复制中调控dTMP代谢的分子机制。
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注：以上文献为示例，实际研究中建议通过PubMed/Google Scholar检索关键词如 **"recombinant thymidylate kinase/synthase"** 或 **"dTMP-binding protein expression"** 获取真实文献。
Thymidine monophosphate (dTMP), a critical precursor for DNA synthesis, is a pyrimidine nucleotide required for cell proliferation and genome stability. Its biosynthesis occurs primarily via the *de novo* pathway, where thymidylate synthase (TYMS) catalyzes the methylation of deoxyuridine monophosphate (dUMP) to dTMP, a rate-limiting step dependent on folate metabolism. Alternatively, salvage pathways recycle thymidine into dTMP via thymidine kinase. Dysregulation of dTMP synthesis disrupts DNA replication and repair, linking it to diseases like cancer and genetic disorders.
Recombinant dTMP-related proteins, such as TYMS or enzymes in folate metabolism (e.g., dihydrofolate reductase, DHFR), are engineered using heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells*) for research and therapeutic applications. These proteins enable mechanistic studies of nucleotide metabolism, drug-target interactions, and enzyme kinetics. For instance, recombinant TYMS is pivotal in studying 5-fluorouracil (5-FU) resistance in cancer, as 5-FU targets TYMS to inhibit dTMP production. Similarly, recombinant DHFR is used to screen antifolate drugs like methotrexate.
The demand for high-purity, scalable dTMP-associated proteins has driven advancements in recombinant technology, including codon optimization, fusion tags, and purification strategies. These proteins also support diagnostic tool development, such as enzyme activity assays for folate deficiency or chemotherapeutic efficacy monitoring. Furthermore, engineered variants with altered catalytic properties or stability are explored for industrial biocatalysis or gene therapy. Overall, recombinant dTMP-related proteins serve as indispensable tools in both basic science and translational medicine, bridging gaps between metabolic pathway elucidation and clinical innovation.
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