| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TYMS |
| Uniprot No | P04818 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-313aa |
| 氨基酸序列 | PVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGM QARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSL GFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCA WNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHIT GLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGY NPHPTIKMEMAV |
| 预测分子量 | 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TYMS(胸苷酸合成酶)重组蛋白的3篇参考文献示例(注：文献为虚构示例，仅用于格式参考)：
---
1. **文献名称**：Cloning, expression, and purification of recombinant human thymidylate synthase for structural studies
**作者**：Johnson A, et al.
**摘要**：本研究报道了人源TYMS基因在大肠杆菌中的高效表达及重组蛋白的纯化方法，通过X射线晶体学解析了其三维结构，为基于结构的药物设计提供了基础。
2. **文献名称**：Functional characterization of a novel TYMS variant and its role in 5-fluorouracil resistance
**作者**：Lee S, et al.
**摘要**：通过构建重组TYMS蛋白突变体，发现其酶活性的改变与结直肠癌细胞对5-FU化疗耐药性相关，揭示了TYMS调控化疗敏感性的分子机制。
3. **文献名称**：Development of a high-throughput assay using recombinant TYMS for anticancer drug screening
**作者**：Martinez R, et al.
**摘要**：利用重组TYMS蛋白建立了一种新型体外酶活性检测体系，成功筛选出多个小分子抑制剂，为开发新型TYMS靶向抗癌药物提供了技术平台。
---
如需真实文献，建议通过PubMed或Web of Science检索关键词“recombinant thymidylate synthase”获取近年研究。
**Background of TYMS Recombinant Protein**
Thymidylate synthase (TYMS), also known as TS, is a key enzyme involved in DNA synthesis and repair. It catalyzes the reductive methylation of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP), a critical step in the *de novo* biosynthesis of thymidine, an essential nucleotide for DNA replication. Due to its pivotal role in cell proliferation, TYMS is a well-studied target in cancer therapeutics, particularly for antimetabolite drugs like 5-fluorouracil (5-FU) and its derivatives, which inhibit TYMS activity to impede tumor growth.
The recombinant TYMS protein is engineered using molecular cloning techniques, typically expressed in bacterial (e.g., *E. coli*) or mammalian cell systems. This recombinant form retains the enzymatic activity of the native protein, enabling researchers to study its structure, function, and interactions with inhibitors in vitro. The protein is often purified via affinity chromatography, leveraging tags such as His-tag or GST-tag for efficient isolation.
Research on TYMS recombinant protein has provided insights into enzyme kinetics, drug resistance mechanisms, and structural biology. For instance, mutations in TYMS linked to reduced drug binding are investigated to understand chemoresistance in cancers. Additionally, structural studies using X-ray crystallography or cryo-EM have revealed conformational changes during catalysis, aiding in the design of next-generation inhibitors.
Beyond oncology, TYMS is studied in infectious diseases, as pathogens like *Plasmodium* (malaria) and some viruses depend on thymidine synthesis for replication. Recombinant TYMS thus serves as a tool for developing antimicrobial agents. Overall, TYMS recombinant protein is indispensable for advancing both basic science and therapeutic innovation in biomedicine.
×
