| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TPMT |
| Uniprot No | P51580 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 4-244aa |
| 氨基酸序列 | TRTSLDIEEYSDTEVQKNQVLTLEEWQDKWVNGKTAFHQEQGHQLLKKHLDTFLKGKSGLRVFFPLCGKAVEMKWFADRGHSVVGVEISELGIQEFFTEQNLSYSEEPITEIPGTKVFKSSSGNISLYCCSIFDLPRTNIGKFDMIWDRGALVAINPGDRKCYADTMFSLLGKKFQYLLCVLSYDPTKHPGPPFYVPHAEIERLFGKICNIRCLEKVDAFEERHKSWGIDCLFEKLYLLTE |
| 预测分子量 | 54.7kDa |
| 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TPMT重组蛋白的3篇示例参考文献(注：以下文献为示例，非真实存在)：
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1. **标题**：*Expression and Functional Characterization of Recombinant Human TPMT in Escherichia coli*
**作者**：Smith J.R., et al.
**摘要**：本研究通过在大肠杆菌中表达重组人源TPMT蛋白，优化了表达和纯化条件。结果显示，重组TPMT具有与天然酶相似的催化活性，并成功用于评估硫嘌呤类药物的甲基化效率，为体外药物代谢研究提供了可靠工具。
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2. **标题**：*Kinetic Analysis of TPMT Genetic Variants Using Recombinant Protein Models*
**作者**：Chen L., Wang H.
**摘要**：通过构建TPMT常见基因突变体(如TPMT*2、TPMT*3A)的重组蛋白，分析了不同变异体的酶动力学参数。研究发现，突变体活性显著降低，解释了携带这些变异的患者对硫嘌呤类药物敏感性升高的机制。
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3. **标题**：*Comparative Study of TPMT Production in Yeast and Mammalian Expression Systems*
**作者**：Gomez M., et al.
**摘要**：对比了酵母和哺乳动物细胞表达系统生产重组TPMT的效率和功能。结果表明，哺乳动物系统表达的TPMT具有更接近天然酶的翻译后修饰，但其产量较低;酵母系统则更适合大规模制备活性重组蛋白。
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如需真实文献，建议通过PubMed或Google Scholar检索关键词“TPMT recombinant protein”“thiopurine methyltransferase expression”等。
**Background of TPMT Recombinant Protein**
Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme critical in the metabolism of thiopurine drugs, such as 6-mercaptopurine (6-MP), 6-thioguanine (6-TG), and azathioprine (AZA). These immunosuppressive and chemotherapeutic agents are widely used to treat conditions like acute lymphoblastic leukemia, autoimmune disorders, and organ transplant rejection. TPMT catalyzes the S-methylation of thiopurines, converting them into inactive metabolites, thereby regulating their therapeutic efficacy and toxicity. Genetic polymorphisms in the *TPMT* gene significantly influence enzyme activity, leading to interindividual variability in drug response. Approximately 0.3–0.5% of populations inherit two nonfunctional alleles (homozygous deficient), resulting in undetectable TPMT activity and a high risk of severe, potentially fatal myelosuppression upon thiopurine exposure.
Recombinant TPMT protein is produced via genetic engineering techniques, typically expressed in bacterial, yeast, or mammalian cell systems. This engineered protein retains the enzymatic activity of native TPMT and serves as a standardized tool for studying enzyme kinetics, substrate specificity, and the functional impact of genetic variants. Its applications span pharmacogenetic research, clinical diagnostics, and drug development. For instance, recombinant TPMT is used in *in vitro* assays to assess patient-specific TPMT activity, guiding personalized dosing to minimize adverse effects. It also aids in developing high-throughput screening kits for detecting TPMT polymorphisms, enabling pre-treatment risk stratification.
Furthermore, recombinant TPMT facilitates mechanistic studies on drug-enzyme interactions and supports the design of novel therapeutic strategies. By elucidating structure-function relationships, researchers aim to optimize thiopurine therapies and explore interventions for patients with TPMT deficiency. Overall, TPMT recombinant protein plays a pivotal role in advancing precision medicine and improving outcomes in thiopurine-treated populations.
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