| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UPP1 |
| Uniprot No | Q16831 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-310aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MAATGANAEK AESHNDCPVR LLNPNIAKMK EDILYHFNLT TSRHNFPALF GDVKFVCVGG SPSRMKAFIR CVGAELGLDC PGRDYPNICA GTDRYAMYKV GPVLSVSHGM GIPSISIMLH ELIKLLYYAR CSNVTIIRIG TSGGIGLEPG TVVITEQAVD TCFKAEFEQI VLGKRVIRKT DLNKKLVQEL LLCSAELSEF TTVVGNTMCT LDFYEGQGRL DGALCSYTEK DKQAYLEAAY AAGVRNIEME SSVFAAMCSA CGLQAAVVCV TLLNRLEGDQ ISSPRNVLSE YQQRPQRLVS YFIKKKLSKA |
| 预测分子量 | 36 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UPP1重组蛋白的3篇参考文献概览：
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1. **文献名称**: *"Cloning, expression, and characterization of recombinant uridine phosphorylase 1 (UPP1) from human liver"*
**作者**: Smith A, et al.
**摘要**: 该研究报道了人源UPP1基因的克隆及其在大肠杆菌中的重组表达，通过纯化获得高活性蛋白，并分析了其酶学特性，为后续抗癌药物代谢研究提供了工具。
2. **文献名称**: *"Structural and functional analysis of UPP1 in pyrimidine salvage pathway: insights from recombinant protein studies"*
**作者**: Tanaka K, et al.
**摘要**: 利用重组UPP1蛋白解析了其晶体结构，揭示了底物结合位点及催化机制，为设计靶向UPP1的抑制剂以增强化疗疗效提供了结构基础。
3. **文献名称**: *"Recombinant UPP1 as a potential biomarker in colorectal cancer: production and clinical validation"*
**作者**: Lee JH, et al.
**摘要**: 研究通过哺乳动物细胞系统表达重组UPP1.发现其在结直肠癌组织中高表达，且血清中UPP1水平与患者预后相关，提示其作为诊断标志物的潜力。
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注：以上文献为示例，实际引用时需根据具体研究内容检索真实发表的论文。可通过PubMed或Web of Science以关键词“UPP1 recombinant protein”进一步查找。
**Background of UPP1 Recombinant Protein**
Uridine phosphorylase 1 (UPP1) is a key enzyme involved in pyrimidine metabolism, catalyzing the reversible phosphorolysis of uridine to uracil and ribose-1-phosphate. This reaction plays a critical role in maintaining nucleotide homeostasis, particularly in tissues with high metabolic activity. UPP1 is also implicated in the activation or detoxification of nucleoside-based chemotherapeutic agents, such as 5-fluorouracil (5-FU), highlighting its clinical relevance in cancer therapy.
The recombinant UPP1 protein is produced through genetic engineering, typically by expressing the *UPP1* gene in heterologous systems like *E. coli* or mammalian cell lines. This allows for large-scale production of the purified enzyme, ensuring consistency and functionality for research or therapeutic applications. Recombinant UPP1 retains the enzymatic activity of its native counterpart, making it a valuable tool for studying uridine metabolism, drug resistance mechanisms, and cellular responses to nucleotide stress.
In cancer biology, UPP1 overexpression has been linked to tumor progression and poor prognosis. Its role in metabolizing uridine supports cancer cell survival under hypoxia or nutrient-deficient conditions by recycling uracil for ATP production. Additionally, UPP1-mediated degradation of uridine influences the efficacy of antimetabolite drugs, underscoring its potential as a biomarker for predicting chemotherapy outcomes.
Beyond oncology, UPP1 is studied in virology due to its interaction with viral replication mechanisms. For instance, it modulates the activity of ribavirin, a nucleoside analog used to treat RNA viruses like hepatitis C. Recombinant UPP1 facilitates structural and functional analyses, aiding in the development of inhibitors to enhance antiviral or anticancer therapies.
Overall, UPP1 recombinant protein serves as a critical resource for dissecting metabolic pathways, advancing drug discovery, and exploring therapeutic strategies targeting nucleotide metabolism in disease.
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