| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UGT1A7 |
| Uniprot No | Q9HAW7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-530aa |
| 氨基酸序列 | GKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEVSWQLGRSLNCTVKTYSTSYTLEDQDREFMVFADARWTAPLRSAFSLLTSSSNGIFDLFFSNCRSLFNDRKLVEYLKESCFDAVFLDPFDACGLIVAKYFSLPSVVFARGIFCHYLEEGAQCPAPLSYVPRLLLGFSDAMTFKERVWNHIMHLEEHLFCPYFFKNVLEIASEILQTPVTAYDLYSHTSIWLLRTDFVLEYPKPVMPNMIFIGGINCHQGKPVPMEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH |
| 预测分子量 | 60.0 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UGT1A7重组蛋白的3篇示例参考文献(内容为模拟概括，建议通过学术数据库核实具体文献)：
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1. **文献名称**: *"Functional Characterization of Recombinant Human UGT1A7 Expressed in Baculovirus-Infected Insect Cells"*
**作者**: Strassburg CP, et al.
**摘要**: 研究利用杆状病毒-昆虫细胞系统表达重组UGT1A7.分析其催化活性及底物特异性，发现其对多种酚类化合物和致癌物(如苯并芘代谢物)具有显著葡萄糖醛酸化能力。
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2. **文献名称**: *"Polymorphic Variants of UGT1A7: Recombinant Protein Expression and Impact on Enzyme Kinetics"*
**作者**: Guillemette C, et al.
**摘要**: 通过构建UGT1A7基因多态性突变体重组蛋白，比较不同突变体(如N129K/R131K)对酶动力学参数(Km、Vmax)的影响，揭示其与个体代谢差异的潜在关联。
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3. **文献名称**: *"Role of UGT1A7 in Drug Metabolism: Studies with Recombinant Enzymes and Human Liver Microsomes"*
**作者**: Tukey RH, et al.
**摘要**: 利用重组UGT1A7蛋白和肝微粒体样本，评估其在药物(如伊立替康)代谢中的作用，证实其在肝脏外组织(如胃肠道)中的解毒功能及临床药物反应个体差异机制。
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**建议检索方法**：
- 使用PubMed或Google Scholar，以关键词“recombinant UGT1A7”、“expression”、“kinetics”、“polymorphism”组合搜索。
- 关注期刊如*Drug Metabolism and Disposition*或*Pharmacogenetics*中的相关研究。
UGT1A7. a member of the uridine diphosphate glucuronosyltransferase (UGT) 1A family, is a phase II metabolic enzyme involved in the detoxification and elimination of endogenous compounds, environmental toxins, and therapeutic drugs. This enzyme catalyzes the conjugation of glucuronic acid to lipophilic substrates, enhancing their water solubility for excretion. UGT1A7 is primarily expressed in extrahepatic tissues, including the gastrointestinal tract, where it plays a critical role in metabolizing carcinogens, dietary mutagens, and pharmaceuticals. Its substrates include phenolic compounds, heterocyclic amines, and certain drugs like irinotecan, a chemotherapeutic agent whose active metabolite (SN-38) is inactivated by glucuronidation.
Recombinant UGT1A7 protein is produced using heterologous expression systems, such as baculovirus-infected insect cells or mammalian cell lines, to study its enzymatic activity, substrate specificity, and genetic polymorphisms. Unlike hepatic UGT isoforms, UGT1A7 exhibits unique tissue-specific regulation and genetic variability. Over 30 UGT1A7 variants have been identified, with some (e.g., UGT1A7*3) linked to reduced enzymatic activity, influencing individual susceptibility to cancers (e.g., colorectal, pancreatic) and drug toxicity. Research on recombinant UGT1A7 aids in understanding interindividual differences in drug metabolism, toxicant bioactivation, and disease mechanisms. It also serves as a tool for screening drug candidates, assessing drug-drug interactions, and developing personalized therapeutic strategies. Structural studies of the recombinant protein further elucidate substrate-binding domains and catalytic mechanisms, providing insights for enzyme engineering or inhibitor design. Despite its physiological relevance, UGT1A7's low hepatic expression underscores the importance of recombinant models in dissecting its biological roles beyond in vivo limitations.
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