| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UGT1A8 |
| Uniprot No | Q9HAW9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-530aa |
| 氨基酸序列 | GKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEVSWQLGKSLNCTVKTYSTSYTLEDLDREFMDFADAQWKAQVRSLFSLFLSSSNGFFNLFFSHCRSLFNDRKLVEYLKESSFDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEEGAQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIASEILQTPVTAYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH |
| 预测分子量 | 59.9 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UGT1A8重组蛋白的3篇参考文献，包含文献名称、作者及简要摘要内容：
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1. **文献名称**: "Functional characterization of human UDP-glucuronosyltransferase 1A8 (UGT1A8) in the metabolism of flavonoids"
**作者**: Lu Y, et al.
**摘要**: 研究利用重组表达的UGT1A8蛋白(HEK293细胞系统)分析其对黄酮类化合物的葡萄糖醛酸化活性，发现UGT1A8对槲皮素和山柰酚具有高催化效率，揭示了其在植物化学物代谢中的作用。
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2. **文献名称**: "Substrate specificity and expression of recombinant UGT1A8 in human intestinal tissues"
**作者**: Strassburg CP, et al.
**摘要**: 通过昆虫细胞(Sf9)系统重组表达UGT1A8.结合肠道组织样本分析，证实UGT1A8在肠道中高表达，并优先代谢酚类化合物及部分药物(如SN-38)，强调了其在首过代谢中的重要性。
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3. **文献名称**: "Comparative analysis of UGT1A8 and UGT1A10 in the glucuronidation of mycotoxins"
**作者**: Miley MJ, et al.
**摘要**: 研究比较了UGT1A8与UGT1A10重组蛋白(均通过杆状病毒系统表达)对多种霉菌毒素的代谢差异，发现UGT1A8对脱氧雪腐镰刀菌烯醇(DON)的葡萄糖醛酸化活性显著高于其他亚型。
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注：以上文献信息为示例性内容，实际引用时需核对具体文献来源及准确性。
UGT1A8. a member of the uridine diphosphate (UDP)-glucuronosyltransferase (UGT) 1A family, is a phase II metabolic enzyme that catalyzes the glucuronidation of endogenous compounds (e.g., steroids, bile acids) and xenobiotics (e.g., drugs, environmental toxins). This post-translational modification enhances the solubility of hydrophobic substrates, facilitating their excretion. UGT1A8 is primarily expressed in the gastrointestinal tract, including the small intestine and colon, distinguishing it from hepatic UGT isoforms. Its localization suggests a role in first-pass metabolism and gut-specific detoxification pathways.
Recombinant UGT1A8 protein is engineered using heterologous expression systems (e.g., baculovirus-insect cells, mammalian cells) to study its enzymatic activity, substrate specificity, and interactions with inhibitors or inducers. Unlike tissue-derived enzymes, recombinant forms offer purity, scalability, and reduced batch variability, making them critical tools for *in vitro* drug metabolism studies. Researchers utilize these proteins to predict pharmacokinetics, assess drug-drug interactions, and explore interindividual variability linked to genetic polymorphisms (e.g., UGT1A8*2 allele).
UGT1A8’s substrates include flavonoids, NSAIDs, and anticancer agents, highlighting its relevance in dietary, therapeutic, and toxicological contexts. Dysregulation or genetic variants of UGT1A8 may influence drug efficacy, toxicity, or susceptibility to diseases like colorectal cancer. Recent studies also explore its role in the metabolism of microbiome-derived metabolites, linking it to gut-liver axis homeostasis.
The production of recombinant UGT1A8. often coupled with advanced analytical techniques (HPLC-MS/MS), enables high-throughput screening in drug development. Its application extends to personalized medicine, where genetic profiling of UGT1A8 variants helps tailor dosing regimens. Despite progress, challenges remain in mimicking native tissue microenvironments *in vitro*, necessitating further research on enzyme kinetics and tissue-specific regulation. Overall, UGT1A8 recombinant protein serves as a vital resource for understanding detoxification mechanisms and optimizing therapeutic interventions.
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