| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | UGT72E2 |
| Uniprot No | Q9LVR1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-481aa |
| 氨基酸序列 | MHITKPHAAMFSSPGMGHVIPVIELGKRLSANNGFHVTVFVLETDAASAQSKFLNSTGVDIVKLPSPDIYGLVDPDDHVVTKIGVIMRAAVPALRSKIAAMHQKPTALIVDLFGTDALCLAKEFNMLSYVFIPTNARFLGVSIYYPNLDKDIKEEHTVQRNPLAIPGCEPVRFEDTLDAYLVPDEPVYRDFVRHGLAYPKADGILVNTWEEMEPKSLKSLLNPKLLGRVARVPVYPIGPLCRPIQSSETDHPVLDWLNEQPNESVLYISFGSGGCLSAKQLTELAWGLEQSQQRFVWVVRPPVDGSCCSEYVSANGGGTEDNTPEYLPEGFVSRTSDRGFVVPSWAPQAEILSHRAVGGFLTHCGWSSTLESVVGGVPMIAWPLFAEQNMNAALLSDELGIAVRLDDPKEDISRWKIEALVRKVMTEKEGEAMRRKVKKLRDSAEMSLSIDGGGLAHESLCRVTKECQRFLERVVDLSRGA |
| 预测分子量 | 56.9 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UGT72E2重组蛋白的3篇代表性文献摘要，供参考：
1. **文献名称**：Functional characterization of recombinant UGT72E2 as a lignin biosynthetic enzyme in Arabidopsis thaliana
**作者**：Lan Wuerfel et al.
**摘要**：研究通过在大肠杆菌中重组表达UGT72E2蛋白，验证其催化松柏醇葡萄糖基化活性，并发现该酶通过调控松柏醇的糖基化平衡，影响拟南芥木质素单体合成途径的代谢流。
2. **文献名称**：Substrate specificity and kinetic analysis of UGT72E2 in phenolic glycosylation
**作者**：Deng Y. et al.
**摘要**：利用纯化的重组UGT72E2蛋白进行酶动力学分析，揭示其对多种酚类底物(如香豆酸、芥子酸)的催化效率差异，提出其在植物防御代谢中的潜在作用。
3. **文献名称**：Heterologous expression and structural insights of UGT72E2 from Populus trichocarpa
**作者**：Chen L. & Machemer K.
**摘要**：首次在毕赤酵母系统中高效表达杨树UGT72E2重组蛋白，结合分子对接实验阐明其活性口袋的关键氨基酸残基，为酶工程改造提供结构基础。
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**说明**：以上文献为示例性内容，实际研究中建议通过PubMed、Web of Science或Google Scholar以“UGT72E2 recombinant protein”为关键词检索最新论文，重点关注其重组表达系统(如E. coli、酵母)、酶学性质及在木质素/类黄酮代谢中的功能验证方向。
UGT72E2 is a member of the uridine diphosphate (UDP)-glycosyltransferase (UGT) family, a group of enzymes widely present in plants that catalyze the transfer of sugar moieties from activated donors to various acceptor molecules. Specifically, UGT72E2 is a plant-derived enzyme initially identified in *Arabidopsis thaliana* and has garnered interest for its role in modifying secondary metabolites, particularly phenylpropanoids. This class of compounds includes lignin precursors, flavonoids, and other phenolic derivatives, which are critical for plant structural integrity, stress responses, and interactions with the environment. UGT72E2 is known to glycosylate monolignols, such as coniferyl alcohol, influencing lignin biosynthesis and potentially altering cell wall composition. Such activity positions it as a target for bioengineering efforts to modify lignin content in crops, which could enhance biomass digestibility for biofuel production or improve agricultural sustainability.
Recombinant UGT72E2 protein is produced via heterologous expression systems, typically in *Escherichia coli* or yeast, to enable large-scale purification and functional characterization. The recombinant form retains the enzymatic activity of its native counterpart, allowing researchers to study substrate specificity, kinetic parameters, and structural features. Its crystal structure and catalytic mechanism have been partially elucidated, revealing conserved motifs critical for UDP-glucose binding and sugar transfer. Beyond lignin metabolism, UGT72E2's ability to glycosylate diverse substrates has implications for synthesizing bioactive glycosides in vitro, with potential applications in pharmaceuticals or nutraceuticals. Studies on UGT72E2 also contribute to understanding the evolutionary diversification of UGTs in tailoring plant specialized metabolism. Overall, this recombinant enzyme serves as a versatile tool for both fundamental research and biotechnological innovation.
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