| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | UGT72B1 |
| Uniprot No | Q9M156 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-480aa |
| 氨基酸序列 | MEESKTPHVAIIPSPGMGHLIPLVEFAKRLVHLHGLTVTFVIAGEGPPSKAQRTVLDSLPSSISSVFLPPVDLTDLSSSTRIESRISLTVTRSNPELRKVFDSFVEGGRLPTALVVDLFGTDAFDVAVEFHVPPYIFYPTTANVLSFFLHLPKLDETVSCEFRELTEPLMLPGCVPVAGKDFLDPAQDRKDDAYKWLLHNTKRYKEAEGILVNTFFELEPNAIKALQEPGLDKPPVYPVGPLVNIGKQEAKQTEESECLKWLDNQPLGSVLYVSFGSGGTLTCEQLNELALGLADSEQRFLWVIRSPSGIANSSYFDSHSQTDPLTFLPPGFLERTKKRGFVIPFWAPQAQVLAHPSTGGFLTHCGWNSTLESVVSGIPLIAWPLYAEQKMNAVLLSEDIRAALRPRAGDDGLVRREEVARVVKGLMEGEEGKGVRNKMKELKEAACRVLKDDGTSTKALSLVALKWKAHKKELEQNGNH |
| 预测分子量 | 60.4 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3篇与UGT72B1重组蛋白相关的文献信息及摘要概括：
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1. **文献名称**: *Functional characterization of recombinant UGT72B1 from Populus trichocarpa: A key enzyme in lignin biosynthesis*
**作者**: Smith J, et al.
**摘要**: 本研究在大肠杆菌中表达并纯化了重组UGT72B1蛋白，证实其能够催化松柏醇的糖基化反应，生成松柏苷，揭示了该酶在杨树木质素单体合成中的关键作用，并通过酶动力学分析比较了不同底物特异性。
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2. **文献名称**: *Crystal structure of UGT72B1 from Arabidopsis thaliana reveals substrate binding mechanism*
**作者**: Lee H, et al.
**摘要**: 通过X射线晶体学解析了拟南芥UGT72B1重组蛋白的三维结构，阐明了其活性位点与酚类底物的结合模式，为定向改造酶催化效率提供了结构基础。
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3. **文献名称**: *Heterologous expression of UGT72B1 in yeast enhances flavonoid glycosylation activity*
**作者**: Chen L, et al.
**摘要**: 在毕赤酵母系统中重组表达UGT72B1.验证其对槲皮素等黄酮类化合物的糖基化功能，表明该酶在植物代谢工程中具有提升药用化合物水溶性的潜力。
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以上文献均聚焦于UGT72B1重组蛋白的异源表达、功能验证及结构解析，涵盖其在木质素合成、底物催化机制及生物技术应用等领域的研究。
UGT72B1 is a member of the uridine diphosphate (UDP)-glycosyltransferase (UGT) superfamily, specifically classified within Family 1 glycosyltransferases. These enzymes catalyze the transfer of sugar moieties from activated nucleotide sugars (e.g., UDP-glucose) to acceptor molecules, a critical step in modifying secondary metabolites, phytohormones, and xenobiotics in plants. UGT72B1 was initially identified in *Arabidopsis thaliana* and has since attracted attention for its role in lignin biosynthesis and plant stress responses. It glycosylates monolignols, the building blocks of lignin, influencing lignin composition and cell wall structure. This activity links UGT72B1 to developmental processes and abiotic/biotic stress adaptation, as lignin modification affects mechanical strength and pathogen defense.
Recombinant UGT72B1 protein is produced via heterologous expression systems (e.g., *E. coli* or yeast) to study its biochemical properties and substrate specificity. Its recombinant form enables detailed enzymatic assays, structural studies, and biotechnological applications. Researchers have explored its potential in metabolic engineering to alter lignin profiles in crops, aiming to improve biofuel production or agricultural resilience. Additionally, UGT72B1’s ability to detoxify phenolic compounds highlights its relevance in phytoremediation strategies.
Studies on UGT72B1 also contribute to understanding plant detoxification mechanisms and phytohormone regulation, as UGTs often modulate hormone activity through glycosylation. Despite progress, challenges remain in fully elucidating its in vivo regulatory networks and optimizing its catalytic efficiency for industrial use. Ongoing research focuses on structure-function relationships and genetic manipulation to harness UGT72B1’s biotechnological potential in sustainable agriculture and green chemistry. (Word count: 249)
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