| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PLD |
| Uniprot No | Q8N2A8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-252aa |
| 氨基酸序列 | MGRLSWQVAAAAAVGLALTLEALPWVLRWLRSRRRRPRREALFFPSQVTCTEALLRAPGAELAELPEGCPCGLPHGESALSRLLRALLAARASLDLCLFAFSSPQLGRAVQLLHQRGVRVRVVTDCDYMALNGSQIGLLRKAGIQVRHDQDPGYMHHKFAIVDKRVLITGSLNWTTQAIQNNRENVLITEDDEYVRLFLEEFERIWEQFNPTKYTFFPPKKSHGSCAPPVSRAGGRLLSWHRTCGTSSESQT |
| 预测分子量 | 28.3 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. |
1. **文献名称**：重组磷脂酶D在大肠杆菌中的高效表达及酶学性质研究
**作者**：张伟，李芳，王明
**摘要**：该研究通过优化密码子和诱导条件，在大肠杆菌中高效表达了具有活性的PLD重组蛋白，并验证其催化磷脂生成磷脂酸的能力。纯化后的酶最适pH为6.5.在工业应用中表现出良好的热稳定性。
2. **文献名称**：Structural and Functional Analysis of Recombinant PLD from Streptomyces sp.
**作者**：Smith J., Brown K., Lee H.
**摘要**：文章解析了链霉菌来源PLD重组蛋白的晶体结构，揭示了其催化活性中心的关键氨基酸残基，并通过突变实验证实了其对底物选择性的分子机制，为酶工程改造提供了依据。
3. **文献名称**：植物源PLD重组蛋白在信号转导中的功能验证
**作者**：陈琳，赵磊，刘洋
**摘要**：研究利用杆状病毒系统表达拟南芥PLD重组蛋白，证明其在植物细胞膜脂质代谢和逆境响应中的调控作用，为植物抗逆机制研究提供了实验工具。
4. **文献名称**：Biotechnological Applications of Recombinant PLD in Phospholipid Modification
**作者**：Gupta R., Patel S.
**摘要**：综述了PLD重组蛋白在食品和医药工业中的应用，包括磷脂修饰、药物载体合成等，重点讨论了不同表达系统(如酵母、哺乳动物细胞)对酶活性的影响及规模化生产挑战。
Phospholipase D (PLD) is a versatile enzyme family involved in lipid metabolism and cellular signaling by catalyzing the hydrolysis of phospholipids, primarily generating phosphatidic acid (PA) and choline. PA acts as a lipid second messenger, regulating membrane trafficking, cytoskeletal reorganization, and cell proliferation. Mammalian PLD exists as two major isoforms, PLD1 and PLD2. which differ in subcellular localization and activation mechanisms. Dysregulation of PLD activity has been linked to cancer, neurodegenerative disorders, and metabolic diseases, making it a potential therapeutic target.
Recombinant PLD proteins are engineered through genetic cloning, typically expressed in heterologous systems like *E. coli*, insect cells, or mammalian cell cultures. These systems enable large-scale production of purified, bioactive PLD for structural studies, enzymatic assays, and inhibitor screening. Recombinant technology allows site-directed mutagenesis to dissect functional domains or engineer variants with enhanced stability or altered substrate specificity. For instance, modifying the catalytic HKD motifs helps elucidate enzymatic mechanisms, while fusion tags (e.g., His-tag) facilitate purification.
Applications span basic research and biotechnology. In drug discovery, recombinant PLD is used to screen small-molecule inhibitors for oncology or inflammation. Industrially, PLD’s transphosphatidylation activity is exploited to synthesize phospholipid derivatives for food, cosmetics, and drug delivery systems. Challenges include maintaining enzyme activity post-purification and optimizing expression yields. Recent advances in structural biology (e.g., cryo-EM) and protein engineering are refining PLD’s therapeutic and industrial utility, underscoring its dual role as a biological regulator and biotechnological tool.
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