| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | EHT1 |
| Uniprot No | P38295 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-451aa |
| 氨基酸序列 | MSEVSKWPAINPFHWGYNGTVSHIVGENGSIKLHLKDNKEQVDFDEFANKYVPTLKNGAQFKLSPYLFTGILQTLYLGAADFSKKFPVFYGREIVKFSDGGVCTADWLIDSWKKDYEFDQSTTSFDKKKFDKDEKATHPEGWPRLQPRTRYLKDNELEELREVDLPLVVILHGLAGGSHEPIIRSLAENLSRSGRFQVVVLNTRGCARSKITTRNLFTAYHTMDIREFLQREKQRHPDRKLYAVGCSFGATMLANYLGEEGDKSPLSAAATLCNPWDLLLSAIRMSQDWWSRTLFSKNIAQFLTRTVQVNMGELGVPNGSLPDHPPTVKNPSFYMFTPENLIKAKSFKSTREFDEVYTAPALGFPNAMEYYKAASSINRVDTIRVPTLVINSRDDPVVGPDQPYSIVEKNPRILYCRTDLGGHLAYLDKDNNSWATKAIAEFFTKFDELVV |
| 预测分子量 | 57.3 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. |
以下是关于EHT1重组蛋白的3篇参考文献示例(注：文献信息为模拟虚构，仅供格式参考)：
1. **标题**：*Functional characterization of recombinant EHT1 in phospholipid biosynthesis*
**作者**：Smith J, et al.
**摘要**：研究利用大肠杆菌表达系统重组表达酿酒酵母EHT1蛋白，证实其作为乙醇胺磷酸转移酶的功能，参与磷脂酰乙醇胺合成，并分析了酶动力学参数。
2. **标题**：*Structural insights into EHT1-mediated lipid metabolism*
**作者**：Li X, Wang Y.
**摘要**：通过X射线晶体学解析EHT1重组蛋白的三维结构，揭示其底物结合域及催化机制，为靶向脂代谢疾病的药物设计提供依据。
3. **标题**：*Heterologous expression of EHT1 in Pichia pastoris and its application in metabolic engineering*
**作者**：Chen R, et al.
**摘要**：在毕赤酵母中高效表达EHT1重组蛋白，优化培养条件提高酶活，应用于合成生物学中磷脂代谢通路的重构与优化。
(注：实际文献需通过PubMed、Google Scholar等平台以关键词"EHT1 recombinant protein"或"ethanolaminephosphotransferase EHT1"检索获取。)
**Background of EHT1 Recombinant Protein**
EHT1 (Ethanolaminephosphotransferase 1) is a key enzyme involved in phospholipid biosynthesis, specifically catalyzing the final step of phosphatidylethanolamine (PE) synthesis via the Kennedy pathway. PE is a critical component of cellular membranes, influencing membrane structure, curvature, and function. EHT1 transfers ethanolamine phosphate from CDP-ethanolamine to diacylglycerol (DAG), generating PE. This enzyme is evolutionarily conserved across eukaryotes, with homologs identified in yeast, plants, and mammals, highlighting its essential role in lipid metabolism.
Recombinant EHT1 protein is produced using heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to enable functional and structural studies. Its recombinant form allows researchers to explore enzymatic kinetics, substrate specificity, and regulatory mechanisms in vitro. EHT1 activity is linked to cellular processes such as membrane biogenesis, stress responses, and autophagy. Dysregulation of PE synthesis has been implicated in metabolic disorders, neurodegenerative diseases, and cancer, making EHT1 a potential therapeutic target.
Recent studies utilize recombinant EHT1 to investigate lipid homeostasis, drug interactions, and genetic mutations affecting enzyme activity. Advanced techniques like X-ray crystallography or cryo-EM rely on high-purity recombinant protein to resolve EHT1’s 3D structure, aiding in rational drug design. Additionally, plant EHT1 homologs are studied for their roles in abiotic stress tolerance, offering biotechnological applications in crop improvement.
In summary, EHT1 recombinant protein serves as a vital tool for dissecting lipid biosynthesis pathways, disease mechanisms, and biotechnological innovations, bridging fundamental biology with translational research.
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