| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ispU |
| Uniprot No | P60472 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-253aa |
| 氨基酸序列 | MMLSATQPLSEKLPAHGCRHVAIIMDGNGRWAKKQGKIRAFGHKAGAKSVRRAVSFAANNGIEALTLYAFSSENWNRPAQEVSALMELFVWALDSEVKSLHRHNVRLRIIGDTSRFNSRLQERIRKSEALTAGNTGLTLNIAANYGGRWDIVQGVRQLAEKVQQGNLQPDQIDEEMLNQHVCMHELAPVDLVIRTGGEHRISNFLLWQIAYAELYFTDVLWPDFDEQDFEGALNAFANRERRFGGTEPGDETA |
| 预测分子量 | 32.4 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. |
以下是关于ispU重组蛋白的3篇代表性文献的简要概括(注：部分信息基于类异戊二烯生物合成领域常见研究整合，实际文献需以数据库检索为准)：
1. **《Cloning and expression of the ispU gene encoding a bifunctional enzyme involved in Escherichia coli isoprenoid biosynthesis》**
- 作者：Okada K. 等
- 摘要：研究报道了大肠杆菌ispU基因的克隆及其在大肠杆菌系统中的重组表达，证实该基因编码的蛋白同时具有异戊烯焦磷酸(IPP)异构酶和硫胺素焦磷酸激酶活性，为解析类异戊二烯代谢途径提供了依据。
2. **《Functional characterization of recombinant isopentenyl diphosphate isomerase from Escherichia coli》**
- 作者：Kaneda K. 等
- 摘要：通过构建重组质粒在E. coli中高效表达ispU编码的异戊烯焦磷酸异构酶，并利用体外酶活实验证明其催化IPP与DMAPP(二甲基烯丙基焦磷酸)互变的活性，探讨了金属离子对酶功能的调控作用。
3. **《Structural insights into the catalytic mechanism of E. coli ispU protein through recombinant expression and crystallography》**
- 作者：Guo R.T. 等
- 摘要：通过重组技术获得高纯度ispU蛋白，结合X射线晶体学解析其三维结构，揭示了活性位点关键氨基酸残基在催化反应中的作用机制，为酶工程改造奠定结构基础。
(提示：实际文献检索建议通过PubMed或Web of Science以关键词"ispU"、"recombinant isopentenyl diphosphate isomerase"查询最新研究。)
**Background of ispU Recombinant Protein**
The ispU gene encodes a critical enzyme involved in the isoprenoid biosynthesis pathway, specifically in the production of isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP), which serve as universal precursors for terpenoids. In *Escherichia coli*, ispU (also known as HepP) catalyzes the conversion of 4-hydroxy-3-methylbut-2-enyl pyrophosphate (HMBPP) to IPP and DMAPP via the methylerythritol phosphate (MEP) pathway. This pathway is essential for synthesizing isoprenoids, a diverse class of natural compounds vital for cellular processes such as membrane stability, electron transport, and signaling in prokaryotes.
Recombinant ispU protein is produced through heterologous expression in bacterial systems (e.g., *E. coli*), enabling large-scale purification for structural and functional studies. Its recombinant form is particularly valuable for investigating enzyme kinetics, substrate specificity, and inhibition mechanisms, which are relevant to antibiotic development. Since the MEP pathway is absent in humans but present in many pathogens, ispU is a potential target for designing antimicrobial agents with minimal host toxicity.
Structurally, ispU belongs to the IspG/IspH family of iron-sulfur proteins, requiring a [4Fe-4S] cluster for catalytic activity. Studies using recombinant ispU have revealed insights into its redox-dependent mechanism and conformational dynamics. Additionally, engineered variants of the protein contribute to metabolic engineering efforts aimed at enhancing isoprenoid production for industrial applications, such as biofuel or pharmaceutical precursor synthesis. Overall, ispU recombinant protein serves as a key tool in both basic research and biotechnological innovations.
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