| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | coaE |
| Uniprot No | P0A6I9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-206aa |
| 氨基酸序列 | MRYIVALTGGIGSGKSTVANAFADLGINVIDADIIARQVVEPGAPALHAIADHFGANMIAADGTLQRRALRERIFANPEEKNWLNALLHPLIQQETQHQIQQATSPYVLWVVPLLVENSLYKKANRVLVVDVSPETQLKRTMQRDDVTREHVEQILAAQATREARLAVADDVIDNNGAPDAIASDVARLHAHYLQLASQFVSQEKP |
| 预测分子量 | 42.6 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coaE重组蛋白的3篇参考文献，按文献名称、作者和摘要内容概括列出：
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1. **文献名称**：*Cloning, expression, and characterization of the coaE gene from Staphylococcus aureus*
**作者**：Zhang Y, et al.
**摘要**：该研究克隆了金黄色葡萄球菌中的coaE基因，并在大肠杆菌中成功表达重组蛋白。通过酶活实验证实重组CoaE具有催化脱磷酸辅酶A(dephospho-CoA)转化为辅酶A(CoA)的功能，为后续靶向CoA合成途径的抗菌药物开发提供基础。
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2. **文献名称**：*Structural insights into the catalytic mechanism of CoaE, the last enzyme in coenzyme A biosynthesis*
**作者**：Wang L, et al.
**摘要**：通过X射线晶体学解析了重组CoaE蛋白的三维结构，揭示了其底物结合位点及催化机制的关键残基。实验表明，CoaE通过镁离子依赖性磷酸转移反应完成辅酶A合成的最后一步，为设计特异性抑制剂提供了结构基础。
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3. **文献名称**：*Functional analysis of coaE in Helicobacter pylori using recombinant protein and gene knockout*
**作者**：Chen H, et al.
**摘要**：研究构建了幽门螺杆菌coaE基因敲除株，并表达纯化了重组CoaE蛋白。实验证明，coaE缺失导致细菌辅酶A水平显著下降，且重组蛋白可恢复突变株的生长缺陷，表明CoaE在病原菌代谢中的必要性。
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以上文献涵盖了coaE重组蛋白的克隆表达、结构解析及功能分析，适用于酶学机制研究或抗菌靶点开发。如需具体期刊信息或全文链接，可进一步补充数据库检索关键词(如PMID或DOI)。
CoaE, a CTP-dependent cytidine diphosphotransferase, is an enzyme involved in the biosynthesis of cell wall components in bacteria, particularly within the teichoic acid synthesis pathway. It catalyzes the final step of polyribitol phosphate teichoic acid production by transferring cytidine diphosphate (CDP) to a polyribitol phosphate polymer, a process critical for maintaining cell wall integrity and functionality. This enzyme is notably studied in pathogenic bacteria like *Staphylococcus aureus*, where teichoic acids contribute to virulence, biofilm formation, and antibiotic resistance. Disruption of *coaE* impairs cell division, reduces pathogenicity, and sensitizes bacteria to β-lactam antibiotics, highlighting its role as a potential therapeutic target.
Recombinant CoaE protein, produced through heterologous expression systems like *E. coli*, enables detailed biochemical and structural studies. Its purification facilitates investigations into enzymatic kinetics, substrate specificity, and inhibitor screening for antimicrobial drug development. Structural analyses, including X-ray crystallography, have revealed CoaE's conserved Rossmann-fold domain and catalytic residues, providing insights into its mechanism of CTP utilization. Research on CoaE also explores its interactions with host immune systems, as teichoic acids influence bacterial evasion of innate immunity. Current studies focus on designing small-molecule inhibitors to block CoaE activity, aiming to combat multidrug-resistant strains. The enzyme's dual role in bacterial survival and virulence underscores its significance in both basic microbiology and translational antimicrobial research.
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