| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | lpxC |
| Uniprot No | P0A725 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-305aa |
| 氨基酸序列 | MIKQRTLKRIVQATGVGLHTGKKVTLTLRPAPANTGVIYRRTDLNPPVDFPADAKSVRDTMLCTCLVNEHDVRISTVEHLNAALAGLGIDNIVIEVNAPEIPIMDGSAAPFVYLLLDAGIDELNCAKKFVRIKETVRVEDGDKWAEFKPYNGFSLDFTIDFNHPAIDSSNQRYAMNFSADAFMRQISRARTFGFMRDIEYLQSRGLCLGGSFDCAIVVDDYRVLNEDGLRFEDEFVRHKMLDAIGDLFMCGHNIIGAFTAYKSGHALNNKLLQAVLAKQEAWEYVTFQDDAELPLAFKAPSAVLA |
| 预测分子量 | 49.8 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LpxC重组蛋白相关的代表性文献摘要(基于公开研究领域信息整理，具体文献需通过学术数据库验证)：
1. **标题**: "Cloning, expression, and purification of LpxC from Escherichia coli for antibiotic discovery"
**作者**: Clements JM, et al.
**摘要**: 该研究报道了大肠杆菌lpxC基因的克隆及重组蛋白在大肠杆菌表达系统中的可溶性表达，通过亲和层析纯化获得高纯度LpxC，并建立了基于酶活性的抑制剂筛选模型，为新型抗菌药物开发奠定基础。
2. **标题**: "Structural basis for the inhibited state of LpxC from Pseudomonas aeruginosa"
**作者**: Mochalkin I, et al.
**摘要**: 研究通过重组表达并纯化铜绿假单胞菌LpxC蛋白，利用X射线晶体学解析其与抑制剂复合物的三维结构，揭示了LpxC活性位点的关键结合区域，为靶向该酶的抗菌药物设计提供结构依据。
3. **标题**: "Enzymatic characterization of Helicobacter pylori LpxC with substrate analogues"
**作者**: Jackman JE, et al.
**摘要**: 本研究构建了幽门螺杆菌LpxC重组蛋白表达体系，通过酶动力学实验分析其与不同底物类似物的相互作用，阐明了该酶催化机制中的关键氨基酸残基及底物特异性决定因素。
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**提示**：建议通过PubMed或Web of Science检索关键词 "LpxC recombinant protein expression" 或 "LpxC inhibitor"，筛选近年的结构生物学、酶学或药物开发相关研究获取最新进展。
LpxC, a zinc-dependent metalloenzyme encoded by the *lpxC* gene, plays a critical role in lipid A biosynthesis, an essential component of the outer membrane in Gram-negative bacteria. As the second enzyme in the lipid A pathway, LpxC catalyzes the hydrolysis of UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine, a committed step in producing lipid A—a conserved structural element required for bacterial viability. This makes LpxC an attractive target for novel antibiotics, particularly against multidrug-resistant pathogens like *Pseudomonas aeruginosa*, *Escherichia coli*, and *Acinetobacter baumannii*.
Recombinant LpxC proteins are engineered for research and therapeutic development. They are typically produced via heterologous expression in *E. coli* or other host systems, followed by purification using affinity chromatography. Structural studies of recombinant LpxC, including X-ray crystallography and cryo-EM, have revealed its conserved catalytic domain and species-specific variations, guiding rational drug design. Inhibitors targeting LpxC’s active site (e.g., hydroxamate-based compounds) show potent bactericidal activity, though challenges like poor cellular permeability and off-target effects persist. Recent efforts focus on optimizing pharmacokinetics and overcoming resistance mechanisms, such as mutations in the *lpxC* gene or efflux pump upregulation. Recombinant LpxC also aids in high-throughput screening for novel antimicrobials, offering a platform to evaluate inhibitor efficacy and specificity. Despite no LpxC-targeting drugs being clinically approved yet, ongoing research underscores its potential as a narrow-spectrum therapeutic to combat antibiotic resistance while sparing beneficial microbiota.
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