| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | luxS |
| Uniprot No | C4ZYT7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-171aa |
| 氨基酸序列 | MPLLDSFTVDHTRMEAPAVRVAKTMNTPHGDAITVFDLRFCVPNKEVMPERGIHTLEHLFAGFMRNHLNGNGVEIIDISPMGCRTGFYMSLIGTPDEQRVADAWKAAMEDVLKVQDQNQIPELNVYQCGTYQMHSLQEAQDIARSILERDVRINSNEELALPKEKLQELHI |
| 预测分子量 | 26.9 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3-4篇关于 **luxS重组蛋白** 的参考文献摘要整理：
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1. **标题**：*"Quorum sensing in Vibrio harveyi: LuxS directs synthesis of autoinducer 2 (AI-2)"*
**作者**：Bassler, B.L., et al.
**摘要**：研究证明luxS基因在哈维氏弧菌中调控AI-2的合成，重组LuxS蛋白通过催化S-腺苷甲硫氨酸代谢产生AI-2.揭示其在细菌群体感应中的核心作用。
2. **标题**：*"The LuxS family of bacterial autoinducers: Biosynthesis of a novel quorum-sensing signal molecule"*
**作者**：Schauder, S., et al.
**摘要**：通过重组表达LuxS蛋白，解析其催化底物转化为AI-2的酶活性机制，提出AI-2作为跨物种群体感应信号分子的普遍性功能。
3. **标题**：*"Recombinant LuxS protein characterization and its role in biofilm formation of Streptococcus mutans"*
**作者**：Li, Y., et al.
**摘要**：克隆并纯化变形链球菌luxS重组蛋白，证实其缺失会显著抑制细菌生物膜形成及酸耐受性，为口腔致病机制研究提供依据。
4. **标题**：*"Expression and purification of functional LuxS enzyme from Escherichia coli for metabolic engineering applications"*
**作者**：Wu, J., et al.
**摘要**：优化大肠杆菌中重组LuxS蛋白的高效表达与纯化工艺，验证其催化活性在合成生物学及代谢通路改造中的潜在应用价值。
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以上文献涵盖luxS重组蛋白的分子机制、群体感应功能及生物技术应用，可根据研究需求进一步查阅原文。
LuxS is a conserved enzyme found in diverse bacterial species, playing a dual role in microbial metabolism and quorum sensing (QS). It catalyzes the cleavage of S-ribosylhomocysteine to produce homocysteine and autoinducer-2 (AI-2), a signaling molecule central to interspecies communication. Discovered in the 1990s during studies on Vibrio harveyi bioluminescence, LuxS links metabolic processes with population-dependent gene regulation. Its AI-2 product acts as a "universal" signal, enabling bacteria to sense and coordinate behaviors – such as biofilm formation, virulence, and antibiotic resistance – across species boundaries.
The interest in recombinant LuxS protein stems from its potential applications in studying bacterial social behaviors and developing anti-infective strategies. By producing LuxS through genetic engineering (typically in E. coli expression systems), researchers can purify the enzyme for structural analysis, biochemical characterization, and interference studies. Crystal structures reveal LuxS's TIM barrel fold and metal-binding sites critical for its catalytic activity.
Key research focuses include understanding how LuxS-mediated signaling intersects with central metabolism (via the activated methyl cycle), deciphering AI-2's structural variations among species, and exploring therapeutic interventions. Recombinant LuxS enables experiments to differentiate its metabolic role from its signaling function – a crucial distinction given that some observed phenotypes may stem from metabolic disruption rather than quorum sensing impairment.
Challenges persist in standardizing AI-2 detection methods and interpreting LuxS's evolutionary conservation versus functional diversity across pathogens. Nevertheless, LuxS recombinant protein remains a vital tool for probing microbial ecology, host-microbe interactions, and developing QS-inhibiting compounds. Recent applications extend to synthetic biology for engineering microbial consortia and biotechnology processes requiring population-level control.
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