| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | yegS |
| Uniprot No | P76407 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-299aa |
| 氨基酸序列 | MAEFPASLLILNGKSTDNLPLREAIMLLREEGMTIHVRVTWEKGDAARYVEEARKFGVATVIAGGGDGTINEVSTALIQCEGDDIPALGILPLGTANDFATSVGIPEALDKALKLAIAGDAIAIDMAQVNKQTCFINMATGGFGTRITTETPEKLKAALGSVSYIIHGLMRMDTLQPDRCEIRGENFHWQGDALVIGIGNGRQAGGGQQLCPNALINDGLLQLRIFTGDEILPALVSTLKSDEDNPNIIEGASSWFDIQAPHDITFNLDGEPLSGQNFHIEILPAALRCRLPPDCPLLR |
| 预测分子量 | 48.0 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yegS重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Structural and functional characterization of the yegS gene product: A novel bacterial kinase involved in phospholipid metabolism*
**作者**：Smith A, et al.
**摘要**：研究通过重组表达纯化了大肠杆菌yegS蛋白，证明其具有磷脂酶D(PLD)结构域和ATP结合活性，揭示了其在磷脂酸代谢中的激酶功能，并分析了其与细菌膜稳态的关联。
2. **文献名称**：*Crystallographic analysis of the yegS/pldB phosphatase from Escherichia coli: Insights into its catalytic mechanism*
**作者**：Chen L, et al.
**摘要**：通过X射线晶体学解析了yegS重组蛋白的三维结构，发现其属于HAD超家族磷酸酶，提出了依赖Mg²⁺的催化机制，并验证了突变体对底物水解活性的影响。
3. **文献名称**：*Functional genomics of yegS in Escherichia coli: Role in stress response and biofilm formation*
**作者**：Yoon JH, et al.
**摘要**：利用基因敲除和重组蛋白回补实验，证明yegS缺失导致细菌对氧化应激敏感且生物膜形成能力下降，提示其在环境适应性中的调控作用。
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注：以上文献信息为示例，实际引用需根据具体论文调整。建议通过PubMed或Google Scholar以“yegS recombinant”“pldB kinase”等关键词检索最新研究。
YegS, also known as phosphatidylglycerol phosphatase or lipid A phosphatase, is a conserved bacterial enzyme involved in lipid metabolism and cell membrane homeostasis. Encoded by the *yegS* gene in *Escherichia coli*, this protein regulates lipid A biosynthesis – a critical component of the outer membrane in Gram-negative bacteria. Functionally, YegS catalyzes the dephosphorylation of undecaprenyl pyrophosphate (UndPP), a lipid carrier essential for peptidoglycan and lipopolysaccharide assembly. Its activity ensures proper lipid recycling and prevents toxic accumulation of UndPP, which could disrupt membrane integrity.
Recombinant YegS protein is produced via heterologous expression systems (e.g., *E. coli* or insect cells) for structural and functional studies. Its purification typically involves affinity chromatography tags like His-tags, enabling detailed biochemical characterization. Research on YegS has gained momentum due to its potential as a therapeutic target. Inhibiting YegS could impair bacterial membrane synthesis, offering a strategy to combat antibiotic-resistant pathogens. Structural analyses, including X-ray crystallography, reveal a haloacid dehalogenase (HAD) superfamily fold with a conserved catalytic motif, providing insights into its mechanism.
Studies also link YegS homologs to stress responses and virulence in pathogenic bacteria, highlighting its broader physiological roles. In biotechnology, recombinant YegS serves as a model enzyme to study lipid-phosphate phosphatase activity and membrane biophysics. Despite progress, questions remain about its regulation and interactions with other lipid-modifying enzymes. Ongoing research aims to exploit YegS’s enzymatic properties for antimicrobial development and industrial applications in lipid engineering.
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