| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | plsC |
| Uniprot No | P26647 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-245aa |
| 氨基酸序列 | MLYIFRLIITVIYSILVCVFGSIYCLFSPRNPKHVATFGHMFGRLAPLFGLKVECRKPTDAESYGNAIYIANHQNNYDMVTASNIVQPPTVTVGKKSLLWIPFFGQLYWLTGNLLIDRNNRTKAHGTIAEVVNHFKKRRISIWMFPEGTRSRGRGLLPFKTGAFHAAIAAGVPIIPVCVSTTSNKINLNRLHNGLVIVEMLPPIDVSQYGKDQVRELAAHCRSIMEQKIAELDKEVAEREAAGKV |
| 预测分子量 | 29.5 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PlsC重组蛋白的示例参考文献(注：文献为示例性质，建议通过学术数据库查询真实文献)：
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1. **文献名称**: "Functional Characterization of the plsC Gene-Encoded Acyltransferase in Escherichia coli"
**作者**: Schujman, D.E., et al.
**摘要**: 研究在大肠杆菌中克隆表达PlsC重组蛋白，证实其作为1-酰基-sn-甘油-3-磷酸酰基转移酶的活性，参与磷脂酸合成，并通过突变分析揭示关键催化位点。
2. **文献名称**: "Crystal Structure of PlsC from Bacillus subtilis and Its Role in Membrane Biogenesis"
**作者**: Yao, J., & Rock, C.O.
**摘要**: 解析了枯草芽孢杆菌PlsC重组蛋白的晶体结构，阐明其底物结合域和催化机制，为针对细菌磷脂合成的抗菌药物设计提供结构基础。
3. **文献名称**: "Antibacterial Drug Discovery Targeting PlsC: A High-Throughput Screening Approach"
**作者**: Zhang, L., et al.
**摘要**: 利用重组PlsC蛋白建立高通量筛选平台，鉴定出小分子抑制剂，证明其可抑制金黄色葡萄球菌PlsC活性并减少细菌存活率。
4. **文献名称**: "Regulation of plsC Expression and Its Role in Bacterial Membrane Homeostasis"
**作者**: Paoletti, L., et al.
**摘要**: 探讨PlsC在细菌应激反应中的调控机制，发现其表达受脂肪酸可用性影响，并通过重组蛋白实验验证其在维持膜完整性中的作用。
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建议通过PubMed、Web of Science等平台以“PlsC recombinant protein”、“PlsC acyltransferase”等关键词检索最新文献。
**Background of PlsC Recombinant Protein**
PlsC, a key enzyme in bacterial phospholipid biosynthesis, is a membrane-associated acyltransferase responsible for the critical step of transferring acyl groups to the sn-2 position of glycerol-3-phosphate (G3P), forming lysophosphatidic acid (LPA). This reaction is essential for constructing the phospholipid bilayer, a fundamental component of bacterial cell membranes. PlsC belongs to the PlsB/PlsC family of acyltransferases and is primarily found in Gram-negative bacteria, including pathogens like *Escherichia coli* and *Salmonella enterica*. Its role in membrane biogenesis makes it a potential target for antibacterial drug development, as disrupting phospholipid synthesis could compromise bacterial viability.
Recombinant PlsC protein is produced through heterologous expression, often in *E. coli* systems, enabling large-scale purification for biochemical and structural studies. The protein is typically engineered with affinity tags (e.g., His-tag) to facilitate purification via chromatography. Studies on PlsC focus on elucidating its catalytic mechanism, substrate specificity, and interaction with inhibitors. Structural analyses, including X-ray crystallography or cryo-EM, aim to resolve its active-site architecture and guide rational inhibitor design.
Additionally, PlsC’s enzymatic activity is utilized in *in vitro* assays to screen antimicrobial compounds targeting lipid metabolism. Its recombinant form also serves as a tool for studying bacterial membrane assembly under stress conditions or genetic mutations. Recent research explores its role in bacterial antibiotic resistance, as altered phospholipid composition may influence membrane permeability to drugs. Despite its functional importance, PlsC’s regulatory mechanisms and potential cross-species variations remain areas of active investigation. Overall, PlsC recombinant protein provides a versatile platform for advancing both basic microbiology and applied therapeutic development.
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