| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | egsA |
| Uniprot No | B3EYN8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-404aa |
| 氨基酸序列 | MNQTLEEVVSLARQCGCGHRHYDIPIEQMVVGREAFARLVAYLRHKRYERVAIVADDHTFAAVERSLCDQLENGSIRYTVCLVQPDENGDVIADERSIVQVLLETPDDVDVLIAVGAGTIHDITRFSSYKMRIPFISVPTAPSVDGFTSMGAPLIIRGVKKTIQAQAPIAVFAHTGVLCQSPKEMIAAGFGDMVAKYTSLADWQFAHWMADEPYCPFVHQLTEQSLQTCVDHIDDIAAGGEQGIRVLMDALLQSGIAMLLMGQSYSASGAEHHLSHYWEMEFLRQKKRQVLHGAKVGVSTPIIIEHYQRVFWPLLNELEKRPKSMDEATWERLKANTASIRELLESLPSPERIRTMLAKVGGAIAPEQLGIDPQLVERSLREAHRLRLNRFTMLYFLNELIFVE |
| 预测分子量 | 47.4 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篇关于 **egsA重组蛋白** 的文献参考(虚构示例，实际文献需根据具体研究检索)：
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1. **文献名称**: *Functional characterization of EgsA as a key enzyme in bacterial lipid A biosynthesis*
**作者**: Smith J, et al.
**摘要**: 本研究解析了egsA基因编码的酶在革兰氏阴性菌脂质A合成中的功能，通过重组蛋白表达和体外酶活实验，证明EgsA催化脂质A前体的关键糖基化步骤，为新型抗生素靶点提供依据。
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2. **文献名称**: *Crystal structure and biochemical analysis of EgsA from Escherichia coli*
**作者**: Tanaka K, et al.
**摘要**: 报道了大肠杆菌EgsA重组蛋白的晶体结构，结合突变体分析揭示了其底物结合口袋及催化机制，阐明了该酶在细胞膜合成中的构效关系。
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3. **文献名称**: *Heterologous expression and purification of EgsA in Pichia pastoris for antimicrobial screening*
**作者**: Wang L, et al.
**摘要**: 成功在毕赤酵母中高效表达并纯化具有活性的EgsA重组蛋白，建立基于该蛋白的高通量抑制剂筛选平台，筛选出多种潜在抗菌先导化合物。
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如需真实文献，建议通过PubMed或Google Scholar检索关键词 **"egsA gene"、"EgsA protein"、"lipid biosynthesis"** 或结合具体物种(如 *Staphylococcus aureus*)。
**Background of egsA Recombinant Protein**
The *egsA* gene encodes a conserved bacterial enzyme, glycerol phosphate synthase (EGS), which plays a critical role in cell membrane biosynthesis. Initially identified in *Staphylococcus aureus*, EGS catalyzes the conversion of phosphatidic acid (PA) to lysyl-phosphatidylglycerol (L-PG), a key step in modifying bacterial membrane lipids. This enzymatic process is vital for maintaining membrane fluidity, charge homeostasis, and resistance to cationic antimicrobial peptides (CAMPs), which are critical for bacterial survival under hostile host environments.
EGS activity is particularly significant in pathogenic bacteria, such as methicillin-resistant *S. aureus* (MRSA), where membrane modifications contribute to antibiotic resistance and immune evasion. The enzyme’s unique substrate specificity and absence in humans make it an attractive target for developing novel antimicrobial therapies. However, structural and functional studies of EGS have been limited by challenges in obtaining sufficient quantities of purified, active protein.
To address this, recombinant EGS (rEGS) is produced via heterologous expression in *E. coli* or other host systems. Cloning the *egsA* gene into expression vectors allows large-scale production of the protein, enabling biochemical characterization, inhibitor screening, and structural analysis (e.g., X-ray crystallography or cryo-EM). Recombinant EGS retains catalytic activity in vitro, facilitating studies on its mechanism, kinetics, and interaction with potential inhibitors.
Recent research highlights rEGS’s role in elucidating bacterial membrane adaptation mechanisms and its potential as a drug target. However, challenges remain, including optimizing protein solubility and stability during purification. Advances in recombinant protein engineering, such as fusion tags or codon optimization, continue to enhance the utility of rEGS in both basic science and antibacterial drug discovery.
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