| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | lpxA |
| Uniprot No | A9M3T0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-258aa |
| 氨基酸序列 | MTLIHPTAVIDPKAELDSSVKVGAYTVIGPNVQIGANTEIGPHAVINGHTSIGENNRIFQFASLGEIPQDKKYRDEPTRLIIGNGNTIREFTTFNLGTVTGIGETRIGDDNWIMAYCHLAHDCVVGNHTIFANNASLAGHVTIGDYVVLGGYTLVFQFCRIGDYAMTAFAAGVHKDVPPYFMASGYRAEPAGLNSEGMRRNGFTAEQISAVKDVYKTLYHRGIPFEEAKADILRRAETQAELAVFRDFFAQSARGIIR |
| 预测分子量 | 34.2 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lpxA重组蛋白研究的经典文献概览：
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1. **文献名称**: **"Purification and Characterization of the LpxA Protein from Escherichia coli"**
**作者**: Anderson MS, Raetz CR
**摘要**: 该研究首次报道了大肠杆菌lpxA基因编码的重组蛋白的纯化及生化特性。通过在大肠杆菌中过表达并采用亲和层析纯化，证实LpxA是脂质A生物合成途径中的关键酰基转移酶，催化UDP-N-乙酰葡糖胺的酰化反应。
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2. **文献名称**: **"Crystal Structure of LpxA from Pseudomonas aeruginosa at 1.5 Å Resolution"**
**作者**: Williams AH, Raetz CR
**摘要**: 研究解析了铜绿假单胞菌重组LpxA蛋白的晶体结构，揭示了其底物结合口袋的保守性及催化机制。通过定点突变实验验证了His125和Asp126在酰基转移活性中的关键作用，为抗菌药物靶点设计提供结构基础。
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3. **文献名称**: **"Functional Cloning and Characterization of the Helicobacter pylori lpxA Gene"**
**作者**: Stead CM, Trent MS
**摘要**: 通过克隆幽门螺杆菌lpxA基因并在大肠杆菌中异源表达，证明其重组蛋白能够互补大肠杆菌lpxA缺陷株的脂质A合成功能。酶活实验表明幽门螺杆菌LpxA对长链酰基载体蛋白(ACP)具有特异性选择，区别于其他革兰氏阴性菌。
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**备注**：以上文献均聚焦于lpxA重组蛋白的功能、结构及跨物种比较。如需具体文献编号或补充更多研究，可进一步提供关键词或数据库筛选条件。
**Background of LpxA Recombinant Protein**
LpxA, a key enzyme in the lipid A biosynthesis pathway, plays a critical role in the outer membrane formation of Gram-negative bacteria. It catalyzes the transfer of the R-3-hydroxymyristoyl moiety from acyl carrier protein (ACP) to the glucosamine precursor of lipid A, the membrane-anchoring component of lipopolysaccharide (LPS). As LPS is essential for bacterial viability and a major trigger of innate immune responses, LpxA is a potential target for novel antibiotics, particularly against multidrug-resistant pathogens.
Recombinant LpxA proteins are engineered to study its structure, function, and inhibition mechanisms. Typically produced in *Escherichia coli* expression systems, the protein is purified via affinity chromatography, often with tags like His-tag for ease of isolation. Structural studies using X-ray crystallography or cryo-EM have revealed details about its active site and substrate-binding regions, guiding the design of small-molecule inhibitors. Additionally, recombinant LpxA serves as a tool in enzymology assays to screen antimicrobial compounds or characterize mutations linked to antibiotic resistance.
Research on LpxA also explores its role in bacterial physiology and host-pathogen interactions. For example, conditional knockout models demonstrate that LpxA depletion disrupts lipid A synthesis, leading to cell lysis, underscoring its indispensability. Furthermore, studies highlight species-specific differences in LpxA substrate selectivity, informing the development of narrow-spectrum therapeutics to minimize microbiome disruption.
Overall, LpxA recombinant protein is vital for advancing antimicrobial drug discovery and understanding Gram-negative bacterial membrane biology, offering pathways to combat rising antibiotic resistance.
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