| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | nlpD |
| Uniprot No | P0ADA3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-379aa |
| 氨基酸序列 | CSDTSNPPAPVSSVNGNAPANTNSGMLITPPPKMGTTSTAQQPQIQPVQQ PQIQATQQPQIQPVQPVAQQPVQMENGRIVYNRQYGNIPKGSYSGSTYTV KKGDTLFYIAWITGNDFRDLAQRNNIQAPYALNVGQTLQVGNASGTPITG GNAITQADAAEQGVVIKPAQNSTVAVASQPTITYSESSGEQSANKMLPNN KPTATTVTAPVTVPTASTTEPTVSSTSTSTPISTWRWPTEGKVIETFGAS EGGNKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSA YAHNDTMLVREQQEVKAGQKIATMGSTGTSSTRLHFEIRYKGKSVNPLRY LPQR |
| 预测分子量 | 54 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nlpD重组蛋白的3篇参考文献及其简要摘要：
1. **文献名称**：Role of NlpD in Cell Division of Escherichia coli
**作者**：Smith A, et al.
**摘要**：研究通过重组表达NlpD蛋白，发现其与细胞分裂蛋白Envc的相互作用，揭示其在调控大肠杆菌分裂环组装中的关键作用。
2. **文献名称**：Recombinant NlpD as a Potential Vaccine Target Against Salmonella
**作者**：Zhang L, et al.
**摘要**：利用大肠杆菌表达系统成功纯化重组NlpD蛋白，动物实验表明其可诱导强烈免疫应答，为沙门氏菌疫苗开发提供候选抗原。
3. **文献名称**：Structural Insights into NlpD-Mediated Outer Membrane Stress Response
**作者**：Chen H, et al.
**摘要**：通过重组表达和X射线晶体学解析NlpD蛋白结构，阐明其作为外膜应激感受器通过β-桶结构域传递信号的分子机制。
注：上述文献为示例性质，实际文献需通过学术数据库检索确认。若需具体文献，建议在PubMed等平台以"NlpD recombinant protein"为关键词搜索。
**Background of nlpD Recombinant Protein**
The nlpD gene encodes a bacterial outer membrane lipoprotein involved in various cellular processes, including cell division, stress response, and biofilm formation. Initially identified in *Escherichia coli*, NlpD plays a critical role in coordinating peptidoglycan synthesis during cell constriction, interacting with proteins like ActS/ActM to regulate amidase activity. Its functional domains, such as the lysin motif (LysM), enable binding to peptidoglycan, facilitating cell wall remodeling.
Recombinant nlpD protein is produced via genetic engineering, typically by cloning the nlpD gene into expression vectors (e.g., *E. coli* systems) to enable large-scale production. Purification methods like affinity chromatography ensure high yield and purity. This engineered protein retains native structural and functional properties, making it valuable for studying bacterial cell division mechanisms and host-pathogen interactions.
In research, nlpD recombinant protein has been utilized to investigate its role in biofilm formation and antibiotic resistance, particularly in pathogens like *Salmonella* and *Pseudomonas aeruginosa*. It also serves as a potential target for antimicrobial strategies, given its conservation across Gram-negative bacteria. Additionally, its immunogenic properties are explored for vaccine development against bacterial infections.
Beyond basic science, applications extend to industrial enzyme production and biosensor development. However, challenges remain in optimizing expression conditions and minimizing endotoxin contamination during purification. Ongoing studies aim to elucidate its interaction networks and exploit its biotechnological potential, positioning nlpD recombinant protein as a versatile tool in microbiology and biomedical engineering.
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