| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | NRPS1 |
| Uniprot No | Q4WT66 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 894-1342aa |
| 氨基酸序列 | LSPIQKLHFMVRKEGQGYFNQSVVTRIDRQINDQDMRRAVEAVVMRHSMLRSRLVDPSTGNSLQLRITEDVAGSYRWRTHYMTAQNEIENAIAESQLCINAFVGPVFAVDFCYVDEDSHNLLSLVAHHLVVDIVSWRIILEDLEDFLLNPQGFVLQNSSLPFQTWCRLQDEQCESVAFENDVQLEDLPAPDLAYWGMEHRQMTYGDVICETFELDPGSTQSILLECHQSLRTEPVDLFLAALVHSFGQTFPERTLPVIYNEGHGREVWDSSLDISRTVGWFTTLYPIFVQEIVSEDPARTVARVKDLRRQVSDNGRQKFASRMFTGKGQQTCRHHYPLEMTFNYVGQHRDLQKQDGLFQLMGHMAGEAGQGGGAADFGEETPRFALLEISALVVQGQLRFTFSFNRFMRHQSGIHAWISRCHQLLASLGQKLQSLAPQPTLSDFPMLSL |
| 预测分子量 | 67.2 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. |
以下是几篇关于NRPS1(非核糖体多肽合成酶1)重组蛋白的模拟参考文献示例(注：以下内容为虚构示例，实际文献需通过学术数据库检索获取)：
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1. **文献名称**：*Heterologous Expression and Functional Analysis of NRPS1 in Saccharomyces cerevisiae*
**作者**：Zhang, L.; Wang, H.; Chen, F.
**摘要**：本研究成功在大肠杆菌和酵母中重组表达了NRPS1蛋白，并通过质谱和酶活性分析验证其功能。结果显示，NRPS1在体外催化特定氨基酸缩合反应，可能参与次生代谢产物的生物合成。
2. **文献名称**：*Structural Insights into the Adenylation Domain of NRPS1 by X-ray Crystallography*
**作者**：Müller, T.; Schmidt, B.; Heide, L.
**摘要**：通过X射线晶体学解析了NRPS1的腺苷化结构域三维结构，揭示了其底物结合口袋的关键氨基酸残基，为理性设计新型非核糖体多肽提供了理论依据。
3. **文献名称**：*NRPS1-Dependent Biosynthesis of Antifungal Compounds in Pseudomonas fluorescens*
**作者**：Kim, S.; Park, J.; Ryu, C.M.
**摘要**：研究证明NRPS1重组蛋白在荧光假单胞菌中负责合成一种新型抗真菌脂肽，其基因敲除导致抗菌活性丧失，表明其在生物防治中的潜在应用。
4. **文献名称**：*Optimization of NRPS1 Recombinant Protein Production in E. coli Using Response Surface Methodology*
**作者**：Gupta, R.; Yadav, S.; Dhingra, G.K.
**摘要**：通过实验设计优化了大肠杆菌中NRPS1重组蛋白的可溶性表达条件，最终蛋白产量提高3倍，并保留完整酶活性。
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**建议**：实际研究中，请通过 **PubMed**、**Web of Science** 或 **Google Scholar** 检索关键词(如“NRPS1 recombinant protein”、“NRPS heterologous expression”)获取真实文献。
**Background of NRPS1 Recombinant Protein**
Nonribosomal peptide synthetase 1 (NRPS1) is a multifunctional enzyme involved in the biosynthesis of nonribibosomal peptides (NRPs), a class of secondary metabolites with diverse biological activities. NRPS1 is part of a modular enzyme system that assembles peptides without relying on ribosomal machinery. Instead, it utilizes adenylation (A), thiolation (T), and condensation (C) domains to activate, transfer, and link amino acid or other carboxylic acid substrates. These peptides often play critical roles in microbial communication, iron acquisition (e.g., siderophores), and host-pathogen interactions.
In plants, NRPS1 homologs have been studied for their roles in defense mechanisms. For instance, *Arabidopsis thaliana* NRPS1 (AtNRPS1) is implicated in synthesizing metabolites that contribute to pathogen resistance. Its recombinant form is engineered for in vitro studies to dissect enzymatic mechanisms, substrate specificity, and interactions with partner proteins. Recombinant NRPS1 is typically produced via heterologous expression systems (e.g., *E. coli* or yeast), enabling large-scale purification and structural-functional analyses.
Research on NRPS1 recombinant protein has advanced synthetic biology applications, such as designing novel peptides with therapeutic or agricultural potential. Additionally, understanding its catalytic domains aids in engineering hybrid NRPS systems for tailored metabolite production. Challenges include optimizing expression conditions to maintain enzyme activity and resolving complex domain interactions.
Overall, NRPS1 recombinant protein serves as a vital tool for exploring nonribosomal peptide biosynthesis, with implications for drug discovery, crop protection, and industrial biotechnology.
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