| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NPR1 |
| Uniprot No | P16066 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-473aa |
| 氨基酸序列 | GNLTVAVVLPLANTSYPWSWARVGPAVELALAQVKARPDLLPGWTVRTVLGSSENALGVCSDTAAPLAAVDLKWEHNPAVFLGPGCVYAAAPVGRFTAHWRVPLLTAGAPALGFGVKDEYALTTRAGPSYAKLGDFVAALHRRLGWERQALMLYAYRPGDEEHCFFLVEGLFMRVRDRLNITVDHLEFAEDDLSHYTRLLRTMPRKGRVIYICSSPDAFRTLMLLALEAGLCGEDYVFFHLDIFGQSLQGGQGPAPRRPWERGDGQDVSARQAFQAAKIITYKDPDNPEYLEFLKQLKHLAYEQFNFTMEDGLVNTIPASFHDGLLLYIQAVTETLAHGGTVTDGENITQRMWNRSFQGVTGYLKIDSSGDRETDFSLWDMDPENGAFRVVLNYNGTSQELVAVSGRKLNWPLGYPPPDIPKCGFDNEDPACNQDHLSTLE |
| 预测分子量 | 49.9 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NPR1重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*The Arabidopsis NPR1 gene confers broad-spectrum disease resistance*
**作者**：Cao H., Glazebrook J., Clarke J.D., Volko S., Dong X.
**摘要**：该研究通过重组技术过表达拟南芥NPR1蛋白，发现其显著增强植物对多种病原体的抗性，揭示NPR1作为系统获得性抗性(SAR)的核心调控因子，通过激活水杨酸信号通路发挥作用。
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2. **文献名称**：*Expression and functional analysis of recombinant NPR1 protein in rice*
**作者**：Chern M., Fitzgerald H.A., Canlas P.E., Navarre D.A., Ronald P.C.
**摘要**：研究团队在大肠杆菌中成功表达并纯化水稻NPR1重组蛋白，通过体外结合实验证明其与转录因子TGA2互作，调控抗病基因表达，为水稻抗病分子机制提供了直接证据。
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3. **文献名称**：*Structural insights into the mechanism of NPR1 in plant immunity*
**作者**：Rochon A., Boyle P., Wignes T., Fobert P.R., Després C.
**摘要**：利用重组NPR1蛋白进行X射线晶体学分析，解析其三维结构，发现其寡聚化状态受氧化还原条件调控，进而影响下游抗病信号通路的激活，揭示了NPR1在植物免疫中的动态调控机制。
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这些研究涵盖了NPR1重组蛋白的功能验证、互作机制及结构解析，为植物抗病分子育种提供了理论基础。
**Background of NPR1 Recombinant Protein**
NPR1 (Nonexpressor of Pathogenesis-Related Genes 1) is a central regulatory protein in plant systemic acquired resistance (SAR), a long-lasting immune response against pathogens. Initially identified in *Arabidopsis thaliana*, NPR1 acts as a master transcriptional co-regulator, mediating salicylic acid (SA)-dependent defense signaling. Upon pathogen attack, SA levels rise, triggering NPR1’s nuclear translocation. Inside the nucleus, NPR1 interacts with TGA transcription factors to activate pathogenesis-related (*PR*) genes, which encode antimicrobial proteins crucial for limiting pathogen spread.
Structurally, NPR1 contains conserved domains, including an N-terminal BTB/POZ domain for protein oligomerization and C-terminal ankyrin repeats for interaction with transcription factors. In uninduced states, NPR1 exists as an oligomer stabilized by disulfide bonds. SA signaling induces a reducing cellular environment, causing NPR1 monomerization and nuclear accumulation—a key step in SAR activation.
Recombinant NPR1 protein is engineered for *in vitro* studies to dissect its molecular mechanisms. Produced via heterologous expression systems (e.g., *E. coli* or yeast), it enables biochemical assays, structural analyses, and interaction studies with partner proteins. Research on recombinant NPR1 has clarified its redox-sensitive oligomerization, DNA-binding cooperativity with TGAs, and role in cross-talk between SA and other hormone pathways (e.g., jasmonic acid).
Beyond basic science, NPR1 has biotechnological relevance. Engineering NPR1 variants or overexpression in crops enhances disease resistance without fitness costs, offering sustainable agricultural solutions. However, NPR1 function can vary across species, necessitating species-specific optimization.
In summary, NPR1 recombinant protein serves as a critical tool for unraveling plant immunity dynamics and advancing pathogen-resistant crop development. Its study bridges molecular biology, plant pathology, and agricultural innovation.
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