| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNASE3 |
| Uniprot No | P12724 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-160aa |
| 氨基酸序列 | MVPKLFTSQICLLLLLGLMGVEGSLHARPPQFTRAQWFAIQHISLNPPRCTIAMRAINNYRWRCKNQNTFLRTTFANVVNVCGNQSIRCPHNRTLNNCHRSRFRVPLLHCDLINPGAQNISNCTYADRPGRRFYVVACDNRDPRDSPRYPVVPVHLDTTI |
| 预测分子量 | 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RNASE3(嗜酸性粒细胞阳离子蛋白，ECP)重组蛋白的3篇参考文献概览：
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1. **文献名称**: *"Recombinant human eosinophil cationic protein: purification and characterization of its ribonuclease activity"*
**作者**: Sorrentino S. et al.
**摘要**: 该研究报道了通过大肠杆菌表达系统成功重组表达人源RNASE3蛋白，并优化了纯化步骤。研究发现重组RNASE3具有与天然蛋白相似的核糖核酸酶活性和抗菌活性，验证了其功能完整性。
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2. **文献名称**: *"Structural and functional insights into the mechanism of action of human eosinophil cationic protein"*
**作者**: Navarro S. et al.
**摘要**: 通过X射线晶体学解析了重组RNASE3的三维结构，揭示了其与RNA底物结合的关键氨基酸位点。实验还证实重组蛋白对细菌膜的破坏能力与其表面正电荷分布密切相关。
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3. **文献名称**: *"Recombinant ECP induces airway inflammation through activation of TLR2 signaling pathway"*
**作者**: Wang H. et al.
**摘要**: 研究利用重组RNASE3蛋白在小鼠模型中模拟哮喘炎症反应，发现其通过激活TLR2信号通路促进Th2型免疫反应，为ECP在过敏性疾病中的作用机制提供了实验依据。
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以上文献涵盖了重组RNASE3的表达纯化、结构功能研究及疾病模型中的应用方向。如需具体年份或期刊信息，可进一步补充关键词检索。
RNASE3. also known as eosinophil cationic protein (ECP), is a member of the ribonuclease A (RNase A) superfamily, primarily secreted by eosinophils, a type of immune cell involved in innate immunity and inflammatory responses. This protein plays dual roles in host defense and pathology. It exhibits ribonuclease activity, enabling RNA degradation, and possesses potent cytotoxic properties against pathogens, including bacteria, parasites, and viruses. Its cationic nature allows it to disrupt microbial membranes, contributing to pathogen clearance. However, excessive RNASE3 release is linked to tissue damage in allergic and inflammatory diseases, such as asthma and eczema.
Recombinant RNASE3 is produced via molecular cloning techniques, typically using bacterial (e.g., *E. coli*) or eukaryotic expression systems. The recombinant form retains the native protein’s structural and functional characteristics, including its catalytic and membrane-binding domains, making it a valuable tool for studying eosinophil-mediated immunity and disease mechanisms. Researchers employ it to dissect structure-function relationships, particularly how specific residues or domains influence enzymatic activity, cell targeting, and cytotoxicity.
In therapeutic contexts, recombinant RNASE3 has been explored for its potential as an antimicrobial or anticancer agent, leveraging its ability to induce apoptosis in certain cancer cells. Additionally, it serves as a biomarker in clinical studies to monitor eosinophil activation in diseases. Engineering variants with modified activity or reduced immunogenicity further highlights its adaptability for biomedical applications. Despite its promise, challenges remain in balancing its beneficial effects with its potential to exacerbate inflammation, underscoring the need for targeted delivery strategies in therapeutic development.
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