纯度 | >90%SDS-PAGE. |
种属 | mouse |
靶点 | DEFa5 |
Uniprot No | P28312 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 59-93aa |
氨基酸序列 | SKKLICYCRIRGCKRRERVFGTCRNLFLTFVFCCS |
预测分子量 | 31.2kDa |
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DEFa5(防御素α5)重组蛋白的3篇文献示例(注:文献信息为模拟概括,仅供参考):
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1. **文献名称**:*"Recombinant human α-defensin 5 (HD5) exhibits broad-spectrum antimicrobial activity against pathogenic bacteria"*
**作者**:Lehrer, R.I., et al.
**摘要**:研究报道了重组HD5蛋白(人源α-防御素5)对革兰氏阴性菌(如大肠杆菌)和革兰氏阳性菌(如金黄色葡萄球菌)的体外抗菌活性,并探讨其通过破坏细菌膜电位和细胞壁完整性的作用机制。
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2. **文献名称**:*"Optimization of DEFa5 expression in E. coli for enhanced production and stability"*
**作者**:Zhang, Y., et al.
**摘要**:通过优化大肠杆菌表达系统的启动子、培养条件和纯化步骤,显著提高了重组DEFa5的产量和稳定性,为大规模生产提供可行方案。
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3. **文献名称**:*"Structural and functional characterization of DEFa5 in mucosal immunity"*
**作者**:Bevins, C.L., et al.
**摘要**:利用核磁共振(NMR)解析了DEFa5的分子结构,发现其通过特定β-折叠构象与宿主肠道上皮细胞受体互作,增强黏膜屏障功能并抑制病原体定植。
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4. **文献名称**:*"Recombinant DEFa5 synergizes with conventional antibiotics against multidrug-resistant pathogens"*
**作者**:Wang, H., et al.
**摘要**:研究表明,重组DEFa5与β-内酰胺类抗生素联用可显著降低耐药性肺炎克雷伯菌的生物膜形成能力,提示其作为抗生素佐剂的潜力。
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**注**:以上文献为示例性内容,实际文献需通过PubMed、Web of Science或Google Scholar检索关键词(如“DEFa5 recombinant protein”、“HD5 antimicrobial”等)获取。近年研究可能聚焦于其在感染性疾病、肠道菌群调控或肿瘤免疫中的应用。
DEFa5 (Human Alpha-Defensin 5), also known as HD5. is a small cationic antimicrobial peptide belonging to the α-defensin family. It is primarily produced by Paneth cells in the small intestine and plays a critical role in innate immune defense. Structurally, DEFa5 consists of 32 amino acids stabilized by three disulfide bonds, forming a compact triple-stranded β-sheet fold. This conformation enhances its stability and interaction with microbial membranes. Its antimicrobial activity targets bacteria, fungi, and enveloped viruses by disrupting membrane integrity through electrostatic interactions with negatively charged microbial surfaces.
Recombinant DEFa5 is engineered using expression systems like *E. coli* or mammalian cells, followed by purification via chromatography to ensure high purity and bioactivity. Its production addresses the challenges of low natural abundance and the complexity of synthesizing disulfide-rich peptides. Research highlights DEFa5's dual role: direct pathogen neutralization and immunomodulatory effects, such as chemotaxis and cytokine regulation. Studies also suggest its potential in cancer therapy due to selective cytotoxicity toward malignant cells.
Clinically, DEFa5 is explored for treating infections, inflammatory bowel disease (IBD), and chronic wounds. Its relevance in gut microbiota homeostasis has drawn attention to its therapeutic potential in dysbiosis-related conditions. However, challenges like enzymatic degradation and optimization of delivery methods remain active areas of investigation. As a model peptide, DEFa5 contributes to understanding defensin biology and developing peptide-based therapeutics, bridging innate immunity and clinical applications.
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