| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | def |
| Uniprot No | P0A6K3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-169aa |
| 氨基酸序列 | SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYAEEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEKSGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFELEADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEKLDRLKARA |
| 预测分子量 | 35.2 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3-4条关于重组防御素(recombinant defensin)蛋白的参考文献示例(内容为模拟概括，仅供参考)：
1. **文献名称**：*Expression and purification of recombinant human β-defensin 2 in Pichia pastoris*
**作者**：Smith A et al.
**摘要**：研究利用毕赤酵母系统表达人β-防御素2.优化发酵条件实现可溶性高产量，并证实其对革兰氏阴性菌的抗菌活性。
2. **文献名称**：*Engineering Escherichia coli for efficient production of functional plant defensin*
**作者**：Lee J et al.
**摘要**：通过密码子优化和融合标签策略，在大肠杆菌中高效表达具有折叠活性的植物防御素，解决原核表达中二硫键形成难题。
3. **文献名称**：*Recombinant defensin-loaded nanoparticles enhance wound healing in diabetic mice*
**作者**：Garcia R et al.
**摘要**：开发壳聚糖纳米颗粒负载重组α-防御素，显著提升其在糖尿病模型中的伤口愈合效果，机制涉及抗微生物和促细胞迁移作用。
4. **文献名称**：*Comparative analysis of defensin production in prokaryotic vs. eukaryotic systems*
**作者**：Kim H et al.
**摘要**：对比大肠杆菌、酵母和哺乳动物细胞表达防御素的优缺点，强调真核系统在复杂修饰中的优势及成本权衡。
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注：以上为模拟文献，实际文献需通过学术数据库(如PubMed、Web of Science)检索关键词“recombinant defensin”获取。
**Background of Recombinant DEF Proteins**
Recombinant DEF proteins, often derived from defensin-like molecules, are engineered versions of naturally occurring proteins involved in diverse biological processes, including antimicrobial defense, immune modulation, and cell signaling. Defensins, a well-studied family of small cysteine-rich proteins, are evolutionarily conserved across species and play critical roles in innate immunity by disrupting microbial membranes or interacting with host receptors to regulate immune responses. The term "DEF" may refer to specific defensins (e.g., human β-defensins) or related proteins engineered for research or therapeutic applications.
The development of recombinant DEF proteins leverages advances in genetic engineering and expression systems. By cloning DEF-encoding genes into bacterial, yeast, or mammalian host systems, researchers produce purified, functional proteins at scale. This approach overcomes limitations of natural extraction, such as low yield or heterogeneity, enabling precise study of DEF structures, mechanisms, and interactions.
Recombinant DEF proteins have broad applications. In biomedicine, they are explored as antimicrobial agents, anti-inflammatory therapeutics, or vaccine adjuvants. Their ability to selectively target pathogens or modulate immune pathways makes them promising alternatives to conventional antibiotics. In agriculture, DEF-based products are investigated for crop protection against microbial diseases.
Challenges include optimizing stability, delivery, and minimizing off-target effects. Advances in protein engineering, such as site-directed mutagenesis or fusion tags, aim to enhance functionality. Overall, recombinant DEF proteins represent a versatile toolset bridging immunology, biotechnology, and translational medicine, with ongoing research focused on unlocking their full therapeutic and industrial potential.
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