| 纯度 | >90%SDS-PAGE. |
| 种属 | Mouse |
| 靶点 | Defb14 |
| Uniprot No | Q7TNV9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-67aa |
| 氨基酸序列 | FLPKTLRKFFCRIRGGRCAVLNCLGKEEQIGRCSNSGRKCCRKKK |
| 预测分子量 | 21.2 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. |
以下是关于Defb14重组蛋白的示例参考文献(内容为虚构示例，仅用于演示格式)：
1. **《重组Defb14蛋白的制备及其抗菌活性研究》**
作者：Smith A, et al.
摘要：本研究通过大肠杆菌表达系统成功制备了重组Defb14蛋白，并验证其对金黄色葡萄球菌和铜绿假单胞菌的广谱抗菌活性，揭示了其通过破坏细菌膜结构发挥作用的机制。
2. **《Defb14重组蛋白在口腔感染模型中的治疗潜力》**
作者：Zhang L, et al.
摘要：实验表明，重组Defb14能显著抑制口腔致病菌生物膜形成，并通过调节炎症因子表达改善小鼠口腔感染模型的病理损伤，提示其作为新型抗菌药物的潜力。
3. **《Defb14重组蛋白的结构与功能关系分析》**
作者：Kim S, et al.
摘要：通过核磁共振技术解析了重组Defb14的三维结构，发现其β-折叠区域的关键氨基酸残基与抗菌活性直接相关，为优化抗菌肽设计提供了结构基础。
4. **《重组Defb14对耐药菌的协同抗菌效应》**
作者：Wang X, et al.
摘要：研究发现，重组Defb14与常用抗生素联用可显著降低耐药大肠杆菌的存活率，其机制可能与增强细胞膜通透性及抑制外排泵活性有关。
(注：以上文献为虚构，实际研究需查询PubMed、Web of Science等数据库获取真实信息。)
Defensins are small, cysteine-rich antimicrobial peptides crucial to innate immunity, categorized into α, β, and θ subtypes. Defb14 (β-defensin 14), a member of the β-defensin family, is encoded by the DEFB14 gene in humans. These peptides are primarily expressed in epithelial tissues and immune cells, serving as frontline defenders against pathogens by disrupting microbial membranes and modulating immune responses. β-defensins, including Defb14. typically contain six conserved cysteine residues forming three disulfide bonds, which stabilize their structure and enhance their antimicrobial activity.
Recombinant Defb14 is produced via biotechnological methods, often using bacterial (e.g., E. coli) or mammalian expression systems. However, its production faces challenges, such as maintaining proper disulfide bond formation and avoiding cytotoxicity to host cells. Post-expression, purification techniques like chromatography are employed to obtain functional protein.
Defb14 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. Beyond direct pathogen neutralization, it recruits immune cells (e.g., dendritic cells, T cells) and influences cytokine production, bridging innate and adaptive immunity. Recent studies explore its therapeutic potential in treating infections, chronic inflammation, and even cancer, where its immunomodulatory properties may enhance antitumor responses. Additionally, Defb14’s role in mucosal health, particularly in the respiratory and urogenital tracts, highlights its importance in barrier defense.
Despite promise, challenges persist, including optimizing recombinant yields, ensuring stability, and addressing potential off-target effects. Structural studies and mutagenesis aim to engineer analogs with improved efficacy and reduced toxicity. As antibiotic resistance rises, Defb14 and its derivatives represent compelling candidates for novel antimicrobial and immunotherapeutic strategies, though further preclinical and clinical validation is needed.
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