纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | DEFB111 |
Uniprot No | Q30KQ9 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-67aa |
氨基酸序列 | MKIQLFFFILHFWVTILPAKKKYPEYGSLDLRRECRIGNGQCKNQCHENEIRIAYCIRPGTHCCLQQ |
分子量 | 33.77 kDa |
蛋白标签 | GST-tag at N-terminal |
缓冲液 | 0 |
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. |
以下是关于重组人DEFB111蛋白的参考文献示例(注:部分内容为假设性概括,实际文献可能需要进一步检索验证):
1. **标题**:**"Expression and functional characterization of recombinant human DEFB111 in a mammalian cell system"**
**作者**:Chen L, et al.
**摘要**:该研究通过哺乳动物表达系统成功重组表达了人DEFB111蛋白,证实其具有广谱抗菌活性,尤其对革兰氏阴性菌(如大肠杆菌)表现出显著杀伤作用,并揭示了其通过破坏细菌膜完整性发挥功能的机制。
2. **标题**:**"Structural insights into the pH-dependent activity of human beta-defensin 111"**
**作者**:Kim S, et al.
**摘要**:通过核磁共振(NMR)解析了重组人DEFB111的立体结构,发现其抗菌活性依赖环境pH值。低pH条件下,蛋白构象变化暴露出疏水区域,增强与病原体细胞膜的相互作用。
3. **标题**:**"Recombinant DEFB111 synergizes with lysozyme to enhance innate immune response in airway epithelial cells"**
**作者**:Martinez F, et al.
**摘要**:本研究证明重组DEFB111与溶菌酶协同作用,可显著增强呼吸道上皮细胞的抗菌和抗炎反应,提示其在黏膜免疫治疗中的潜在应用价值。
4. **标题**:**"High-yield production of bioactive human DEFB111 using Pichia pastoris expression system"**
**作者**:Zhang Y, et al.
**摘要**:开发了一种基于毕赤酵母的重组DEFB111高效表达与纯化工艺,获得的蛋白具有与天然分子相似的结构和生物活性,为大规模生产提供了可行方案。
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**注意**:以上文献为示例性质,实际研究中DEFB111的相关公开数据可能有限。建议通过PubMed或Web of Science以“DEFB111 recombinant”“human beta-defensin 111”等关键词检索最新文献。若研究较少,可拓展至相近的β-防御素家族(如DEFB1、DEFB4)或重组防御素蛋白的表达策略作为参考。
Human beta-defensin 111 (DEFB111), a member of the β-defensin family, is a small cationic antimicrobial peptide encoded by the DEFB111 gene on chromosome 8p23.1. β-defensins are integral components of innate immunity, broadly involved in microbial defense, immune modulation, and tissue repair. DEFB111 is primarily expressed in epithelial tissues, including the skin, respiratory tract, and urogenital system, where it acts as a first-line barrier against pathogens by disrupting microbial membranes via electrostatic interactions. Its antimicrobial activity spans bacteria, fungi, and enveloped viruses. Beyond direct pathogen neutralization, DEFB111 interacts with immune receptors (e.g., CCR6) to recruit immune cells, bridging innate and adaptive immunity.
Recombinant DEFB111 protein is produced using prokaryotic (e.g., E. coli) or eukaryotic expression systems, often requiring careful optimization to maintain proper disulfide bond formation—critical for its functional tertiary structure. Purification typically involves affinity chromatography and refolding steps. Research focuses on its therapeutic potential in antimicrobial resistance, chronic wound healing, and immunoregulatory disorders. Challenges include stability in physiological environments and targeted delivery. Recent studies also explore synergies with conventional antibiotics, positioning recombinant DEFB111 as a promising candidate for multifunctional therapeutic development.
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