| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DEFb103A |
| Uniprot No | P81534 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-67aa |
| 氨基酸序列 | GIINTLQKYYCRVRGGRCAVLSCLPKEEQI GKCSTRGRKCCRRKK |
| 预测分子量 | 5 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DEFb103A(hBD-3)重组蛋白的3篇代表性文献概览：
1. **《Human beta-defensin 3: A novel antimicrobial peptide with diverse biological functions》**
- **作者**: Harder J, et al.
- **摘要**: 该研究首次克隆并重组表达了hBD-3蛋白，证实其广谱抗菌活性(包括对抗多重耐药菌)，并揭示了其在皮肤免疫防御中的关键作用。
2. **《Structure-activity analysis of β-defensin homology in recombinant hBD-3》**
- **作者**: Schneider JJ, et al.
- **摘要**: 通过重组表达和NMR技术解析hBD-3的蛋白结构，发现其特定氨基酸残基对抗菌活性和细胞趋化功能至关重要，为药物设计提供依据。
3. **《Recombinant hBD-3 accelerates wound healing and reduces biofilm formation in a murine model》**
- **作者**: Kawai T, et al.
- **摘要**: 动物实验表明，重组hBD-3通过促进上皮再生和抑制细菌生物膜形成显著加速伤口愈合，提示其作为新型创面治疗剂的潜力。
注：以上文献为示例，实际引用需核对具体论文信息。如需扩展，可补充工程化表达优化(如Kluver E, 2006)或免疫调节机制(如Becknell B, 2015)相关研究。
DEFb103A, also known as human β-defensin 103A, is a small cationic peptide belonging to the defensin family, which plays a critical role in innate immunity. Naturally produced by epithelial cells at mucosal surfaces and skin, it exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and enveloped viruses. Its mechanism involves disrupting microbial membranes through electrostatic interactions with negatively charged pathogen surfaces while exhibiting minimal toxicity to host cells. Beyond direct pathogen neutralization, DEFb103A modulates immune responses by recruiting immune cells and influencing cytokine production, bridging innate and adaptive immunity.
Recombinant DEFb103A is engineered via genetic cloning and expression systems, such as *E. coli* or mammalian cell cultures, to overcome limitations of natural extraction, including low yield and purification challenges. The recombinant form retains the native protein’s functional properties, enabling scalable production for research and therapeutic applications. Its stability and bioactivity are carefully optimized through codon optimization, fusion tags, or modified culture conditions.
Interest in recombinant DEFb103A spans antimicrobial therapy, wound healing, and immunomodulation. It is explored as a topical agent for infections resistant to conventional antibiotics, a vaccine adjuvant, or a component of antimicrobial coatings for medical devices. Challenges include maintaining structural integrity in physiological environments and minimizing off-target effects. Current research focuses on delivery systems (nanoparticles, hydrogels) and structure-function relationships to enhance therapeutic efficacy. As antibiotic resistance escalates, DEFb103A represents a promising template for next-generation antimicrobial agents, though clinical translation requires further pharmacokinetic and safety validation.
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