| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | hfb2 |
| Uniprot No | P79073 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 16-86aa |
| 氨基酸序列 | AVCPTGLFSNPLCCATNVLDLIGVDCKTPTIAVDTGAIFQAHCASKGSKPLCCVAPVADQALLCQKAIGTF |
| 预测分子量 | 12.7kDa |
| 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HFB2重组蛋白的3篇参考文献示例：
1. **文献名称**: Expression and characterization of recombinant hydrophobin HFB2 in Pichia pastoris
**作者**: Wang et al.
**摘要**: 研究利用毕赤酵母系统高效表达HFB2重组蛋白，优化发酵条件后获得高纯度蛋白，证实其表面活性及自组装成纳米膜的能力，在生物材料涂层领域具应用潜力。
2. **文献名称**: Functionalization of nanoparticles using HFB2 hydrophobin for drug delivery
**作者**: Smith et al.
**摘要**: 通过大肠杆菌重组表达HFB2蛋白，将其用于修饰脂质纳米颗粒表面，显著提升疏水药物负载率及细胞靶向性，为肿瘤靶向治疗提供新策略。
3. **文献名称**: Structural stability of HFB2 under extreme pH and temperature conditions
**作者**: Zhang & Li
**摘要**: 分析重组HFB2蛋白在极端pH(2-12)及高温(80℃)下的结构稳定性，发现其β-桶状构象高度保守，证实其在工业酶固定化中的耐候性优势。
注：以上文献信息为示例性质，实际研究中建议通过PubMed或Web of Science检索最新论文。HFB2研究热点集中在异源表达优化、界面活性机制及生物医学应用等领域。
HFB2. a Class II hydrophobin, is a small fungal protein (7-15 kDa) renowned for its exceptional surface-active properties. Naturally produced by filamentous fungi like Trichoderma species, these amphipathic proteins play crucial ecological roles in spore dispersal and fungal-host interactions by reducing water surface tension. Their unique structural signature features eight conserved cysteine residues forming four disulfide bonds, creating a rigid globular core with distinct hydrophobic and hydrophilic patches.
The recombinant form of HFB2 is engineered through heterologous expression systems such as *E. coli* or *Pichia pastoris*, enabling scalable production for biotechnological applications. This bioengineering approach allows for molecular modifications like fusion tags or functional domain incorporation while preserving the protein's innate ability to self-assemble at interfaces. When exposed to hydrophilic-hydrophobic boundaries, HFB2 undergoes structural rearrangement, forming stable monolayers with remarkable mechanical strength and thermal stability (up to 80°C).
Biomedical and industrial interest in recombinant HFB2 stems from its dual functionality: It can reverse surface wettability, creating biocompatible coatings for medical implants or converting hydrophobic materials like plastics into water-dispersible forms. In drug delivery systems, its film-forming capacity enables nanoparticle stabilization and controlled payload release. Emerging applications include biosensor interfaces, antimicrobial coatings, and tissue engineering scaffolds capitalizing on its non-immunogenic nature.
Current research focuses on optimizing expression yields and functionalizing HFB2 through protein engineering, addressing challenges in large-scale production and application-specific performance tuning. Its eco-friendly profile and multifunctional characteristics position recombinant HFB2 as a sustainable alternative to synthetic surfactants in green chemistry initiatives.
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