| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | hfb1 |
| Uniprot No | P52754 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-97aa |
| 氨基酸序列 | SNGNGNVCPPGLFSNPQCCATQVLGLIGLDCKVPSQNVYDGTDFRNVCAKTGAQPLCCVAPVAGQALLCQTAVGA |
| 预测分子量 | 23.5 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HFB1重组蛋白的3篇参考文献示例(注：文献为示例性质，建议通过学术数据库检索最新研究)：
1. **《Efficient expression and characterization of a hydrophobin HFB1 from Trichoderma reesei in Pichia pastoris》**
- 作者：Wang, X., et al.
- 摘要：研究利用毕赤酵母系统高效表达重组HFB1蛋白，优化发酵条件后获得高产量，并通过表面活性实验证实其自组装形成两亲性膜的能力，为工业涂层应用提供基础。
2. **《Self-assembly of recombinant HFB1 hydrophobin as a tool for hydrophobic surface modification》**
- 作者：Linder, M.B., et al.
- 摘要：通过大肠杆菌表达重组HFB1.纯化后证明其可在疏水表面形成稳定单层膜，显著改变材料亲水性，应用于生物传感器和医疗材料表面功能化。
3. **《Biotechnological applications of hydrophobin HFB1: Nanoparticle stabilization and drug delivery》**
- 作者：Zhang, Y., et al.
- 摘要：重组HFB1蛋白包载疏水性药物形成纳米颗粒，实验显示其能增强药物溶解度和靶向性，在小鼠模型中验证了抗肿瘤效果，突显其在纳米医药中的潜力。
建议通过PubMed或Web of Science检索真实文献，关键词包括“HFB1 recombinant”、“hydrophobin expression”等。
**Background of HFB1 Recombinant Protein**
Hydrophobins are small, cysteine-rich proteins predominantly produced by filamentous fungi, playing critical roles in fungal development and environmental interactions. Among these, *HFB1* (Hydrophobin Family B member 1), derived from species like *Trichoderma reesei*, has garnered significant attention due to its unique amphiphilic structure and self-assembly properties. HFB1 is classified as a Class II hydrophobin, characterized by its ability to form stable, amphipathic monolayers at hydrophobic-hydrophilic interfaces. This structural adaptability arises from its eight conserved cysteine residues, which form disulfide bonds to stabilize a rigid hydrophobic patch on one surface and a hydrophilic region on the other.
Recombinant HFB1 is produced via heterologous expression systems, such as *Escherichia coli* or yeast, enabling scalable and controlled production. Its recombinant form retains the native protein's functional properties, including high thermal stability, surfactant activity, and the capacity to modify surface wettability. These features make HFB1 valuable in biotechnological and industrial applications. For instance, it serves as a bioemulsifier, stabilizes foams or emulsions, and facilitates hydrophobic drug delivery by enhancing solubility. Additionally, HFB1-coated surfaces are explored for antifouling coatings or biocompatible material engineering.
Research also highlights its potential in sustainable technologies, such as biosensors or renewable energy devices, where surface modification is crucial. Despite its promise, challenges in recombinant production—such as low yields or improper folding—require optimization of expression conditions and purification strategies. Ongoing studies aim to unravel structure-function relationships and expand its applicability, positioning HFB1 as a versatile tool in both fundamental research and applied sciences.
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