| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | csgB |
| Uniprot No | P0ABK7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-151aa |
| 氨基酸序列 | AGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR |
| 预测分子量 | 16KDa |
| 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CsgB重组蛋白的3篇参考文献示例：
1. **"Structural and functional characterization of the curli subunit CsgB"**
*作者：Collinson, S. K. et al. (1999)*
摘要：研究通过重组表达纯化CsgB蛋白，分析其在curli纤维组装中的关键作用，证实CsgB作为成核蛋白促进CsgA单体聚合的分子机制。
2. **"Recombinant CsgB production in E. coli for biofilm engineering applications"**
*作者：Wang, X. et al. (2016)*
摘要：开发了一种高效重组表达CsgB的方法，利用His标签纯化技术，证明其在体外调控生物膜形成及生物材料开发的潜力。
3. **"Self-assembly of engineered recombinant CsgB protein into functional amyloid nanostructures"**
*作者：Zhong, C. et al. (2018)*
摘要：通过基因工程改造CsgB，实现其在大肠杆菌中的可溶性表达，并证明重组蛋白可在体外自组装为稳定纳米纤维，用于生物传感器构建。
注：以上文献信息为示例，实际引用需根据具体论文核实。建议通过PubMed或Web of Science以“CsgB recombinant”为关键词检索最新研究。
**Background of CsgB Recombinant Protein**
CsgB, a key structural component of bacterial curli fibers, is encoded by the *csgB* gene within the *csgBAC* operon in *Escherichia coli*. Curli are amyloid-like extracellular protein fibers critical for biofilm formation, host-cell adhesion, and environmental persistence in many Gram-negative bacteria. CsgB acts as a nucleator protein, initiating the polymerization of the major curli subunit CsgA into functional amyloid fibrils. Unlike pathogenic amyloids, curli fibers serve as functional structural elements, contributing to microbial community organization and resilience.
Recombinant CsgB is produced via heterologous expression systems, often in *E. coli*, to study its nucleation mechanism or engineer bio-inspired materials. Its ability to self-assemble into stable amyloid structures has attracted interest in nanotechnology and biomedicine. For instance, CsgB-based scaffolds are explored for drug delivery, tissue engineering, or biosensors due to their high stability and programmable assembly. Additionally, CsgB recombinant protein aids in dissecting amyloidogenesis pathways, offering insights into both functional and disease-associated amyloid formation.
Research also leverages CsgB to develop anti-biofilm strategies, targeting its role in biofilm infrastructure. Structural studies using recombinant CsgB, including X-ray crystallography and NMR, reveal conserved amyloidogenic domains and nucleation interfaces, guiding synthetic biology applications. Despite its prokaryotic origin, CsgB’s amyloid properties parallel those of eukaryotic proteins, making it a simplified model for studying amyloid-related diseases like Alzheimer’s.
Overall, CsgB recombinant protein bridges microbiology, materials science, and medicine, highlighting its versatility as a tool for both basic research and applied biotechnology.
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