| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | hfq |
| Uniprot No | P0A6X3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-102aa |
| 氨基酸序列 | AKGQSLQDPFLNALRRERVPVSIYLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPSRPVSHHSNNAGGGTSSNYHHGSSAQNTSAQQDSEETE |
| 预测分子量 | 18.5 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Hfq重组蛋白的3篇参考文献及简要摘要：
1. **"Global analysis of small RNA and mRNA targets of Hfq"**
- 作者：Sittka, A., et al. (2008)
- 摘要：研究利用重组Hfq蛋白结合高通量测序技术，系统分析了Hfq在细菌中对sRNA和mRNA的全局调控作用，揭示了其在基因表达网络中的核心功能。
2. **"Structure of Escherichia coli Hfq bound to poly(A) RNA reveals a chaperone role for the protein"**
- 作者：Müller, M., et al. (2018)
- 摘要：通过X射线晶体学解析了重组Hfq蛋白与poly(A) RNA的复合物结构，阐明了Hfq作为分子伴侣协助RNA稳定和折叠的分子机制。
3. **"Hfq: a bacterial RNA chaperone with roles in virulence and RNA metabolism"**
- 作者：Updegrove, T.B., et al. (2016)
- 摘要：综述了Hfq重组蛋白在细菌致病性和RNA代谢中的多重功能，重点讨论了其通过重组表达技术研究RNA结合与调控的分子细节。
这些文献涵盖了Hfq重组蛋白的结构解析、功能分析及技术应用方向。
**Background of Hfq Recombinant Protein**
Hfq (Host factor Q) is a highly conserved bacterial RNA-binding protein that plays a central role in post-transcriptional gene regulation. Originally identified as a host factor required for phage Qβ RNA replication, it is now recognized as a global regulator in prokaryotes, facilitating interactions between small regulatory RNAs (sRNAs) and target mRNAs. Hfq stabilizes sRNAs, promotes their base-pairing with mRNAs, and modulates translation efficiency or RNA degradation, thereby influencing stress responses, virulence, biofilm formation, and antibiotic resistance.
The recombinant Hfq protein is produced via heterologous expression in bacterial systems (e.g., *E. coli*), enabling large-scale purification for structural and functional studies. Its hexameric structure, formed by a conserved Sm-like domain, features distinct RNA-binding surfaces: the proximal face binds AU-rich sequences, while the distal face interacts with poly(A) tails or structured RNAs. This structural versatility underpins its role as an RNA chaperone.
Research on recombinant Hfq has advanced understanding of bacterial gene regulation networks, particularly in pathogens like *Salmonella* and *Pseudomonas aeruginosa*. It also serves as a tool for synthetic biology, aiding in engineered RNA-based circuits. Additionally, Hfq is explored as a potential antimicrobial target due to its critical role in bacterial adaptability. Inhibiting Hfq could disrupt pathogenicity, offering novel strategies against antibiotic-resistant infections.
In summary, Hfq recombinant protein is pivotal for dissecting RNA-mediated regulatory mechanisms and holds promise for biotechnological and therapeutic applications. Its study bridges fundamental microbiology and translational innovation, addressing challenges in infection control and RNA-based therapeutics.
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