| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TLR5 |
| Uniprot No | O60602 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 517-634aa |
| 氨基酸序列 | LPPGVFSHLTALRGLSLNSNRLTVLSHNDLPANLEILDISRNQLLAPNPD VFVSLSVLDITHNKFICECELSTFINWLNHTNVTIAGPPADIYCVYPDSF SGVSLFSLSTEGCDEEEV |
| 预测分子量 | 39 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TLR5重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**：*Structural Basis of TLR5-Flagellin Recognition and Signaling*
**作者**：Alexei V. Letarsec et al.
**摘要**：通过X射线晶体学解析了TLR5重组蛋白与细菌鞭毛蛋白(flagellin)的复合物结构，揭示了TLR5通过其N端结构域特异性识别flagellin的D1结构域，阐明了TLR5激活的分子机制。
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2. **文献名称**：*Recombinant TLR5 Agonist as a Potent Vaccine Adjuvant*
**作者**：Kai-Lin Hong et al.
**摘要**：研究证明重组TLR5蛋白与flagellin片段结合后，可显著增强抗原呈递细胞(APC)的活化，并促进Th1/Th17免疫应答，提出其作为新型疫苗佐剂的潜在应用价值。
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3. **文献名称**：*TLR5-Dependent Regulation of Intestinal Inflammation*
**作者**：Jennifer K. Grenz et al.
**摘要**：利用重组TLR5蛋白和小鼠模型，发现TLR5通过调控肠道上皮细胞NF-κB通路维持黏膜屏障完整性，其功能失调与炎症性肠病(IBD)的发病机制密切相关。
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**备注**：以上文献信息为虚拟示例，实际研究需通过PubMed或Web of Science等平台检索。建议结合关键词“TLR5 recombinant protein”或“TLR5 signaling”查找近期高引用论文。
**Background of TLR5 Recombinant Protein**
Toll-like receptor 5 (TLR5) is a transmembrane protein belonging to the Toll-like receptor family, which plays a pivotal role in the innate immune system by detecting pathogen-associated molecular patterns (PAMPs). Specifically, TLR5 recognizes bacterial flagellin, a major structural protein of bacterial flagella, and initiates immune responses against flagellated pathogens like *Salmonella* and *Escherichia coli*. Upon ligand binding, TLR5 activates downstream signaling pathways (e.g., NF-κB and MAPK), triggering the production of pro-inflammatory cytokines and chemokines to combat infections.
Recombinant TLR5 proteins are engineered versions of the native receptor, typically produced using heterologous expression systems such as *E. coli*, insect cells, or mammalian cell lines (e.g., HEK293). These proteins retain the ligand-binding extracellular leucine-rich repeat (LRR) domain, which is critical for flagellin interaction, while the transmembrane and cytoplasmic Toll/interleukin-1 receptor (TIR) domains may be modified or truncated for solubility and purification purposes. Recombinant TLR5 is often fused with tags (e.g., Fc, His, or GST) to facilitate detection, isolation, or functional studies.
TLR5 recombinant proteins are widely utilized in biomedical research to study innate immunity mechanisms, screen for TLR5 agonists/antagonists, and develop therapeutics or vaccine adjuvants. For instance, they serve as tools to investigate TLR5-mediated signaling dysregulation in autoimmune diseases, chronic inflammation, or cancer. Additionally, recombinant TLR5 has been explored in preclinical models to enhance anti-tumor immunity or improve antibacterial responses. Recent studies also highlight its potential in designing flagellin-based vaccines, leveraging TLR5’s ability to bridge innate and adaptive immunity.
Despite advancements, challenges remain, including optimizing recombinant TLR5 stability and mimicking native post-translational modifications. Ongoing research aims to refine production techniques and expand therapeutic applications, underscoring TLR5’s significance in immunology and drug development.
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