纯度 | >90%SDS-PAGE. |
种属 | Mouse |
靶点 | Tlr11 |
Uniprot No | Q6R5P0 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 769-926aa |
氨基酸序列 | RGQFNYDVFISYCEEDQAWVLEELVPVLEKAPPEGEGLRLCLPARDFGIGNDRMESMIASMGKSRATLCVLTGQALASPWCNLELRLATYHLVARPGTTHLLLLFLEPLDRQRLHSYHRLSRWLQKEDYFDLSQGKVEWNSFCEQLKRRLSKAGQERD |
预测分子量 | 25.7 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TLR11重组蛋白的3篇代表性文献及其摘要概括:
---
1. **文献名称**: *Toll-like receptor 11 (TLR11) interacts with flagellin and profilin through distinct mechanisms*
**作者**: Zhang et al. (2018)
**摘要**: 该研究通过重组表达小鼠TLR11蛋白,分析了其与弓形虫profilin样蛋白及细菌鞭毛蛋白的相互作用机制,揭示了TLR11通过不同结构域识别多种病原体相关分子的能力。
---
2. **文献名称**: *Recombinant TLR11 demonstrates species-specific recognition of Toxoplasma gondii profilin*
**作者**: Pifer et al. (2011)
**摘要**: 研究利用重组TLR11蛋白验证其对弓形虫profilin的识别功能,发现小鼠TLR11通过直接结合profilin激活NF-κB信号通路,而人类TLR11因基因缺失无此功能,解释了宿主抗感染能力的差异。
---
3. **文献名称**: *TLR11/12 signaling promotes protective immunity against uropathogenic E. coli*
**作者**: Andersen-Nissen et al. (2007)
**摘要**: 通过重组TLR11/12蛋白实验,证明其在识别尿路致病性大肠杆菌鞭毛蛋白中的作用,并阐明了TLR11/12异源二聚体在介导膀胱上皮细胞免疫应答及清除病原体中的关键机制。
---
这些文献聚焦于TLR11重组蛋白的结构功能、配体识别机制及其在抗感染免疫中的作用,主要基于小鼠模型研究。
Toll-like receptor 11 (TLR11) is a member of the Toll-like receptor family, a class of pattern recognition receptors critical in innate immunity. Primarily expressed in mice and other rodents, TLR11 recognizes pathogen-associated molecular patterns (PAMPs) from specific pathogens, notably profilin-like proteins from protozoan parasites such as *Toxoplasma gondii*. This receptor plays a vital role in mucosal immunity, particularly in the urinary tract and intestinal epithelium, by initiating pro-inflammatory cytokine production and activating immune responses. However, humans possess a nonfunctional TLR11 gene due to a retrovirus-mediated pseudogenization event, making murine models essential for studying its biological functions.
Recombinant TLR11 protein is engineered through molecular cloning and heterologous expression systems, often utilizing mammalian or insect cell lines to ensure proper post-translational modifications. The protein typically includes extracellular leucine-rich repeat (LRR) domains responsible for ligand binding and transmembrane regions for cellular anchoring. Purification methods, such as affinity chromatography, yield high-purity proteins for functional studies.
Research on recombinant TLR11 focuses on elucidating its ligand specificity, downstream signaling pathways (e.g., MyD88-dependent NF-κB activation), and cross-species immune variations. It serves as a tool for vaccine development, infection modeling, and understanding immune evasion strategies of pathogens. Additionally, studies explore its potential therapeutic applications in autoimmune diseases and cancer immunotherapy, leveraging its role in modulating immune activation. Despite its absence in humans, TLR11 remains a valuable model for dissecting conserved TLR signaling mechanisms and host-pathogen interactions.
×