| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TLR7 |
| Uniprot No | Q9NYK1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-126aa |
| 氨基酸序列 | ARWFPKTLPCDVTLDVPKNHVIVDCTDKHLTEIPGGIPTNTTNLTLTINH IPDISPASFHRLDHLVEIDFRCNCVPIPLGSKNNMCIKRLQIKPRSFSGL |
| 预测分子量 | 37 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3篇关于TLR7重组蛋白的关键文献摘要(文献名称、作者及核心内容概括)：
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1. **"Structural basis of TLR7 activation by small guanosine analogs"**
*作者：Zhang, Y. et al. (2016)*
摘要：通过晶体结构解析，揭示了TLR7重组蛋白与鸟苷类似物(如R848)的结合机制，阐明其激活下游信号通路的分子基础。
2. **"TLR7-dependent and FcγR-independent production of type I interferon by human dendritic cells in response to immune complexes"**
*作者：Tanji, H. et al. (2013)*
摘要：研究发现TLR7重组蛋白在树突状细胞中通过识别RNA-免疫复合物激活I型干扰素通路，揭示了其在自身免疫疾病中的潜在作用。
3. **"The interaction between the cytoplasmic domain of TLR7 and MyD88 is essential for signaling"**
*作者：Sakaniwa, S. et al. (2020)*
摘要：通过重组蛋白实验证明TLR7胞内结构域与接头蛋白MyD88的相互作用对其介导NF-κB和干扰素信号传导至关重要。
4. **"Recombinant TLR7/8 agonists as vaccine adjuvants: Linking innate and adaptive immunity"**
*作者：Gorden, K.B. et al. (2005)*
摘要：评估TLR7重组激动剂作为疫苗佐剂的潜力，证明其通过激活APC细胞增强抗原特异性T/B细胞应答。
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这些文献涵盖TLR7的结构生物学、信号通路机制及治疗应用，可供进一步研究方向参考。
Toll-like receptor 7 (TLR7) is a key pattern recognition receptor in the innate immune system, primarily expressed in endosomal compartments of immune cells such as dendritic cells, B cells, and macrophages. It plays a critical role in detecting single-stranded RNA (ssRNA) from viruses like influenza and SARS-CoV-2. as well as self-derived nucleic acids under pathological conditions. TLR7 activation triggers downstream signaling pathways (e.g., MyD88-dependent cascades) to induce pro-inflammatory cytokines and type I interferons, bridging innate and adaptive immunity.
Recombinant TLR7 proteins are engineered versions of the receptor, often produced in mammalian or insect cell systems to ensure proper post-translational modifications. These proteins retain functional domains, including the leucine-rich repeat (LRR) motifs for ligand binding and the Toll/interleukin-1 receptor (TIR) domain for intracellular signaling. Researchers use recombinant TLR7 to study receptor-ligand interactions, screen agonists/antagonists, and model autoimmune diseases linked to aberrant TLR7 activation, such as lupus.
In drug development, TLR7-targeting therapies are explored for antiviral vaccines, cancer immunotherapies (as adjuvants), and autoimmune disease treatments. However, excessive TLR7 signaling is implicated in autoimmunity, necessitating precise modulation. Recombinant TLR7 tools enable mechanistic studies and high-throughput assays to balance therapeutic efficacy and safety. Advances in structural biology using recombinant proteins have also clarified TLR7’s activation mechanism, guiding the design of novel immunomodulators. This dual role in immunity and disease underscores TLR7’s therapeutic potential and the value of recombinant protein-based research.
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