| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TOLLIP |
| Uniprot No | Q9H0E2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-274aa |
| 氨基酸序列 | MATTVSTQRGPVYIGELPQDFLRITPTQQQRQVQLDAQAAQQLQYGGAVG TVGRLNITVVQAKLAKNYGMTRMDPYCRLRLGYAVYETPTAHNGAKNPRW NKVIHCTVPPGVDSFYLEIFDERAFSMDDRIAWTHITIPESLRQGKVEDK WYSLSGRQGDDKEGMINLVMSYALLPAAMVMPPQPVVLMPTVYQQGVGYV PITGMPAVCSPGMVPVALPPAAVNAQPRCSEEDLKAIQDMFPNMDQEVIR SVLEAQRGNK DAAINSLLQMGEEPVEHHHHHH |
| 预测分子量 | 31 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TOLLIP重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*"Tollip, a novel component of the IL-1RI pathway, links IRAK to the IL-1 receptor"*
**作者**：Burns, K., et al.
**摘要**：该研究通过重组TOLLIP蛋白的体外实验，揭示其作为IL-1受体信号通路的关键适配蛋白，与IRAK激酶相互作用并调控炎症反应的负反馈机制，表明TOLLIP可能通过抑制TLR/IL-1R信号通路限制过度免疫反应。
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2. **文献名称**：*"Structural basis for the interaction between Tollip and Tom1 and implications for the regulation of endosomal trafficking"*
**作者**：Katoh, Y., et al.
**摘要**：研究利用大肠杆菌表达系统获得重组TOLLIP蛋白，结合X射线晶体学解析其CUE结构域与Tom1蛋白的结合模式，揭示了TOLLIP在内吞体分选和膜运输中的分子机制，为相关疾病靶点提供结构基础。
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3. **文献名称**：*"Tollip modulates host autophagy to restrict intracellular Mycobacterium tuberculosis replication"*
**作者**：Chen, Z., et al.
**摘要**：通过表达纯化的重组TOLLIP蛋白进行功能实验，发现其通过促进自噬体形成增强宿主细胞对结核分枝杆菌的清除能力，证实TOLLIP在自噬相关通路中的调控作用及其抗感染潜力。
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以上文献涵盖了TOLLIP在信号通路调控、结构生物学及宿主防御中的功能研究，均涉及重组蛋白的表达与应用。
Toll-interacting protein (TOLLIP) is a ubiquitously expressed adaptor protein involved in modulating innate immune responses and membrane trafficking processes. It was initially identified as a negative regulator of Toll-like receptor (TLR) signaling pathways, which are critical for detecting pathogen-associated molecular patterns (PAMPs) and initiating inflammatory responses. TOLLIP interacts directly with key TLR signaling components, including interleukin-1 receptor-associated kinase 1 (IRAK1) and myeloid differentiation primary response 88 (MyD88), to suppress excessive activation of NF-κB and pro-inflammatory cytokine production. This regulatory mechanism helps prevent hyperinflammatory conditions and maintains immune homeostasis.
Structurally, TOLLIP contains an N-terminal C2 domain that binds phospholipids and membranes, a central conserved region for protein interactions, and a C-terminal coupling of ubiquitin to endoplasmic reticulum degradation (CUE) domain that facilitates ubiquitin binding. These domains enable TOLLIP to participate in endosomal sorting, autophagy, and receptor turnover. Notably, it collaborates with Tom1 (Target of Myb1) to mediate clathrin-dependent trafficking of ubiquitinated cargo, linking immune regulation to vesicular transport.
Recombinant TOLLIP proteins are engineered for in vitro studies to dissect its molecular interactions, post-translational modifications (e.g., phosphorylation, ubiquitination), and structural dynamics. Researchers utilize these purified proteins in assays like co-immunoprecipitation, surface plasmon resonance, or crystallography to map binding partners and resolve 3D conformations. Dysregulation of TOLLIP has been implicated in chronic inflammatory diseases, cancer progression, and neurodegenerative disorders like Alzheimer’s, where its role in clearing protein aggregates is of particular interest. Recombinant TOLLIP thus serves as a vital tool for exploring therapeutic strategies targeting TLR pathways or membrane trafficking defects.
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