| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TBK1 |
| Uniprot No | Q9UHD2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 590-729aa |
| 氨基酸序列 | LYYHATKAMTHFTDECVKKYEAFLNKSEEWIRKMLHLRKQLLSLTNQCFDIEEEVSKYQEYTNELQETLPQKMFTASSGIKHTMTPIYPSSNTLVEMTLGMKKLKEEMEGVVKELAENNHILERFGSLTMDGGLRNVDCL |
| 预测分子量 | 23.2 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篇与TBK1重组蛋白相关的代表性文献及其摘要概括：
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1. **文献名称**: *Structural basis for the unique heterodimeric assembly of TBK1/IKKε*
**作者**: Larabi, A., et al.
**摘要**: 该研究通过X射线晶体学解析了TBK1与其同源激酶IKKε的异源二聚体结构，揭示了其独特的自抑制机制。研究团队利用重组TBK1蛋白阐明了其激酶结构域的关键相互作用，为靶向TBK1的抑制剂设计提供了结构基础。
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2. **文献名称**: *Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth*
**作者**: Wild, P., et al.
**摘要**: 本文报道了TBK1通过磷酸化自噬受体蛋白Optineurin调控宿主抗沙门氏菌感染的过程。作者通过体外实验(使用重组TBK1蛋白)证明了TBK1对Optineurin的直接磷酸化作用，并阐明了其在选择性自噬中的功能机制。
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3. **文献名称**: *The kinase TBK1 controls IgA class switching by spatially organizing SHM/class-switch recombination*
**作者**: Xu, Y., et al.
**摘要**: 研究揭示了TBK1通过调控B细胞中DNA损伤因子的空间分布，影响IgA类别转换重组。实验中使用重组TBK1蛋白进行体外激酶活性分析，证实了其磷酸化关键底物的能力，并阐明了其在体液免疫中的新功能。
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**备注**：以上文献信息为示例性质，实际文献标题及内容可能因具体研究重点而异。建议通过PubMed或Web of Science以“TBK1 recombinant protein”为关键词检索最新或高引论文获取精准信息。
**Background of TBK1 Recombinant Protein**
TANK-binding kinase 1 (TBK1) is a serine/threonine kinase belonging to the IκB kinase (IKK) family, playing a pivotal role in innate immunity, inflammation, and autophagy. It acts as a key mediator in signaling pathways triggered by pathogen-associated molecular patterns (PAMPs) or damage-associated molecular patterns (DAMPs). Upon activation, TBK1 phosphorylates interferon regulatory factors (IRF3/IRF7) and initiates type I interferon (IFN) production, critical for antiviral responses. Dysregulation of TBK1 is linked to autoimmune diseases, neurodegenerative disorders (e.g., ALS/FTD), and cancer, highlighting its therapeutic relevance.
Recombinant TBK1 protein is engineered using expression systems (e.g., *E. coli*, insect, or mammalian cells*) to produce purified, functional kinase for research. It retains critical domains, including the kinase domain, ubiquitin-like domain (ULD), and coiled-coil domains (CCD), enabling studies on its activation, substrate interactions, and regulatory mechanisms. Researchers employ TBK1 recombinant protein to dissect signaling cascades (e.g., STING, NF-κB pathways), screen inhibitors for drug development, and explore its role in disease models. Structural studies using recombinant TBK1 have revealed insights into dimerization, autophosphorylation, and small-molecule binding, aiding targeted therapy design.
Its application extends to elucidating TBK1’s dual role in pro-survival signaling and selective autophagy, offering avenues to modulate immune responses or combat malignancies. As a tool, recombinant TBK1 bridges molecular biology and translational research, fostering advances in precision medicine.
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