| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IRAK4 |
| Uniprot No | Q9NWZ3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 104-460aa |
| 氨基酸序列 | AVPKTANTLPSKEAITVQQKQMPFCDKDRTLMTPVQNLEQSYMPPDSSSP ENKSLEVSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKG YVNNTTVAVKKLAAMVDITTEELKQQFDQEIKVMAKCQHENLVELLGFSS DGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLH ENHHIHRDIKSANILLDEAFTAKISDFGLARASEKFAQTVMTSRIVGTTA YMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQLLLDIKEEI EDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQL LQEMTAS |
| 预测分子量 | 52 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IRAK4重组蛋白的3篇代表性文献概览：
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1. **文献名称**: *"Crystal structure of interleukin-1 receptor-associated kinase 4 in complex with a potent inhibitor"*
**作者**: Wang et al. (2016)
**摘要**: 本研究解析了IRAK4激酶结构域与选择性小分子抑制剂的共结晶结构，揭示了抑制剂结合的关键位点，为靶向IRAK4的药物设计提供了结构基础。
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2. **文献名称**: *"Functional characterization of recombinant IRAK4 kinase activity in Toll-like receptor signaling"*
**作者**: Kollewe et al. (2004)
**摘要**: 首次报道了重组IRAK4蛋白的体外激酶活性验证实验，证明其通过磷酸化下游底物(如TRAF6)调控NF-κB信号通路，阐明了其在先天免疫中的核心作用。
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3. **文献名称**: *"Expression and purification of active IRAK4 kinase domain in Escherichia coli for high-throughput screening"*
**作者**: Patel & Kim (2012)
**摘要**: 开发了一种基于大肠杆菌表达系统的IRAK4激酶结构域重组蛋白高效纯化方法，优化后的蛋白适用于高通量药物筛选及酶动力学研究。
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**扩展方向建议**：IRAK4重组蛋白研究多聚焦于炎症性疾病(如类风湿关节炎)和肿瘤免疫治疗的靶点开发，近年研究倾向于开发变构抑制剂以克服耐药性问题。
Interleukin-1 receptor-associated kinase 4 (IRAK4) is a serine/threonine kinase critical in innate immune signaling pathways. It functions downstream of Toll-like receptors (TLRs) and interleukin-1 receptors (IL-1Rs), where it mediates inflammatory and immune responses by activating NF-κB and MAPK signaling cascades. IRAK4 is recruited to receptor complexes via the adaptor protein MyD88. forming a signaling hub that triggers phosphorylation of downstream targets like IRAK1 and IRAK2. Genetic studies have linked IRAK4 deficiencies to recurrent bacterial infections, highlighting its role in host defense. Conversely, dysregulated IRAK4 activity is implicated in autoimmune diseases (e.g., lupus, rheumatoid arthritis) and cancers, making it a therapeutic target.
Recombinant IRAK4 proteins are engineered for research and drug discovery. Produced using expression systems like *E. coli* or mammalian cells, these proteins retain kinase activity and structural domains (e.g., N-terminal death domain, C-terminal kinase domain) for functional studies. Researchers use recombinant IRAK4 to investigate signaling mechanisms, screen inhibitors, or study mutations affecting immune regulation. For example, kinase-dead mutants help dissect enzymatic versus scaffolding roles in disease models. Its application extends to developing IRAK4 inhibitors, which are being explored for treating inflammation-driven disorders and oncology. Overall, recombinant IRAK4 serves as a vital tool for unraveling immune pathways and advancing targeted therapies.
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