| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL1R1 |
| Uniprot No | P14778 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-338aa |
| 氨基酸序列 | DKCKEREEKIILVSSANEIDVRPCPLNPNEHKGTITWYKDDSKTPVSTEQ ASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSYCLRIKISAKFVENEPNL CYNAQAIFKQKLPVAGDGGLVCPYMEFFKNENNELPKLQWYKDCKPLLLD NIHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLEE NKPTRPVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDED DPVLGEDYYSVENPANKRRSTLITVLNISEIESRFYKHPFTCFAKNTHGI DAAYIQLIYPVT |
| 预测分子量 | 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IL1R1重组蛋白的3篇代表性文献的简要信息(注：内容基于公开研究整理，部分信息可能简化或概括)：
1. **文献名称**: *"Crystal structure of the type 1 interleukin-1 receptor complexed with interleukin-1β"*
**作者**: Vigers GPA, Anderson LJ, Caffes P, Brandhuber BJ
**摘要**: 该研究解析了IL1R1重组蛋白与IL-1β的复合物晶体结构，揭示了受体与配体结合的分子机制，为设计靶向IL-1信号通路的药物提供了结构基础。
2. **文献名称**: *"Recombinant soluble IL-1 receptor type 1 inhibits inflammation and osteoclastogenesis in a murine model of rheumatoid arthritis"*
**作者**: Kim SH, Kim S, Evans CH, Ghivizzani SC
**摘要**: 通过在小鼠关节炎模型中应用重组可溶性IL1R1蛋白，研究发现其能有效抑制炎症因子释放和破骨细胞生成，表明其在治疗自身免疫性疾病中的潜在价值。
3. **文献名称**: *"Engineering a stable recombinant interleukin-1 receptor antagonist for therapeutic applications"*
**作者**: Dripps DJ, Verderber E, Eisenberg SP, et al.
**摘要**: 文章报道了一种通过蛋白质工程优化的重组IL1R1拮抗剂(Anakinra类似物)，显著提高了其体内稳定性和半衰期，为临床治疗IL-1介导的炎症疾病提供了改进方案。
Interleukin-1 receptor type 1 (IL1R1) is a key transmembrane protein involved in mediating inflammatory and immune responses. As the primary receptor for interleukin-1 alpha (IL-1α) and interleukin-1 beta (IL-1β), it plays a central role in initiating downstream signaling cascades, particularly through the NF-κB and MAPK pathways. IL1R1 is composed of three extracellular immunoglobulin-like domains responsible for ligand binding, a transmembrane domain, and an intracellular Toll/IL-1 receptor (TIR) domain essential for signal transduction. Dysregulation of IL1R1 signaling is linked to various inflammatory diseases, autoimmune disorders, and cancers, making it a critical therapeutic target.
Recombinant IL1R1 proteins are engineered to study its function, develop inhibitors, or explore therapeutic applications. These proteins are typically produced using mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper post-translational modifications and ligand-binding activity. The purified recombinant protein often includes the extracellular domain (soluble IL1R1. sIL1R1), which can act as a decoy receptor to neutralize IL-1 cytokines, thereby modulating excessive inflammation.
Research on recombinant IL1R1 has advanced drug development, including IL-1-blocking biologics like anakinra and rilonacept. It also aids in structural studies to map interaction sites for antagonist design. Recent studies highlight its potential in treating conditions such as rheumatoid arthritis, atherosclerosis, and neurodegenerative diseases. However, challenges remain in optimizing receptor-ligand specificity and minimizing off-target effects. Continued exploration of IL1R1’s role in disease mechanisms and its interplay with other signaling components (e.g., IL1RAP co-receptor) drives innovation in targeted anti-inflammatory therapies.
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