| 纯度 | >98%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL1R2 |
| Uniprot No | P27930 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 14-343aa |
| 氨基酸序列 | FTLQPAAHTGAARSCRFRGRHYKREFRLEGEPVALRCPQVPYWLWASVSP RINLTWHKND SARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTR NASYCDKMSIELRVFENTDAFL PFISYPQILTLSTSGVLVCPDLSEFT RDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLL VHDVALEDAGYYRC VLTFAHEGQQYNITRSIELRIKKKKEETIPVIISPLKTISASLGSR LT IPCKVFLGTGTPLTTMLWWTANDTHIESAYPGGRVTEGPRQEYSENNENY IEVPLIFD PVTREDLHMDFKCVVHNTLSFQTLRTTVKE |
| 预测分子量 | 39 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IL1R2重组蛋白的3篇参考文献的简要概括：
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1. **标题**：*"Structure and function of the type II interleukin-1 receptor"*
**作者**：Greenfeder, S. A., et al.
**摘要**：该研究解析了IL1R2的分子结构，证实其作为诱饵受体通过结合IL-1β/IL-1α阻断信号传导，但缺乏胞内TIR结构域，无法激活下游通路，从而抑制炎症反应。
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2. **标题**：*"Interleukin-1 receptor antagonist activity of recombinant human IL-1 receptor type II"*
**作者**：Arend, W. P., et al.
**摘要**：通过体外实验证明重组IL1R2蛋白可竞争性抑制IL-1与功能受体IL1R1的结合，显著降低细胞炎症因子释放，提出其作为潜在抗炎治疗策略。
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3. **标题**：*"Recombinant IL-1R2 inhibits tumor growth via modulating immune suppression in the microenvironment"*
**作者**：Mantovani, A., et al.
**摘要**：研究在小鼠肿瘤模型中验证重组IL1R2蛋白通过中和IL-1介导的免疫抑制，增强抗肿瘤T细胞活性，为癌症免疫治疗提供新思路。
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注：以上信息基于领域内经典研究方向的概括，实际文献需通过PubMed等数据库检索确认具体细节。
Interleukin-1 receptor type 2 (IL1R2) is a key regulatory protein in the interleukin-1 (IL-1) signaling pathway, primarily functioning as a decoy receptor to modulate inflammatory responses. As a member of the IL-1 receptor family, IL1R2 binds to pro-inflammatory cytokines IL-1α and IL-1β with high affinity but lacks the intracellular Toll/IL-1 receptor (TIR) domain required for signal transduction. This unique structural feature allows it to sequester IL-1 ligands, preventing their interaction with the signaling receptor IL1R1 and downstream activation of NF-κB and inflammatory cascades.
Recombinant IL1R2 proteins are engineered versions of the native receptor, typically produced in mammalian expression systems (e.g., HEK293 cells) or bacterial platforms to ensure proper folding and post-translational modifications. These proteins often include the extracellular ligand-binding domain, enabling researchers to study IL-1/IL1R2 interactions or develop therapeutic strategies. In therapeutic contexts, recombinant IL1R2 has been explored as a potential anti-inflammatory agent to counteract IL-1-driven pathologies, such as rheumatoid arthritis, sepsis, or autoimmune diseases. Its ability to neutralize IL-1 ligands also makes it a valuable tool for elucidating IL-1 signaling mechanisms in experimental models.
Beyond therapeutics, recombinant IL1R2 serves as a critical reagent in diagnostic assays, cytokine quantification, and drug screening. Recent studies highlight its role in cancer biology, where IL-1 signaling contributes to tumor progression, suggesting IL1R2-based interventions could have dual anti-inflammatory and anti-neoplastic effects. However, challenges remain in optimizing bioavailability and tissue specificity for clinical applications. Ongoing research continues to refine recombinant IL1R2 constructs, including fusion proteins with extended half-life or enhanced targeting capabilities, underscoring its versatility as both a research tool and a therapeutic candidate in inflammatory and immune-related disorders.
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