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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL37 |
| Uniprot No | Q9NZH6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 46-218aa |
| 氨基酸序列 | VHTSPKVKNLNPKKFSIHDQDHKVLVLDSGNLIAVPDKNYIRPEIFFALA SSLSSASAEKGSPILLGVSKGEFCLYCDKDKGQSHPSLQLKKEKLMKLAA QKESARRPFIFYRAQVGSWNMLESAAHPGWFICTSCNCNEPVGVTDKFEN RKHIEFSFQPVCKAEMSPSEVSD |
| 预测分子量 | 19 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IL-37重组蛋白的3篇参考文献及摘要内容概述：
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1. **文献名称**: *IL-37 is a fundamental inhibitor of innate immunity*
**作者**: Nold, M. F. et al.
**摘要**: 该研究首次揭示了IL-37作为天然免疫系统的关键抑制因子，通过抑制TLR通路和炎症小体活性减少促炎细胞因子(如IL-1β、TNF-α)的产生，并在脓毒症模型中证明重组IL-37可显著减轻炎症反应。
2. **文献名称**: *Recombinant IL-37 suppresses lung inflammation in mice with allergic asthma*
**作者**: Li, C. et al.
**摘要**: 研究利用重组IL-37蛋白治疗小鼠过敏性哮喘，发现其通过抑制Th2细胞分化和减少嗜酸性粒细胞浸润缓解气道炎症，为IL-37在过敏性疾病中的治疗潜力提供了实验依据。
3. **文献名称**: *IL-37 requires the receptors IL-18Rα and IL-1R8 to exert its anti-inflammatory function*
**作者**: Boraschi, D. et al.
**摘要**: 该研究阐明了重组IL-37蛋白的抗炎机制，证实其依赖IL-18Rα和IL-1R8受体复合物激活下游信号通路，从而抑制NF-κB和MAPK通路，为开发基于IL-37的炎症性疾病疗法提供了分子机制支持。
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以上文献均聚焦IL-37重组蛋白的生物学功能及治疗潜力，涵盖基础机制到疾病模型的应用研究。
Interleukin-37 (IL-37), a member of the interleukin-1 (IL-1) cytokine family, is a potent anti-inflammatory cytokine discovered in the early 2000s. Unlike most IL-1 family members that promote inflammation, IL-37 functions as a natural suppressor of innate and adaptive immune responses. It is expressed in humans and certain primates but lacks a murine homolog, complicating in vivo studies. IL-37 exists in five splice variants (IL-37a-e), with IL-37b being the most biologically active isoform. It is produced as a precursor protein that requires caspase-1-mediated cleavage for activation, linking it to inflammasome regulation.
Recombinant IL-37 refers to the engineered protein produced via heterologous expression systems, typically in *E. coli* or mammalian cells. This technology enables large-scale production for research and therapeutic exploration. Structurally, recombinant IL-37 retains the conserved β-trefoil fold of IL-1 family cytokines but uniquely binds to IL-18Rα and recruits the orphan receptor IL-1R8 (SIGIRR) to form a tripartite signaling complex. This interaction suppresses pro-inflammatory pathways (e.g., NF-κB, MAPK) and inhibits NLRP3 inflammasome activation, making it a key regulator in conditions like sepsis, autoimmune diseases, and chronic inflammation.
Preclinical studies highlight IL-37's therapeutic potential in rheumatoid arthritis, inflammatory bowel disease, and metabolic disorders. Its recombinant form has shown efficacy in reducing cytokine storms and tissue damage in animal models of COVID-19 and sepsis. Current research focuses on optimizing delivery methods, including fusion proteins and nanoparticle carriers, to enhance stability and bioavailability. Despite promising data, clinical translation requires further investigation into its dual role in cancer immunology and long-term safety profiles.
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