首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 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 | 1-218aa |
| 氨基酸序列 | MSFVGENSGVKMGSEDWEKDEPQCCLEDPAGSPLEPGPSLPTMNFVHTSPKVKNLNPKKFSIHDQDHKVLVLDSGNLIAVPDKNYIRPEIFFALASSLSSASAEKGSPILLGVSKGEFCLYCDKDKGQSHPSLQLKKEKLMKLAAQKESARRPFIFYRAQVGSWNMLESAAHPGWFICTSCNCNEPVGVTDKFENRKHIEFSFQPVCKAEMSPSEVSD |
| 预测分子量 | 51.1 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篇代表性文献摘要：
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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**：该研究首次报道重组人IL-37蛋白通过抑制TLR信号通路和NF-κB活化，显著减少巨噬细胞促炎因子(如TNF-α、IL-1β)的释放，证实其作为天然免疫反应的关键负调控因子作用。
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2. **文献名称**：*Recombinant IL-37 suppresses lung adenocarcinoma growth via enhancing T cell immunity*
**作者**：Li, Y., et al.
**摘要**：在小鼠肺癌模型中，重组IL-37蛋白通过激活CD8+ T细胞并抑制调节性T细胞(Tregs)功能，显著抑制肿瘤生长，提示其作为癌症免疫治疗潜在分子的可能性。
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3. **文献名称**：*IL-37 ameliorates sepsis by modulating macrophage polarization through STAT3 signaling*
**作者**：Wang, D., et al.
**摘要**：研究表明，重组IL-37蛋白通过STAT3通路促进巨噬细胞向抗炎M2表型极化，减轻脓毒症小鼠的全身炎症反应和器官损伤，为脓毒症治疗提供新靶点。
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4. **文献名称**：*Recombinant IL-37 protects against cardiac ischemia-reperfusion injury in mice*
**作者**：Bulkhi, A. B., et al.
**摘要**：实验发现，重组IL-37预处理可减少心肌细胞凋亡及中性粒细胞浸润，通过抑制NLRP3炎症小体活化，显著改善小鼠心脏缺血再灌注损伤后的心功能。
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以上研究均聚焦重组IL-37蛋白在炎症、免疫调节及疾病治疗中的分子机制，为开发IL-37相关疗法提供了理论基础。
Interleukin-37 (IL-37), a member of the interleukin-1 (IL-1) cytokine family, was first identified in 2000 as a unique anti-inflammatory cytokine with immunosuppressive properties. Unlike most pro-inflammatory IL-1 family members, IL-37 acts as a natural brake on excessive immune responses, playing critical roles in maintaining immune homeostasis. It exists in five splice variants (IL-37a-e), with IL-37b being the most studied isoform due to its full-length functional structure. IL-37 is constitutively expressed at low levels in various tissues but is upregulated during inflammation or infection.
The recombinant IL-37 protein is produced through genetic engineering, typically using bacterial (e.g., E. coli) or mammalian expression systems, to enable research and therapeutic applications. Mechanistically, IL-37 binds to IL-18 receptor alpha (IL-18Rα) and recruits IL-1R8 (formerly TIR8), triggering intracellular Smad3 and STAT3 signaling pathways. This interaction suppresses NF-κB activation and inhibits the production of pro-inflammatory cytokines (e.g., TNF-α, IL-6). Notably, IL-37 can also translocate to the nucleus to regulate gene expression independently of receptor binding.
Preclinical studies highlight IL-37's therapeutic potential in autoimmune diseases (e.g., rheumatoid arthritis), chronic inflammatory conditions (e.g., inflammatory bowel disease), and sepsis. Its ability to mitigate excessive inflammation while preserving antimicrobial immunity makes it particularly promising. Recent research also explores its dual role in cancer, showing both tumor-suppressive and microenvironment-modulating effects. Despite progress, clinical translation remains limited, with ongoing phase I/II trials assessing safety in humans. Challenges include optimizing delivery methods and understanding isoform-specific functions. Recombinant IL-37 continues to be a valuable tool for decoding immune regulation mechanisms and developing novel anti-inflammatory therapies.
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