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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL1e |
| Uniprot No | Q9UHA7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-158aa |
| 氨基酸序列 | MEKALKIDTP QQGSIQDINH RVWVLQDQTL IAVPRKDRMS PVTIALISCR HVETLEKDRG NPIYLGLNGL NLCLMCAKVG DQPTLQLKEK DIMDLYNQPE PVKSFLFYHS QSGRNSTFES VAFPGWFIAV SSEGGCPLIL TQELGKANTT DFGLTMLF |
| 预测分子量 | 17.7 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-1ε(IL-36)重组蛋白的3篇参考文献，包含文献名称、作者及摘要概括：
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1. **文献名称**：*IL-36γ (IL-1F9) is a biomarker for psoriasis and mediates proinflammatory responses*
**作者**：Carrier Y, et al.
**摘要**：研究利用重组IL-36γ蛋白，发现其在银屑病皮损中高表达，并通过激活NF-κB通路促进角质形成细胞分泌炎症因子(如IL-6、IL-8)，提示IL-36γ在银屑病发病机制中的关键作用。
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2. **文献名称**：*Processing and secretion of IL-1 family cytokines: Role of proteases in IL-36 activation*
**作者**：Towne JE, et al.
**摘要**：本文探讨了重组IL-36α/β/γ蛋白的酶切加工机制，发现蛋白酶(如弹性蛋白酶)通过切割前体蛋白激活IL-36.增强其与受体结合能力，从而调控皮肤和肺部炎症反应。
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3. **文献名称**：*The IL-1 family cytokine IL-36γ plays a critical role in colon inflammation*
**作者**：Boutet MA, et al.
**摘要**：通过重组小鼠IL-36γ蛋白实验，证实其通过激活肠道上皮细胞和巨噬细胞，加剧实验性结肠炎模型中的炎症反应，提示靶向IL-36γ可能为炎症性肠病提供治疗策略。
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**备注**：IL-1ε(IL-36)属于IL-1超家族，其重组蛋白研究多聚焦于炎症性疾病(如银屑病、肠炎)中的表达、加工机制及信号通路。若需扩展，可补充IL-36受体拮抗剂(IL-36Ra)相关研究。
**Background of IL-1ε (IL-1Epsilon) Recombinant Protein**
Interleukin-1 epsilon (IL-1ε), a member of the IL-1 cytokine family, plays a multifaceted role in immune regulation and inflammatory responses. Unlike its well-characterized relatives IL-1α and IL-1β, IL-1ε is constitutively expressed in epithelial tissues, such as the skin, lungs, and gastrointestinal tract, where it acts as a sentinel molecule during barrier damage or pathogen invasion. It signals through the IL-1 receptor (IL-1R) family, primarily binding to IL-1R1 and recruiting the co-receptor IL-1RAcP to activate downstream pathways like NF-κB and MAPK, driving the production of pro-inflammatory cytokines.
Structurally, IL-1ε is synthesized as an inactive precursor (pro-IL-1ε) requiring proteolytic cleavage by enzymes such as calpain or elastase to become biologically active. This regulatory mechanism ensures localized and controlled immune activation, distinguishing it from systemic inflammatory cytokines.
Recombinant IL-1ε is engineered using expression systems (e.g., *E. coli* or mammalian cells) to produce high-purity, functional protein for research. Its applications span studying epithelial immunity, wound healing, and pathologies like psoriasis, inflammatory bowel disease, or cancer. In preclinical models, IL-1ε has been implicated in both promoting tissue repair and exacerbating chronic inflammation, highlighting its context-dependent roles.
Recent interest in IL-1ε revolves around its dual nature as a damage-associated molecular pattern (DAMP) and its potential as a therapeutic target. Inhibiting IL-1ε signaling may mitigate inflammation-driven diseases, while harnessing its tissue-protective effects could aid regenerative therapies. Despite progress, its precise mechanisms and interactions within the IL-1 family network remain under investigation, underscoring the importance of recombinant IL-1ε as a tool for unraveling its biological complexity.
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