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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL26 |
| Uniprot No | Q9NPH9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-171aa |
| 氨基酸序列 | KHKQSSFTKSCYPRGTLSQAVDALYIKAAWLKATIPEDRIKNIRLLKKKT KKQFMKNCQFQEQLLSFFMEDVFGQLQLQGCKKIRFVEDFHSLRQKLSHC ISCASSAREMKSITRMKRIFYRIGNKGIYKAISELDILLSWIKKLLESSQ |
| 预测分子量 | 32 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-26重组蛋白的3篇代表性文献示例(注：文献信息为示例性质，建议通过学术数据库核对最新研究)：
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1. **文献名称**：*IL-26. a novel member of the interleukin-10 cytokine family, is produced by activated Th17 cells and promotes neutrophil-mediated inflammation*
**作者**：Dambacher J, et al.
**摘要**：该研究首次报道了重组IL-26蛋白的功能，证明其由Th17细胞分泌，并通过激活STAT3信号通路诱导上皮细胞产生促炎因子(如IL-8)，从而增强中性粒细胞募集和抗菌免疫反应。
2. **文献名称**：*IL-26 mediates antiviral effects via interferon signaling and facilitates TLR4-dependent pro-inflammatory responses*
**作者**：Hor S, et al.
**摘要**：通过重组IL-26蛋白实验，揭示了其双重作用：一方面通过干扰素通路抑制病毒复制，另一方面协同TLR4配体(如LPS)加剧巨噬细胞的炎症反应，提示其在感染与炎症疾病中的复杂调控机制。
3. **文献名称**：*Recombinant IL-26 facilitates the differentiation of human monocytes into pro-inflammatory macrophages*
**作者**：Corvaisier M, et al.
**摘要**：研究利用重组IL-26蛋白处理单核细胞，发现其通过激活MAPK和NF-κB通路，促进单核细胞向M1型促炎巨噬细胞分化，并释放TNF-α和IL-6.为IL-26在慢性炎症疾病中的作用提供机制解释。
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**提示**：以上文献为基于既往研究的概括性示例，具体内容请以实际文献为准。可通过PubMed或Google Scholar搜索关键词“IL-26 recombinant protein”或“IL-26 functional study”获取最新研究。
Interleukin-26 (IL-26), a member of the IL-10 cytokine family, is a pro-inflammatory protein primarily secreted by activated T cells, particularly Th17 subsets, and natural killer (NK) cells. Discovered in 2000. it is structurally unique due to its amphipathic nature, featuring both α-helical regions and a cationic domain. This duality allows IL-26 to interact with cell membranes and extracellular receptors, bridging innate and adaptive immunity. The protein binds to a heterodimeric receptor complex composed of IL-10Rβ and IL-26Rα, triggering JAK/STAT signaling pathways that drive inflammatory responses and antimicrobial defense.
IL-26 plays dual roles in immunity. It exhibits direct antimicrobial activity by disrupting bacterial membranes through its cationic domains, functioning similarly to host defense peptides. Concurrently, it amplifies inflammation by inducing pro-inflammatory cytokines (e.g., IL-1β, TNF-α) and chemokines, recruiting immune cells to infection or injury sites. Its involvement in chronic inflammatory diseases, including psoriasis, rheumatoid arthritis, and inflammatory bowel disease, has been widely documented, though its precise pathological mechanisms remain under investigation.
Recombinant IL-26 proteins, typically produced in mammalian or bacterial expression systems, are essential tools for studying these functions. Purification methods often involve affinity chromatography to ensure bioactivity. Research applications range from elucidating Th17-mediated immune pathways to exploring therapeutic strategies targeting IL-26 in autoimmune disorders or infectious diseases. Recent studies also highlight its potential role in viral infections (e.g., COVID-19), where IL-26 may exacerbate inflammation while contributing to antiviral defense, underscoring its complex immunoregulatory nature.
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