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| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL10 |
| Uniprot No | P22301 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-178aa |
| 氨基酸序列 | SENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFK GYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRR CHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMK IRN |
| 预测分子量 | 18 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3篇关于IL-10重组蛋白的经典文献摘要(基于公开学术信息整理)：
1. **文献名称**：*"Interleukin-10 and the interleukin-10 receptor"*
**作者**：Moore, K.W. et al.
**摘要**：综述了IL-10的生物学功能及其受体信号通路，重点讨论了重组IL-10在免疫调控中的抗炎作用，以及在治疗炎症性疾病中的潜在应用。
2. **文献名称**：*"Recombinant human interleukin 10 in the treatment of patients with mild to moderate active Crohn's disease"*
**作者**：van Deventer, S.J.H. et al.
**摘要**：通过II期临床试验证明，皮下注射重组人IL-10可显著缓解克罗恩病患者的炎症症状，但部分患者出现头痛等副作用，提示需优化给药方案。
3. **文献名称**：*"IL-10 elicits IFNγ-dependent tumor immune surveillance"*
**作者**：Mumm, J.B. et al.
**摘要**：研究发现重组IL-10可通过激活CD8+ T细胞和增强干扰素γ(IFNγ)分泌，抑制小鼠肿瘤模型中的肿瘤生长，揭示了其在癌症免疫治疗中的潜力。
4. **文献名称**：*"Nanoparticle delivery of recombinant IL-10 for osteoarthritis therapy"*
**作者**：Zhang, Y. et al.
**摘要**：开发了一种纳米颗粒包裹的重组IL-10递送系统，显著延长了IL-10在关节腔内的滞留时间，并在骨关节炎模型中有效减轻软骨退化和炎症反应。
(注：以上文献为示例性内容，实际引用时请通过PubMed或学术数据库核对原文信息。)
**Background of IL-10 Recombinant Protein**
Interleukin-10 (IL-10), a pleiotropic cytokine, was first identified in 1989 for its ability to suppress cytokine synthesis in Th2 cells. It is primarily produced by immune cells, including T cells, B cells, macrophages, and dendritic cells, and plays a critical role in modulating inflammatory and immune responses. Structurally, IL-10 is a homodimeric protein with each monomer consisting of 160 amino acids, forming a conserved α-helical bundle. Its anti-inflammatory properties are mediated through binding to the IL-10 receptor (IL-10R), activating JAK-STAT signaling pathways, which downregulate pro-inflammatory cytokines (e.g., TNF-α, IL-6. IL-1β) and inhibit antigen-presenting cell functions.
Recombinant IL-10 proteins are engineered using expression systems like *E. coli* or mammalian cells to ensure high purity and bioactivity. These proteins retain the native structure and function of endogenous IL-10. enabling research and therapeutic applications. Preclinical studies highlight their potential in treating chronic inflammatory diseases (e.g., inflammatory bowel disease, rheumatoid arthritis), autoimmune disorders, and transplant rejection. Paradoxically, IL-10 also exhibits dual roles in cancer, either suppressing antitumor immunity or enhancing cytotoxic T-cell activity depending on the context.
Despite therapeutic promise, challenges such as short half-life and systemic toxicity limit clinical translation. Ongoing efforts focus on optimizing delivery systems (e.g., nanoparticles) or engineering IL-10 variants with improved stability and tissue targeting. Recombinant IL-10 remains a vital tool for dissecting immune regulation mechanisms and developing precision therapies for immune-related pathologies.
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