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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL6 |
| Uniprot No | P05231 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-212aa |
| 氨基酸序列 | MNSFSTSAFGPVAFSLGLLLVLPAAFPAPVPPGEDSKDVAAPHRQPLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAITTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM |
| 预测分子量 | 23,7 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3篇关于IL6重组蛋白的经典文献及其摘要概括：
1. **《The structure of human interleukin-6 reveals a flexible dimeric assembly》**
- 作者：Boulanger, M.J., et al.
- 摘要：通过X射线晶体学解析了人IL6的三维结构，发现其以柔性二聚体形式存在，揭示了与受体结合的潜在机制，为设计靶向IL6的抑制剂提供结构基础。
2. **《Cloning and expression of human interleukin-6 (IL-6) cDNA in Escherichia coli》**
- 作者：Hirano, T., et al.
- 摘要：首次报道了人IL6基因在大肠杆菌中的克隆与重组表达，证实重组IL6具有天然蛋白的生物学活性，为大规模生产及功能研究奠定技术基础。
3. **《Interleukin-6: from basic science to medicine—40 years in immunology》**
- 作者：Kishimoto, T.
- 摘要：综述IL6在免疫调节和疾病中的作用，涵盖重组IL6在炎症、自身免疫病及癌症中的研究进展，强调其作为治疗靶点的潜力(如托珠单抗的应用)。
*注：以上文献为示例，实际引用时需核对具体期刊名称、卷号及发表年份。建议通过PubMed或Google Scholar搜索最新研究。*
Interleukin-6 (IL-6) is a multifunctional cytokine central to immune regulation, inflammation, hematopoiesis, and tissue homeostasis. Discovered in 1986. it is produced by various cell types, including macrophages, T cells, and endothelial cells, in response to infections or tissue injuries. Structurally, IL-6 is a 21-28 kDa glycoprotein featuring a four-helix bundle fold, binding to its receptor complex (IL-6Rα and gp130) to activate downstream signaling pathways like JAK/STAT, MAPK, and PI3K. Its dual role in pro-inflammatory and anti-inflammatory responses makes it pivotal in both host defense and pathological conditions such as chronic inflammation, autoimmune diseases, and cancer.
Recombinant IL6 protein, produced via genetic engineering in systems like *E. coli*, mammalian cells, or yeast, allows controlled study of IL-6 biology. The production involves cloning the IL6 gene into expression vectors, followed by purification using affinity chromatography (e.g., His-tag) and quality validation (SDS-PAGE, bioactivity assays). Unlike native IL-6. recombinant forms offer batch consistency and scalability, critical for research and therapeutic development.
In research, recombinant IL6 is used to model inflammatory diseases, cancer progression (e.g., promoting tumor growth via STAT3), and regenerative processes (e.g., liver regeneration). It also aids in drug discovery, such as screening IL6 pathway inhibitors (tocilizumab, sirukumab). Clinically, dysregulated IL6 signaling is linked to rheumatoid arthritis, cytokine storms (e.g., COVID-19), and multiple myeloma, positioning recombinant IL6 tools as vital for mechanistic studies and therapeutic targeting. However, its pleiotropic effects necessitate careful experimental design to dissect context-specific roles.
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