首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL-6 |
| Uniprot No | P05231 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-212aa |
| 氨基酸序列 | VPPGEDSKDVAAPHRQPLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAITTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM |
| 预测分子量 | 28.3 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. |
1. **《Molecular cloning of a human interleukin-6 (IL-6) cDNA and its expression in eukaryotic cells**》
- **作者**: Akira, S., et al.
- **摘要**: 该研究首次报道了人IL-6基因的克隆及其在真核细胞中的表达，验证了重组IL-6蛋白在调控免疫反应和炎症中的生物学活性，为后续功能研究奠定基础。
2. **《Interleukin-6: from basic science to medicine—40 years in immunology》**
- **作者**: Kishimoto, T.
- **摘要**: 综述IL-6的发现历程、信号转导机制(包括经典和反式信号通路)及其在疾病(如类风湿性关节炎、细胞因子风暴)中的作用，强调重组IL-6作为研究工具和治疗靶点的潜力。
3. **《IL-6 trans-signaling via the soluble IL-6 receptor: importance for the pro-inflammatory activities of IL-6》**
- **作者**: Rose-John, S., et al.
- **摘要**: 研究通过重组IL-6和可溶性IL-6受体阐明IL-6的“反式信号”机制，揭示其在慢性炎症和癌症中的关键作用，并提出靶向该通路治疗疾病的策略。
4. **《The role of interleukin-6 in the pathogenesis of rheumatoid arthritis》**
- **作者**: Hunter, C.A., & Kastelein, R.A.
- **摘要**: 通过重组IL-6蛋白及动物模型，验证IL-6在类风湿性关节炎中的促炎作用，并探讨针对IL-6的单克隆抗体(如托珠单抗)的临床疗效。
以上文献涵盖IL-6重组蛋白的分子机制、信号通路及疾病治疗应用，适合快速了解其核心研究方向。
Interleukin-6 (IL-6) is a pleiotropic cytokine first identified in the 1980s for its role in immune regulation, inflammation, and hematopoiesis. Structurally, it is a 184-amino acid protein featuring a four-helix bundle topology, produced by diverse cell types, including macrophages, T cells, endothelial cells, and fibroblasts. IL-6 exerts biological effects by binding to a membrane-bound IL-6 receptor (IL-6R) or soluble IL-6R, triggering gp130 homodimerization and activation of downstream JAK/STAT, MAPK, and PI3K signaling pathways. Its multifunctional roles span acute-phase inflammation, B-cell differentiation, fever induction, and metabolic regulation.
Recombinant IL-6 protein, generated via genetic engineering in systems like *E. coli* or mammalian cells, retains the native protein’s bioactivity while ensuring high purity and batch consistency. This technology enables large-scale production for research and therapeutic applications. IL-6 is implicated in pathologies such as autoimmune diseases (rheumatoid arthritis, Crohn’s disease), cytokine release syndrome (e.g., severe COVID-19), and cancers (multiple myeloma, lymphoma). Consequently, IL-6 signaling inhibitors (e.g., tocilizumab, siltuximab) have been developed, underscoring the protein’s clinical relevance.
In research, recombinant IL-6 is widely used to study inflammatory pathways, immune cell activation, and crosstalk between metabolic and immune systems. It also serves as a critical reagent in diagnostic assays, drug screening, and *in vitro* disease modeling. Despite its pathogenic roles, IL-6’s regenerative functions in tissue repair and hematopoiesis highlight its dual nature. Ongoing studies explore its context-dependent mechanisms, aiming to refine therapeutic strategies targeting IL-6 signaling.
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