首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >90%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 | 28-212aa |
| 氨基酸序列 | APVPPGEDSKDVAAPHRQPLTSSERIDKQIRYILDGISALRKETCNKSNM CESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLE YLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAITTPDPTTNASLLT KLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM |
| 预测分子量 | 21 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-6重组蛋白的3篇经典文献的简要概括：
1. **文献名称**：*"Cloning and expression of human interleukin-6 (IL-6) in Escherichia coli*"
**作者**：Hirano, T. 等(1986)
**摘要**：首次报道了人IL-6基因的克隆及在大肠杆菌中的重组表达，验证了重组IL-6的生物活性(如诱导B细胞分化)，为后续机制研究奠定基础。
2. **文献名称**：*"Interleukin-6 receptor and signal transduction*"
**作者**：Kishimoto, T. 等(1989)
**摘要**：系统阐述IL-6受体(IL-6R)的结构及其信号转导机制(如JAK-STAT通路)，揭示重组IL-6在炎症和免疫调控中的分子基础。
3. **文献名称**：*"The pro- and anti-inflammatory properties of interleukin-6*"
**作者**：Scheller, J. 等(2011)
**摘要**：综述IL-6重组蛋白在疾病模型中的双重作用，如促进炎症(类风湿关节炎)和组织修复(肝脏再生)，强调其在治疗中的潜在靶点价值。
(如需第4篇，可补充关于重组IL-6在特定疾病模型中的应用研究文献。)
Interleukin-6 (IL-6) is a multifunctional cytokine critical to immune regulation, inflammation, hematopoiesis, and tissue homeostasis. Discovered in 1986. it is produced by immune cells (e.g., macrophages, T cells), endothelial cells, and fibroblasts in response to pathogens or tissue damage. Structurally, IL-6 is a 184-amino acid protein with a four-helix bundle topology, signaling through a receptor complex comprising IL-6Rα and gp130 subunits. Its pleiotropic actions include inducing acute-phase proteins, B-cell differentiation, and T-cell activation, while dysregulation is linked to chronic inflammation, autoimmune diseases (e.g., rheumatoid arthritis), and cancer.
Recombinant IL-6 protein, engineered via genetic cloning in prokaryotic (E. coli) or eukaryotic (mammalian, insect) expression systems, allows standardized study of IL-6 pathways and therapeutic applications. Bacterial systems yield non-glycosylated proteins suitable for structural studies, while mammalian cells (e.g., CHO, HEK293) produce glycosylated forms mimicking native human IL-6 for functional assays. Rigorous purification (HPLC, affinity chromatography) and quality control (SDS-PAGE, endotoxin testing) ensure batch consistency.
Research applications include in vitro modeling of inflammatory responses, drug screening (e.g., anti-IL-6 therapies like tocilizumab), and elucidating IL-6’s dual pro-/anti-inflammatory roles. Clinically, recombinant IL-6 aids immunotherapy trials and biomarker studies, particularly in cytokine storm syndromes (e.g., COVID-19. CAR-T therapy toxicity). Challenges remain in balancing its therapeutic inhibition without compromising metabolic and regenerative functions. Ongoing studies explore IL-6 signaling nuances, including trans-signaling mechanisms and tissue-specific effects, driving innovations in targeted biologics and personalized medicine approaches.
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