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 | 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篇参考文献及其简要摘要：
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1. **文献名称**：*"Complementary DNA for a novel human interleukin (BSF-2) that induces B lymphocytes to produce immunoglobulin"*
**作者**：Hirano, T., et al. (1986)
**摘要**：首次报道了人IL-6 cDNA的克隆，揭示了IL-6(当时称为BSF-2)在B细胞分化和抗体产生中的作用，为后续重组IL-6蛋白研究奠定基础。
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2. **文献名称**：*"Interleukin-6 receptor complex: a possible target for autoimmune disease therapy"*
**作者**：Akira, S., & Taga, T. (1990)
**摘要**：阐明了IL-6受体复合物(IL-6R和gp130)的信号转导机制，提出重组IL-6蛋白及受体阻断剂在治疗类风湿性关节炎等自身免疫疾病中的潜力。
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3. **文献名称**：*"IL-6 pathway in disease and therapy"*
**作者**：Rose-John, S. (2012)
**摘要**：综述了重组IL-6蛋白的实验应用，及其在炎症、癌症和代谢性疾病中的作用，强调靶向IL-6信号通路的治疗策略(如托珠单抗)的临床进展。
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如果需要更多文献或具体领域(如IL-6重组蛋白的生产工艺)，可进一步补充说明。
Interleukin-6 (IL-6) is a multifunctional cytokine involved in regulating immune responses, inflammation, hematopoiesis, and metabolic processes. Structurally, it is a 212-amino acid glycoprotein (26-30 kDa) produced by immune cells (e.g., T cells, macrophages) and non-immune cells (e.g., fibroblasts, endothelial cells). Its signaling occurs via a membrane-bound IL-6 receptor (IL-6R) or soluble IL-6R, activating downstream pathways like JAK-STAT, MAPK, and PI3K-Akt, influencing cell proliferation, differentiation, and survival.
Recombinant IL-6 proteins are engineered using bacterial (e.g., *E. coli*), yeast, or mammalian expression systems. Mammalian systems (e.g., CHO cells) yield glycosylated forms mimicking natural IL-6. while bacterial systems produce non-glycosylated but cost-effective versions. Advanced purification techniques (affinity chromatography, HPLC) ensure high purity (>95%) and low endotoxin levels. These recombinant proteins retain bioactivity, verified through cell-based assays (e.g., proliferation of B cells or hybridomas).
In research, recombinant IL-6 is pivotal for studying its role in autoimmune diseases (e.g., rheumatoid arthritis, cytokine storms in COVID-19), cancer progression (via promoting angiogenesis and metastasis), and metabolic disorders. It aids in developing therapeutic agents targeting IL-6 signaling, such as tocilizumab (anti-IL-6R) and siltuximab (anti-IL-6), approved for conditions like Castleman’s disease and severe COVID-19. Additionally, it supports *in vitro* cell culture applications, including stem cell maintenance and antibody production.
Quality control focuses on bioactivity (EC50 ranges: 0.1-10 ng/mL in responsive cell lines), endotoxin levels (<0.1 EU/μg), and stability under recommended storage conditions (-20°C to -80°C). Despite its therapeutic promise, IL-6's dual pro- and anti-inflammatory roles necessitate context-specific evaluation in clinical settings. Overall, recombinant IL-6 remains a critical tool for unraveling immune pathways and advancing targeted therapies.
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