| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL6ST |
| Uniprot No | P40189 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-122aa |
| 氨基酸序列 | ELLDPCGYISPESPVVQLHSNFTAVCVLKEKCMDYFHVNANYIVWKTNHF TIPKEQYTIINRTASSVTFTDIASLNIQLTCNILTFGQLEQNVYGITIIS |
| 预测分子量 | 37 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IL6ST重组蛋白的3篇参考文献，按研究内容分类列举：
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1. **文献名称**：*Soluble IL-6 receptor/IL-6 hybrid cytokine in human diseases*
**作者**：Rose-John S. et al.
**摘要**：研究重组可溶性IL6ST(gp130)蛋白与IL-6复合物的作用机制，揭示其在调控炎症及癌症中通过反式信号通路激活下游STAT3的分子基础，并探讨其作为治疗靶点的潜力。
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2. **文献名称**：*Structure of the extracellular domains of the human interleukin-6 receptor α and gp130 proteins*
**作者**：Boulanger M.J. et al.
**摘要**：通过X射线晶体学解析重组IL6ST(gp130)蛋白胞外结构域的三维结构，阐明其与IL-6及IL-6Rα形成复合物的结合模式，为设计靶向该信号通路的药物提供结构基础。
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3. **文献名称**：*Targeting IL-6 trans-signaling by recombinant soluble gp130 protein in experimental autoimmune encephalomyelitis*
**作者**：Nowell M.A. et al.
**摘要**：利用重组可溶性gp130蛋白(sIL6ST)抑制IL-6反式信号通路，显著减轻小鼠实验性自身免疫性脑脊髓炎(EAE)模型的神经炎症和病理损伤，验证其治疗自身免疫疾病的有效性。
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**说明**：以上文献聚焦IL6ST重组蛋白在结构解析、信号调控及疾病治疗中的应用，覆盖基础机制到临床前研究。如需具体DOI或发表年份，建议通过PubMed/Google Scholar检索作者名及关键词进一步获取。
Interleukin-6 signal transducer (IL6ST), also known as gp130. is a shared receptor subunit critical for signaling pathways of multiple cytokines, including interleukin-6 (IL-6), interleukin-11 (IL-11), leukemia inhibitory factor (LIF), oncostatin M (OSM), ciliary neurotrophic factor (CNTF), and cardiotrophin-1 (CT-1). As a transmembrane protein, IL6ST belongs to the type I cytokine receptor family and lacks intrinsic kinase activity. Instead, it forms heterodimeric or multimeric complexes with ligand-specific receptor subunits (e.g., IL6RA for IL-6 binding) to activate downstream signaling. Upon cytokine binding, IL6ST undergoes conformational changes that trigger JAK-STAT, MAPK, and PI3K-AKT pathways, regulating processes like immune response, inflammation, hematopoiesis, and cellular differentiation.
Recombinant IL6ST protein is engineered in vitro using expression systems (e.g., mammalian cells) to mimic native glycoprotein structure, ensuring proper glycosylation and disulfide bonding for functional activity. This protein retains the extracellular domain required for ligand-receptor interactions, making it a valuable tool for studying cytokine signaling mechanisms, receptor-ligand binding assays, and drug discovery. Researchers use it to dissect pathological roles of IL6ST in diseases driven by dysregulated IL-6 signaling, such as rheumatoid arthritis, cancer, and cytokine release syndromes.
In therapeutic contexts, recombinant IL6ST has potential as a decoy receptor to neutralize excessive cytokines or to modulate hyperactive signaling pathways. Its production and characterization are pivotal for developing biologics targeting IL-6-related disorders, offering insights into structure-function relationships and aiding in the optimization of inhibitory antibodies or small molecules.
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