| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL6R |
| Uniprot No | P08887 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-365aa |
| 氨基酸序列 | LAPRRCPAQEVARGVLTSLPGDSVTLTCPGVEPEDNATVHWVLRKPAAGS HPSRWAGMGRRLLLRSVQLHDSGNYSCYRAGRPAGTVHLLVDVPPEEPQL SCFRKSPLSNVVCEWGPRSTPSLTTKAVLLVRKFQNSPAEDFQEPCQYSQ ESQKFSCQLAVPEGDSSFYIVSMCVASSVGSKFSKTQTFQGCGILQPDPP ANITVTAVARNPRWLSVTWQDPHSWNSSFYRLRFELRYRAERSKTFTTWM VKDLQHHCVIHDAWSGLRHVVQLRAQEEFGQGEWSEWSPEAMGTPWTESR SPPAENEVSTPMQALTTNKDDDNILFRDSANATSLPVQDSSSVPLP |
| 预测分子量 | 40 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IL6R重组蛋白的3篇参考文献及其摘要概括：
1. **"Cloning and expression of the human interleukin-6 receptor in mammalian cells"**
- **作者**: Browning, J.L., et al.
- **摘要**: 该研究报道了人源IL6R重组蛋白的克隆与哺乳动物细胞表达，分析了其结构与配体IL6的结合特性，揭示了其在炎症信号转导中的潜在作用。
2. **"Soluble IL-6 receptor: its role in regulating IL-6 activity"**
- **作者**: Murakami, M., et al.
- **摘要**: 文章探讨了可溶性IL6R重组蛋白(sIL6R)的功能机制，发现其通过结合IL6并激活下游信号通路(如JAK/STAT)，参与炎症和细胞增殖的调控。
3. **"Therapeutic targeting of IL-6 receptor signaling in autoimmune diseases"**
- **作者**: Kishimoto, T., et al.
- **摘要**: 综述了IL6R重组蛋白在疾病治疗中的应用，包括通过阻断IL6-IL6R相互作用(如托珠单抗)治疗类风湿关节炎等自身免疫病的临床研究进展。
4. **"Structure-function analysis of IL-6 receptor gp130 domains"**
- **作者**: Rose-John, S., et al.
- **摘要**: 通过重组蛋白技术解析IL6R与gp130复合物的结构，阐明了其介导信号转导的关键结构域，为靶向药物设计提供了理论依据。
(注：上述文献为示例，实际引用需核实具体文献来源。)
Interleukin-6 receptor (IL6R) is a key component of the IL-6 signaling pathway, which regulates immune responses, inflammation, hematopoiesis, and cell survival. As a cytokine receptor, IL6R exists in both membrane-bound and soluble forms. The membrane-bound IL6R (mIL6R) is expressed on specific cell types, including hepatocytes and leukocytes, while the soluble form (sIL6R) arises from proteolytic cleavage of mIL6R or alternative mRNA splicing. IL6R binds to interleukin-6 (IL-6), a pleiotropic cytokine involved in acute-phase reactions and chronic inflammatory diseases. This interaction triggers the formation of a hexameric signaling complex with glycoprotein 130 (gp130), initiating downstream JAK/STAT, MAPK, and PI3K pathways.
Recombinant IL6R proteins are engineered in vitro to study IL-6 signaling mechanisms or develop therapeutic agents. These proteins typically include the extracellular domain of IL6R, which retains IL-6 binding capacity. Researchers produce recombinant IL6R using mammalian expression systems (e.g., CHO cells) or bacterial systems (E. coli), followed by purification via affinity chromatography. Structural studies of recombinant IL6R have revealed critical binding interfaces with IL-6 and gp130. informing drug design.
Clinically, IL6R-targeted therapies like tocilizumab (a monoclonal antibody against IL6R) exploit this pathway to treat autoimmune disorders, including rheumatoid arthritis and cytokine release syndrome. Recombinant IL6R proteins also serve as tools to investigate IL-6 trans-signaling, a process where sIL6R enables IL-6 responsiveness in cells lacking mIL6R, implicated in cancer progression and chronic inflammation. Ongoing research explores engineered IL6R variants to modulate signaling specificity or improve therapeutic efficacy.
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