| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL-5Rα |
| Uniprot No | Q01344 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-335aa |
| 氨基酸序列 | DLLPDEKISLLPPVNFTIKVTGLAQVLLQWKPNPDQEQRNVNLEYQVKIN APKEDDYETRITESKCVTILHKGFSASVRTILQNDHSLLASSWASAELHA PPGSPGTSIVNLTCTTNTTEDNYSRLRSYQVSLHCTWLVGTDAPEDTQYF LYYRYGSWTEECQEYSKDTLGRNIACWFPRTFILSKGRDWLAVLVNGSSK HSAIRPFDQLFALHAIDQINPPLNVTAEIEGTRLSIQWEKPVSAFPIHCF DYEVKIHNTRNGYLQIEKLMTNAFISIIDDLSKYDVQVRAAVSSMCREAG LWSEWSQPIYVGNDE |
| 预测分子量 | 38 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-5R伪重组蛋白的参考文献示例(注：部分内容为假设性描述，实际文献需通过学术数据库验证)：
1. **"Structural and Functional Characterization of a Recombinant IL-5Rα Pseudoreceptor"**
- **作者**: Smith A, et al.
- **摘要**: 本研究通过重组技术表达IL-5Rα胞外段的突变体(伪受体)，分析其与IL-5的结合能力。结果表明，该伪受体能竞争性抑制IL-5与天然受体的结合，为靶向IL-5信号通路的药物开发提供结构基础。
2. **"Engineering a Soluble IL-5 Receptor Antagonist for Eosinophilic Disease Therapy"**
- **作者**: Johnson R, et al.
- **摘要**: 构建了一种可溶性IL-5R伪重组蛋白，可在体外和动物模型中阻断IL-5介导的嗜酸性粒细胞活化，显著减少炎症反应，提示其作为治疗哮喘等疾病的潜在生物制剂。
3. **"Mechanistic Insights into IL-5 Signaling Inhibition by a Recombinant Decoy Receptor"**
- **作者**: Lee S, et al.
- **摘要**: 利用X射线晶体学解析了IL-5与伪重组受体复合物的三维结构，揭示了伪受体通过模拟天然受体α亚基的结合界面抑制信号传导，为优化拮抗剂设计提供依据。
4. **"In Vivo Efficacy of a Modified IL-5R Pseudoprotein in Allergic Inflammation Models"**
- **作者**: Wang Y, et al.
- **摘要**: 在小鼠过敏性气道炎症模型中，注射IL-5R伪重组蛋白显著降低嗜酸性粒细胞浸润和Th2细胞因子水平，证明其具有抗炎作用且无显著毒性。
**提示**：以上文献标题及摘要均为示例，实际研究需参考PubMed、Web of Science等平台的真实论文(如涉及美泊利单抗或IL-5靶点药物开发的临床研究)。
Interleukin-5 receptor pseudorecombinant proteins (IL-5R pseudoreceptors) are engineered molecules designed to study or modulate IL-5 signaling pathways. The native IL-5 receptor consists of two subunits: a unique α-chain (IL-5Rα) that binds IL-5 with high specificity and a shared β-chain (βc) common to receptors for IL-3 and GM-CSF. This receptor complex is critical for eosinophil development, survival, and activation, making it a therapeutic target in eosinophilic disorders like asthma and hypereosinophilic syndromes.
Pseudorecombinant proteins typically mimic parts of the receptor structure but lack functional domains required for downstream signaling. For example, soluble IL-5Rα fragments or chimeric proteins combining IL-5Rα extracellular domains with non-signaling scaffolds have been developed. These constructs act as decoy receptors, competitively binding IL-5 to prevent its interaction with membrane-bound receptors. Some variants incorporate mutations to enhance binding affinity or stability.
Research on IL-5R pseudorecombinant proteins advanced alongside monoclonal antibody therapies (e.g., mepolizumab). Unlike biologics, pseudoreceptors offer potential advantages in production cost and versatility for diagnostic applications. However, challenges remain in optimizing pharmacokinetics and minimizing immunogenicity. Current studies focus on their utility as research tools for mapping IL-5/IL-5R interactions and as exploratory therapeutics for conditions driven by pathological eosinophil activity. Their design principles also inform broader efforts in cytokine receptor engineering.
×
