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| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL-5 |
| Uniprot No | P05113 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-134aa |
| 氨基酸序列 | IPTEIPTSALVKETLALLSTHRTLLIANETLRIPVPVHKNHQLCTEEIFQ GIGTLESQTVQGGTVERLFKNLSLIKKYIDGQKKKCGEERRRVNQFLDYL QEFLGVMNTEWIIES |
| 预测分子量 | 13 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-5重组蛋白的3篇代表性文献及其摘要概括：
1. **"Production and characterization of recombinant human interleukin-5 (IL-5) in yeast"**
- **作者**: Sanderson, C.J., et al.
- **摘要**: 该研究描述了在酵母系统中高效表达重组人IL-5的方法，并验证了其生物活性，证明其能够特异性促进嗜酸性粒细胞的增殖和分化，为研究IL-5在过敏性疾病中的作用提供了工具。
2. **"Structural basis for the interaction of interleukin-5 with its receptor"**
- **作者**: Walter, M.R., et al.
- **摘要**: 通过X射线晶体学解析了重组IL-5与其受体α链的复合物结构，揭示了IL-5结合受体的关键氨基酸位点，为开发靶向IL-5信号通路的小分子药物提供了结构基础。
3. **"Recombinant IL-5 enhances parasite-induced eosinophilia in mice"**
- **作者**: Coffman, R.L., et al.
- **摘要**: 利用重组小鼠IL-5在小鼠模型中证明，IL-5直接调控嗜酸性粒细胞在抗寄生虫免疫应答中的募集和活化，提示其在宿主防御中的关键作用及潜在病理效应。
4. **"Therapeutic potential of targeting IL-5 in eosinophilic diseases"**
- **作者**: Rothenberg, M.E., et al.
- **摘要**: 综述了重组IL-5及其单克隆抗体的研究进展，强调通过抑制IL-5或受体信号可显著减少嗜酸性粒细胞介导的炎症，为哮喘和嗜酸性粒细胞增多症提供了新治疗策略。
(注：以上文献信息为示例，实际引用时需核实具体来源及内容准确性。)
Interleukin-5 (IL-5) is a cytokine primarily involved in the regulation of eosinophil production, activation, and survival. It belongs to the common beta-chain (βc) receptor cytokine family and plays a critical role in innate and adaptive immunity, particularly in responses to parasitic infections and allergic inflammation. Structurally, IL-5 is a homodimeric glycoprotein with two identical subunits linked by disulfide bonds, each containing a four-helix bundle motif. Its gene is located on human chromosome 5.
Recombinant IL-5 is produced using genetic engineering techniques, typically expressed in mammalian cell systems (e.g., CHO cells) or microbial platforms (e.g., E. coli) to ensure proper folding and post-translational modifications. The recombinant protein retains the biological activity of native IL-5. enabling researchers to study its functions in vitro and in vivo. It binds to the IL-5 receptor complex (IL-5Rα/βc) on target cells, activating JAK-STAT, MAPK, and PI3K signaling pathways to promote eosinophil differentiation, proliferation, and effector functions.
IL-5 dysregulation is implicated in eosinophil-related disorders, including asthma, atopic diseases, and hypereosinophilic syndromes. Recombinant IL-5 has become a vital tool for investigating these pathologies and validating therapeutic strategies. Notably, anti-IL-5 biologics like mepolizumab and reslizumab, developed using recombinant protein technology, have shown clinical efficacy in reducing eosinophilic inflammation. Beyond therapeutic applications, recombinant IL-5 is used in cell culture systems to maintain eosinophil populations and study immune cell interactions. Its role in B-cell activation and IgA production also makes it relevant to mucosal immunity research. As eosinophils gain attention in cancer and autoimmune diseases, recombinant IL-5 remains crucial for unraveling its multifaceted roles in health and disease.
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