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| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL5 |
| 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IL5重组蛋白的3篇代表性文献概览：
1. **《Production and characterization of recombinant human interleukin-5》**
作者：Tavernier et al. (1989)
摘要：该研究首次报道了通过基因工程技术在大肠杆菌中成功表达重组人IL-5.并验证其生物活性。实验证明重组IL-5能够特异性促进嗜酸性粒细胞的分化与增殖。
2. **《Crystal structure of recombinant human interleukin-5 at 2.4 Å resolution》**
作者：Milburn et al. (1993)
摘要：通过X射线晶体学解析了重组人IL-5的三维结构，揭示了其独特的二聚体构象及与受体结合的关键结构域，为靶向药物设计提供了结构基础。
3. **《Therapeutic targeting of IL-5 in eosinophilic diseases using a recombinant antibody》**
作者：Kolbeck et al. (2010)
摘要：研究开发了靶向IL-5的重组单抗(如美泊利单抗)，通过阻断IL-5信号显著降低哮喘患者嗜酸性粒细胞水平，验证了重组蛋白在治疗Th2型炎症疾病中的临床潜力。
Interleukin-5 (IL-5) is a cytokine primarily involved in regulating the growth, differentiation, and activation of eosinophils, a type of white blood cell critical in immune responses against parasites and allergic inflammation. It functions by binding to a heterodimeric receptor complex (IL-5Rα and βc subunits) on target cells, triggering signaling pathways like JAK-STAT, which promote eosinophil survival and recruitment to tissues. Dysregulated IL-5 signaling is implicated in eosinophilic disorders, including asthma, chronic rhinosinusitis, and hypereosinophilic syndromes.
Recombinant IL-5 protein, produced via genetic engineering in systems like mammalian (e.g., CHO cells) or bacterial (e.g., E. coli) expression platforms, enables precise study of IL-5 biology and therapeutic development. Unlike native IL-5. recombinant forms are highly purified, standardized, and free of contaminants, making them essential tools for in vitro assays, animal studies, and drug screening. They retain functional activity, binding to IL-5 receptors to simulate or inhibit downstream effects.
Clinically, IL-5-targeted biologics—such as monoclonal antibodies (e.g., mepolizumab, reslizumab)—leverage insights from recombinant IL-5 research to neutralize IL-5 or its receptor, reducing eosinophil levels in diseases like severe eosinophilic asthma. However, recombinant IL-5 itself has limited therapeutic use due to its pro-inflammatory role. Current studies focus on optimizing IL-5 pathway modulation, balancing efficacy with safety, and exploring combination therapies. Challenges remain in understanding tissue-specific effects and long-term impacts of IL-5 inhibition, driving ongoing research into its molecular mechanisms and translational applications.
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