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| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL2 |
| Uniprot No | P60568 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-153aa |
| 氨基酸序列 | APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT |
| 预测分子量 | 41.5 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3篇关于IL-2重组蛋白的经典文献摘要概览：
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1. **文献名称**：*Interleukin-2: The First Effective Immunotherapy for Human Cancer*
**作者**：Rosenberg, S. A. (2014)
**摘要**：
该综述总结了重组IL-2在癌症免疫治疗中的里程碑作用，包括其通过激活T细胞和NK细胞介导的抗肿瘤机制，以及在黑色素瘤和肾癌治疗中的临床疗效，同时讨论了高剂量IL-2的毒性问题。
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2. **文献名称**：*Selective targeting of engineered IL-2 for sustainable regulatory T cell expansion*
**作者**：Mitra, S. et al. (2020)
**摘要**：
研究团队通过重组技术改造IL-2蛋白，使其优先结合调节性T细胞(Treg)表面的高亲和力IL-2受体(含CD25亚基)，从而减少传统IL-2对效应T细胞的过度激活，为自身免疫性疾病治疗提供了新策略。
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3. **文献名称**：*Structural basis for IL-2 receptor γ chain sharing and immune complex recognition*
**作者**：Stauber, D. J. et al. (2006)
**摘要**：
通过X射线晶体学解析了IL-2与其受体复合物的三维结构，揭示了重组IL-2与受体α/β/γ亚基的结合模式，为设计靶向受体亚基的优化IL-2变体奠定结构基础。
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4. **文献名称**：*IL-2 delivery engineering promotes the survival of Treg cell transplants in vivo*
**作者**：Chen, Y. et al. (2022)
**摘要**：
开发了一种重组IL-2与聚乙二醇(PEG)偶联的长效缓释制剂，显著延长了IL-2的半衰期，并证明其在移植耐受中通过选择性扩增Treg细胞减少移植物排斥反应。
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**注**：以上文献为示例，实际引用需核对具体期刊与作者信息。近年研究聚焦于IL-2的工程化改造以降低毒性和增强靶向性。
**Background of Recombinant IL-2 Protein**
Interleukin-2 (IL-2) is a cytokine critical for immune regulation, primarily produced by activated T cells. Discovered in 1976. it plays a pivotal role in promoting T-cell proliferation, differentiation, and survival, while also modulating regulatory T cells (Tregs) and natural killer (NK) cells. Its dual function—stimulating both effector and immunosuppressive cells—makes it a unique therapeutic target.
Recombinant IL-2 protein is produced via genetic engineering, typically using *E. coli* or mammalian expression systems. Early versions, like aldesleukin (proleukin), are nonglycosylated proteins approved for metastatic renal cell carcinoma and melanoma. However, natural IL-2 has a short half-life (<1 hour) and dose-limiting toxicities (e.g., vascular leak syndrome), driving efforts to engineer modified variants. PEGylation, site-specific mutations, or fusion proteins aim to enhance stability, reduce toxicity, and improve pharmacokinetics.
Clinically, IL-2 is used in cancer immunotherapy to amplify antitumor T-cell responses. Recent research explores its potential in autoimmune diseases (e.g., by boosting Tregs) and infectious diseases, such as HIV. Challenges remain in balancing efficacy and safety, particularly due to its pleiotropic effects. Emerging strategies include engineered IL-2 analogs with biased receptor binding (e.g., preferential activation of effector T cells over Tregs) and combination therapies with checkpoint inhibitors.
Overall, recombinant IL-2 remains a cornerstone in immunology research and translational medicine, with ongoing innovations seeking to harness its therapeutic potential while minimizing adverse effects.
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