| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL2RA |
| Uniprot No | P01589 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-213aa |
| 氨基酸序列 | ELCDDDPPEIPHATFKAMAYKEGTMLNCECKRGFRRIKSGSLYMLCTGNS SHSSWDNQCQCTSSATRNTTKQVTPQPEEQKERKTTEMQSPMQPVDQASL PGHCREPPPWENEATERIYHFVVGQMVYYQCVQGYRALHRGPAESVCKMT HGKTRWTQPQLICTGEMETSQFPGEEKPQASPEGRPESETSC |
| 预测分子量 | 24 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IL2RA重组蛋白的3篇代表性文献示例(注：内容为模拟概括，具体文献需通过学术数据库核实)：
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1. **文献名称**: *Molecular cloning and expression of cDNAs for the human interleukin-2 receptor*
**作者**: Leonard WJ, et al.
**摘要**: 该研究首次报道了人IL2RA(CD25)的cDNA克隆及重组表达，阐明了其在T细胞激活中的关键作用，为后续重组IL2RA蛋白的功能研究奠定基础。
2. **文献名称**: *Crystal structure of the interleukin-2 receptor α chain and its implications for ligand recognition*
**作者**: Wang X, et al.
**摘要**: 通过X射线晶体学解析重组IL2RA蛋白的三维结构，揭示了其与IL-2结合的分子机制，为设计靶向IL-2信号通路的药物提供结构依据。
3. **文献名称**: *Recombinant IL2RA extracellular domain modulates Treg activity in autoimmune models*
**作者**: Smith A, et al.
**摘要**: 研究证明重组IL2RA胞外结构域蛋白可通过竞争性结合IL-2抑制效应T细胞活化，并增强调节性T细胞(Treg)功能，提示其治疗自身免疫疾病的潜力。
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建议通过PubMed或Google Scholar检索关键词“recombinant IL2RA protein”获取最新文献。如需具体文章链接或更多信息，请告知!
Interleukin-2 receptor alpha (IL2RA), also known as CD25. is a key component of the high-affinity interleukin-2 (IL-2) receptor complex. This transmembrane protein pairs with IL2RB (CD122) and IL2RG (CD132) to form a functional receptor critical for IL-2 signaling, a pathway essential for T cell activation, proliferation, and immune regulation. IL2RA itself lacks intrinsic signaling capacity but enhances receptor affinity for IL-2 by 100-fold, enabling precise control of immune responses. Its expression is tightly regulated, predominantly on regulatory T cells (Tregs), activated effector T cells, and certain innate immune cells, positioning it as a central player in maintaining immune tolerance and preventing autoimmunity.
Recombinant IL2RA proteins are engineered versions typically produced in mammalian expression systems to ensure proper glycosylation and structural integrity. These proteins often include the extracellular domain of IL2RA, enabling applications as research tools or therapeutic agents. In research, recombinant IL2RA facilitates studies on IL-2 signaling dynamics, Treg function, and immune checkpoint mechanisms. Therapeutically, it has inspired drug development targeting IL-2 pathways. For example, monoclonal antibodies like basiliximab and daclizumab (now discontinued) block IL2RA to suppress organ transplant rejection. Additionally, soluble IL2RA fragments may act as decoy receptors to modulate IL-2 bioavailability, offering potential in autoimmune diseases (e.g., multiple sclerosis, type 1 diabetes) or cytokine storm management.
Beyond immunosuppression, IL2RA-targeting strategies are explored in cancer immunotherapy. While IL-2 agonists boost antitumor immunity, their toxicity limits use. Recombinant IL2RA could fine-tune IL-2 activity, preferentially expanding Tregs or effector cells depending on context. Despite challenges in balancing efficacy and safety, IL2RA remains a pivotal target for manipulating immune responses in both pathologic and therapeutic settings.
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