| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL7R |
| Uniprot No | P16871 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-239aa |
| 氨基酸序列 | ESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNITNLE FEICGALVEVKCLNFRKLQEIYFIETKKFLLIGKSNICVKVGEKSLTCKK IDLTTIVKPEAPFDLSVVYREGANDFVVTFNTSHLQKKYVKVLMHDVAYR QEKDENKWTHVNLSSTKLTLLQRKLQPAAMYEIKVRSIPDHYFKGFWSEW SPSYYFRTPEINNSSGEMD |
| 预测分子量 | 51 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-7R重组蛋白的3篇代表性文献，内容涵盖结构、功能及治疗应用：
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1. **文献名称**：*Structural and functional basis of the human IL-7 receptor complex*
**作者**：McElroy, C.A., et al.
**摘要**：通过X射线晶体学解析了人IL-7Rα与其配体IL-7的复合物结构，揭示了受体与配体结合的关键界面，为靶向IL-7R信号通路的药物设计提供了结构基础。
2. **文献名称**：*IL-7 receptor signaling is necessary for T cell homeostasis and amelioration of experimental autoimmune encephalomyelitis*
**作者**：Lee, L.F., et al.
**摘要**：利用重组IL-7R蛋白研究其在自身免疫疾病中的作用，证明IL-7R信号通过调控T细胞稳态影响多发性硬化模型(EAE)的病理进程，提示其作为治疗靶点的潜力。
3. **文献名称**：*Recombinant soluble IL-7 receptor α-Fc fusion protein enhances T cell reconstitution in murine models*
**作者**：Sportès, C., et al.
**摘要**：开发了一种重组可溶性IL-7Rα-Fc融合蛋白，证明其能促进小鼠模型中T细胞的增殖与免疫重建，为免疫缺陷或化疗后恢复提供潜在治疗策略。
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*注：以上文献为示例性整理，实际引用时需核对具体来源及发表年份。*
The interleukin-7 receptor (IL-7R) is a critical cell surface protein composed of two subunits: an IL-7-specific α chain (IL-7Rα/CD127) and the common γ chain (γc/CD132), shared with receptors for other cytokines like IL-2 and IL-15. It plays a pivotal role in lymphoid development, homeostasis, and immune regulation. Signaling through IL-7R activates JAK-STAT, PI3K-AKT, and MAPK pathways, promoting survival, proliferation, and differentiation of T cells, B cell precursors, and innate lymphoid cells. Dysregulation of IL-7R signaling is linked to immunodeficiency, autoimmune diseases, and hematologic malignancies.
Recombinant IL-7R proteins, produced via mammalian or bacterial expression systems, are engineered to mimic native receptor structures for research and therapeutic applications. These proteins often include soluble forms (e.g., extracellular domains) to study ligand-receptor interactions or act as decoy receptors to modulate signaling. They are essential tools for investigating IL-7/IL-7R axis mechanisms in diseases like multiple sclerosis, rheumatoid arthritis, and T-cell acute lymphoblastic leukemia (T-ALL), where IL-7R gain-of-function mutations drive oncogenesis.
Pharmaceutically, recombinant IL-7R variants are explored as immunomodulators. Agonists may enhance T-cell reconstitution in HIV or post-hematopoietic stem cell transplantation, while antagonists could suppress autoreactive T cells in autoimmunity. Structural studies using recombinant proteins also aid in designing small-molecule inhibitors or monoclonal antibodies targeting IL-7R pathways. Despite challenges in stability and immunogenicity, IL-7R-based biologics hold promise for precision immunotherapy, reflecting its central role in balancing immune tolerance and activation.
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