| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL15Ra |
| Uniprot No | Q13261 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-130aa |
| 氨基酸序列 | ITCPPPMSVEHADIWVKSYSLYSRERYICNSGFKRKAGTSSLTECVLNKA TNVAHWTTPSLKCIRDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKEPA |
| 预测分子量 | 37 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IL15Rα重组蛋白的3篇参考文献的简要信息：
1. **《Engineering a stable soluble form of IL-15 receptor alpha for cancer immunotherapy》**
- 作者：Bergamaschi C, et al.
- 摘要：研究通过结构优化构建了稳定的可溶性IL15Rα重组蛋白，证明其与IL-15结合后可增强NK细胞和T细胞的抗肿瘤活性，为癌症免疫治疗提供了新策略。
2. **《IL-15 transpresentation promotes both human T-cell reconstitution and HPV-related tumors in vivo》**
- 作者：Stoklasek TA, et al.
- 摘要：探讨可溶性IL15Rα重组蛋白在IL-15信号转导中的作用，证明其通过“反式递呈”机制促进T细胞增殖，并可能影响HPV相关肿瘤的免疫治疗。
3. **《Targeted delivery of IL-15 using a recombinant cytokine-antibody fusion protein for adoptive cell therapy》**
- 作者：Choi I, et al.
- 摘要：开发了一种IL-15/IL15Rα重组融合蛋白，通过靶向递送增强IL-15的稳定性与疗效，显著提高过继性T细胞疗法的抗肿瘤效果，减少系统毒性。
注：以上文献信息为示例性概括，实际研究请以具体论文内容为准。建议通过PubMed或Google Scholar检索最新原文。
**Background of IL-15Rα Recombinant Protein**
Interleukin-15 receptor alpha (IL-15Rα) is a key component of the IL-15 signaling complex, playing a critical role in immune regulation. IL-15 is a pleiotropic cytokine involved in the development, survival, and activation of natural killer (NK) cells, CD8+ memory T cells, and innate lymphoid cells. Unlike other cytokines, IL-15 signals through a unique *trans*-presentation mechanism: IL-15Rα binds IL-15 intracellularly in antigen-presenting cells and "presents" the cytokine to neighboring cells expressing the IL-2/IL-15 receptor βγ subunits (IL-2Rβ/γc). This process ensures localized and controlled immune activation, preventing systemic toxicity.
Recombinant IL-15Rα proteins are engineered to mimic the native receptor’s structure and function. Produced via mammalian or bacterial expression systems, these proteins typically include the extracellular domain of IL-15Rα, which is essential for IL-15 binding and stabilization. The recombinant form is often fused with Fc regions or tags to enhance solubility, stability, and pharmacokinetics.
Research on IL-15Rα recombinant proteins has gained momentum due to their therapeutic potential. In cancer immunotherapy, IL-15Rα/IL-15 complexes exhibit enhanced efficacy compared to IL-15 alone, promoting sustained NK and T cell responses. They are also explored in treating viral infections and autoimmune diseases by modulating immune cell activity. Additionally, IL-15Rα serves as a tool to study IL-15 signaling dynamics and receptor interactions.
Despite promise, challenges remain, including optimizing delivery systems and minimizing off-target effects. Ongoing clinical trials aim to harness IL-15Rα-based therapies for improved immune modulation, highlighting its significance in translational immunology.
×
