| 纯度 | > 95 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | CD47 |
| Uniprot No | Q08722-3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-139aa |
| 氨基酸序列 | QLLFNKTKSVEFTFCNDTVVIPCFVTNMEAQNTTEVYVKWKFKGRDIYTF DGALNKSTVPTDFSSAKIEVSQLLKGDASLKMDKSDAVSHTGNYTCEVTE LTREGETIIELKYRVVSWFSP |
| 预测分子量 | 40 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CD47重组蛋白的3篇代表性文献示例(注：文献信息为示例，可能与实际发表情况存在差异，建议通过学术数据库核实)：
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1. **文献名称**：*CD47 functions as a molecular switch for myeloid cell phagocytosis*
**作者**：Oldenborg, P. A., et al.
**摘要**：该研究首次揭示了CD47通过与巨噬细胞表面SIRPα结合，传递“别吃我”信号，抑制吞噬作用，保护正常细胞免受免疫系统攻击，为肿瘤免疫逃逸机制提供了关键解释。
2. **文献名称**：*Targeting CD47 in cancer immunotherapy*
**作者**：Weiskopf, K., & Weissman, I. L.
**摘要**：综述了CD47在肿瘤微环境中的过表达现象，讨论了重组CD47蛋白或抗体阻断CD47-SIRPα通路的治疗潜力，包括增强巨噬细胞对癌细胞的清除能力及临床前模型中的疗效。
3. **文献名称**：*Structural and functional characterization of recombinant CD47-SIRPα interaction*
**作者**：Hatherley, D., et al.
**摘要**：通过X射线晶体学解析CD47与SIRPα的结合界面，阐明了二者相互作用的分子机制，为设计靶向CD47的重组蛋白药物(如融合蛋白或拮抗剂)提供了结构基础。
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如需具体文献，建议通过PubMed或Google Scholar检索关键词“CD47 recombinant protein”、“CD47-SIRPα therapy”获取最新研究。
CD47 is a widely expressed transmembrane protein belonging to the immunoglobulin superfamily, recognized as a critical "don't eat me" signal in regulating innate immune responses. It interacts with signal regulatory protein alpha (SIRPα) on phagocytic cells, such as macrophages, to inhibit phagocytosis and maintain cellular homeostasis. This interaction plays a key role in preventing the destruction of healthy cells, particularly red blood cells, by the immune system. However, CD47 is often overexpressed in cancer cells, enabling them to evade immune surveillance—a mechanism that has made it a prominent target in oncology research.
Recombinant CD47 protein is engineered through genetic modification to produce purified, functional CD47 extracellular domains in vitro. Commonly expressed in systems like mammalian cells (e.g., HEK293 or CHO cells) or insect cells, these proteins retain the structural integrity required for binding studies. They often incorporate tags (e.g., Fc fusion or His tags) to facilitate purification and detection. Recombinant CD47 serves as a vital tool for studying CD47-SIRPα signaling pathways, screening therapeutic antibodies, and developing cancer immunotherapies. For instance, CD47-blocking agents, including monoclonal antibodies and fusion proteins, are being explored to disrupt the "don't eat me" signal, thereby enhancing phagocytosis of tumor cells.
Beyond cancer, recombinant CD47 proteins contribute to research in autoimmune diseases, atherosclerosis, and tissue repair. Challenges remain in balancing therapeutic efficacy with on-target toxicity, as systemic CD47 inhibition may affect normal cells. Ongoing studies aim to optimize targeting strategies, such as tumor-specific antibody formats or combination therapies with checkpoint inhibitors. Overall, recombinant CD47 proteins are pivotal in advancing both mechanistic understanding and clinical translation of immune-modulating therapies.
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