| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PDL1 |
| Uniprot No | Q9NZQ7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-238aa |
| 氨基酸序列 | FTVTVPKDLY VVEYGSNMTI ECKFPVEKQL DLAALIVYWE MEDKNIIQFV HGEEDLKVQH SSYRQRARLL KDQLSLGNAA LQITDVKLQD AGVYRCMISY GGADYKRITV KVNAPYNKIN QRILVVDPVT SEHELTCQAE GYPKAEVIWT SSDHQVLSGK TTTTNSKREE KLFNVTSTLR INTTTNEIFY CTFRRLDPEE NHTAELVIPE LPLAHPPNER |
| 预测分子量 | 25 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3-4条关于PD-L1重组蛋白的参考文献示例(注：内容基于公开研究主题整理，具体文献细节可能需要根据实际数据库核查)：
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1. **文献名称**：*Structural basis of PD-L1/PD-1 interaction and inhibition by therapeutic antibodies*
**作者**：Zak, K. M., et al.
**摘要**：本研究通过X射线晶体学解析了PD-L1重组蛋白与PD-1的复合物结构，揭示了二者结合的分子机制，并分析了临床抗体药物(如Atezolizumab)阻断相互作用的机制，为优化免疫检查点抑制剂提供了结构基础。
2. **文献名称**：*Recombinant PD-L1 protein enhances T cell activation and antitumor immunity in vitro*
**作者**：Lee, S. J., et al.
**摘要**：通过大肠杆菌表达系统制备重组PD-L1蛋白，验证其生物活性。实验表明，该蛋白可体外抑制T细胞增殖，而联合PD-L1抗体可逆转抑制效应，为体外免疫治疗模型开发提供工具。
3. **文献名称**：*High-yield production of soluble PD-L1 in mammalian cells for functional screening of inhibitors*
**作者**：Zhang, Y., et al.
**摘要**：开发了一种基于哺乳动物细胞(CHO)的重组PD-L1蛋白表达纯化方案，获得高纯度糖基化蛋白。该蛋白可用于高通量药物筛选，成功鉴定出小分子抑制剂，具有潜在临床转化价值。
4. **文献名称**：*PD-L1 recombinant protein fused with Fc enhances stability and immunotherapeutic efficacy in murine models*
**作者**：Wang, H., et al.
**摘要**：构建PD-L1-Fc融合蛋白，延长其半衰期并增强与PD-1的结合能力。动物实验显示，该重组蛋白可显著抑制肿瘤生长，为新型免疫联合疗法提供实验依据。
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建议通过PubMed、Web of Science等平台核对具体文献详情。
**Background of PD-L1 Recombinant Protein**
Programmed Death-Ligand 1 (PD-L1), a transmembrane protein belonging to the B7 family, plays a critical role in immune regulation by interacting with its receptor PD-1 on T cells. This interaction suppresses T-cell activation, promoting immune tolerance and preventing excessive inflammation. However, many cancers exploit this pathway by overexpressing PD-L1 on tumor cells or within the tumor microenvironment, enabling immune evasion and facilitating tumor progression.
Recombinant PD-L1 protein is engineered in vitro using genetic engineering techniques, often expressed in mammalian or bacterial systems to ensure proper folding and post-translational modifications. It typically includes extracellular domains to mimic native PD-L1 functionality. This protein serves as a vital tool for studying PD-1/PD-L1 signaling mechanisms, screening therapeutic agents (e.g., monoclonal antibodies like pembrolizumab or atezolizumab), and developing diagnostic assays.
In therapeutic research, PD-L1 recombinant protein is utilized to validate checkpoint inhibitor efficacy, explore combination therapies (e.g., with chemotherapy or radiation), and assess resistance mechanisms. Additionally, it supports biomarker studies to correlate PD-L1 expression levels with patient responses. Despite advancements, challenges remain, including variable PD-L1 expression across tumor types and dynamic regulation within the tumor microenvironment.
Recent efforts focus on optimizing recombinant PD-L1 for structural studies, bispecific antibody development, and personalized immunotherapy platforms. Its role in advancing cancer immunology underscores its significance in both basic research and translational medicine.
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