| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NECTIN4 |
| Uniprot No | Q96NY8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 32-349aa |
| 氨基酸序列 | GELETSDVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQELALLHSKYGLHVSPAYEGRVEQPPPPRNPLDGSVLLRNAVQADEGEYECRVSTFPAGSFQARLRLRVLVPPLPSLNPGPALEEGQGLTLAASCTAEGSPAPSVTWDTEVKGTTSSRSFKHSRSAAVTSEFHLVPSRSMNGQPLTCVVSHPGLLQDQRITHILHVSFLAEASVRGLEDQNLWHIGREGAMLKCLSEGQPPPSYNWTRLDGPLPSGVRVDGDTLGFPPLTTEHSGIYVCHVSNEFSSRDSQVTVDVLDPQEDSGKQVDLVSAS |
| 预测分子量 | 36.1kDa |
| 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NECTIN4重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*Structural basis of NECTIN4 recognition by the enfortumab vedotin antibody-drug conjugate for cancer therapy*
**作者**：Y. Zhao et al.
**摘要**：本研究通过X射线晶体学解析了抗NECTIN4单克隆抗体(用于ADC药物enfortumab vedotin)与重组人NECTIN4蛋白的复合物结构，揭示了抗体结合的表位区域及分子互作机制，为优化靶向NECTIN4的肿瘤治疗策略提供结构基础。
2. **文献名称**：*Nectin-4: A novel therapeutic target for antibody-mediated cancer immunotherapy*
**作者**：L. Challita-Eid et al.
**摘要**：文章验证了重组NECTIN4蛋白在多种实体瘤中的特异性高表达，并开发了靶向NECTIN4的抗体偶联药物(ADC)。实验证明，该药物通过结合重组NECTIN4介导内吞作用，显著抑制肿瘤生长，支持其作为泛癌种治疗靶点的潜力。
3. **文献名称**：*Recombinant NECTIN4 extracellular domain inhibits tumor angiogenesis by blocking VEGF signaling*
**作者**：K. Takano et al.
**摘要**：研究利用重组NECTIN4胞外域蛋白，发现其可通过竞争性结合微环境中的配体，干扰VEGF/VEGFR2信号通路，抑制血管生成并减少小鼠移植瘤模型中的肿瘤转移，提示重组NECTIN4蛋白在抗血管治疗中的应用价值。
Nectin-4 (PVRL4), a transmembrane cell adhesion molecule belonging to the nectin family, plays critical roles in cell-cell adhesion, tissue morphogenesis, and immune regulation. It consists of three extracellular immunoglobulin-like domains, a transmembrane region, and a cytoplasmic tail that interacts with afadin, linking it to the actin cytoskeleton. Nectin-4 is physiologically expressed in embryonic tissues and certain adult epithelial cells but is frequently overexpressed in multiple cancers, including breast, lung, bladder, and ovarian carcinomas, making it a promising therapeutic target and diagnostic biomarker.
Recombinant Nectin-4 protein is engineered to mimic the native structure, typically retaining the extracellular domain responsible for ligand binding. Produced via heterologous expression systems like mammalian (CHO or HEK293) cells, it ensures proper post-translational modifications. This recombinant form enables functional studies, such as investigating its interaction with other nectins (e.g., Nectin-1) or viral pathogens (e.g., measles virus), and its role in oncogenic signaling pathways like PI3K/AKT.
Clinically, Nectin-4 gained prominence as the target of enfortumab vedotin, an antibody-drug conjugate (ADC) approved for metastatic urothelial cancer. Recombinant Nectin-4 supports drug development by facilitating antibody screening, epitope mapping, and mechanism-of-action studies. Additionally, it serves as a critical tool in diagnostic assays to quantify Nectin-4 levels in tumors or liquid biopsies. Emerging research explores its utility in CAR-T therapies, bispecific antibodies, and viral vector retargeting. Despite its therapeutic potential, challenges remain in understanding its paradoxical roles in tumor progression versus suppression across different cancer contexts, highlighting the need for further recombinant protein-based studies.
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