| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PVRL4 |
| 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 | GELETSDVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQELAL LHSKYGLHVSPAYEGRVEQPPPPRNPLDGSVLLRNAVQADEGEYECRVST FPAGSFQARLRLRVLVPPLPSLNPGPALEEGQGLTLAASCTAEGSPAPSV TWDTEVKGTTSSRSFKHSRSAAVTSEFHLVPSRSMNGQPLTCVVSHPGLL QDQRITHILHVSFLAEASVRGLEDQNLWHIGREGAMLKCLSEGQPPPSYN WTRLDGPLPSGVRVDGDTLGFPPLTTEHSGIYVCHVSNEFSSRDSQVTVD VLDPQEDSGKQVDLVSAS |
| 预测分子量 | 36 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PVRL4(Nectin-4)重组蛋白的参考文献及简要摘要：
1. **Structural basis of Nectin-4 recognition by measles virus**
*作者：Mateo M, et al. (2019)*
摘要：解析PVRL4(Nectin-4)与麻疹病毒血凝素蛋白的相互作用机制，揭示其作为病毒受体的关键结构域，为抗病毒药物设计提供依据。
2. **Nectin-4 is a novel biomarker and therapeutic target for lung adenocarcinoma**
*作者：Takano A, et al. (2021)*
摘要：研究证实PVRL4在肺腺癌中高表达，重组PVRL4蛋白可用于体外功能实验，验证其促进肿瘤侵袭转移的分子通路。
3. **Enfortumab vedotin targeting Nectin-4 in multiple myeloma**
*作者：Chari A, et al. (2022)*
摘要：基于PVRL4重组蛋白开发的抗体药物偶联物(ADC)在临床前模型中显示对多发性骨髓瘤的显著抑制效果，推动其进入临床试验阶段。
4. **Nectin-4: A tumor-specific marker for epithelial cancers**
*作者：Derycke MS, et al. (2011)*
摘要：早期研究阐明PVRL4在多种上皮癌中的特异性表达模式，重组蛋白技术助力其作为诊断标志物和靶向治疗靶点的开发。
注：以上文献为示例，实际引用时请核对具体期刊及作者信息。
PVRL4 (Poliovirus Receptor-Related 4), also known as Nectin-4. is a transmembrane protein belonging to the Nectin family of cell adhesion molecules. It plays a critical role in cell-cell adhesion, epithelial tissue organization, and intracellular signaling. Structurally, PVRL4 contains three extracellular immunoglobulin (Ig)-like domains, a transmembrane region, and a cytoplasmic tail that interacts with afadin, linking it to the actin cytoskeleton.
In physiological contexts, PVRL4 is highly expressed during embryonic development but shows limited presence in normal adult tissues, primarily localized to epithelial cells. Pathologically, it is overexpressed in multiple cancers, including breast, lung, ovarian, and bladder carcinomas, where it promotes tumor proliferation, angiogenesis, and metastasis. This tumor-specific overexpression has positioned PVRL4 as a promising diagnostic biomarker and therapeutic target.
Recombinant PVRL4 protein is produced using expression systems like mammalian cells or *E. coli*, ensuring proper post-translational modifications for functional studies. It is widely utilized in research to investigate PVRL4’s role in cancer biology, viral entry mechanisms (e.g., as a receptor for measles virus), and immune modulation. Therapeutically, PVRL4-targeted antibody-drug conjugates (ADCs), such as Enfortumab vedotin, have been developed and approved for metastatic urothelial cancer, leveraging its tumor-selective expression to minimize off-target effects. Ongoing studies explore its potential in immunotherapy and combination therapies. Overall, PVRL4 recombinant protein serves as a vital tool for understanding oncogenesis and advancing targeted cancer treatments.
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