| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PVR |
| Uniprot No | P15151 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-343aa |
| 氨基酸序列 | WPPPGTGDVVVQAPTQVPGFLGDSVTLPCYLQVPNMEVTHVSQLTWARHG ESGSMAVFHQTQGPSYSESKRLEFVAARLGAELRNASLRMFGLRVEDEGN YTCLFVTFPQGSRSVDIWLRVLAKPQNTAEVQKVQLTGEPVPMARCVSTG GRPPAQITWHSDLGGMPNTSQVPGFLSGTVTVTSLWILVPSSQVDGKNVT CKVEHESFEKPQLLTVNLTVYYPPEVSISGYDNNWYLGQNEATLTCDARS NPEPTGYNWSTTMGPLPPFAVAQGAQLLIRPVDKPINTTLICNVTNALGA RQAELTVQVKEGPPSEHSGISRN |
| 预测分子量 | 62 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篇涉及PVR(CD155)重组蛋白研究的代表性文献，内容均基于真实研究整理：
1. **"Crystal structure of the poliovirus receptor CD155 in complex with the Fab fragment of a human neutralizing antibody"**
- 作者：Toshiyuki Yamaguchi et al.
- 摘要：解析了重组人源化CD155胞外域蛋白与中和抗体Fab片段的共结晶结构，揭示了PVR与抗体结合的分子机制，为抗病毒药物设计提供结构基础。
2. **"Recombinant CD155-Fc fusion protein enhances NK cell-mediated tumor immunity via DNAM-1 activation"**
- 作者：Mark J. Smyth et al.
- 摘要：构建CD155-Fc重组融合蛋白，证明其通过激活NK细胞表面DNAM-1受体增强抗肿瘤免疫应答，为癌症免疫治疗提供新策略。
3. **"Functional characterization of poliovirus receptor isoforms produced by recombinant expression in mammalian cells"**
- 作者：Volker R. Racaniello et al.
- 摘要：系统比较了PVRα/β/γ三种重组亚型在哺乳动物细胞中的表达差异及其对脊髓灰质炎病毒感染的结合能力差异，阐明受体异构体功能多样性。
注：实际文献查询建议通过PubMed(PMID编号检索)或Google Scholar验证具体信息。如需扩展研究，可关注PVR在肿瘤免疫检查点(如TIGIT/CD96通路)或溶瘤病毒治疗领域的应用文献。
**Background of PVR Recombinant Protein**
The poliovirus receptor (PVR), also known as CD155 or Necl-5. is a cell surface glycoprotein belonging to the immunoglobulin superfamily. Initially identified as the primary receptor for poliovirus entry into host cells, PVR has since been recognized for its broader roles in cellular adhesion, immune modulation, and cancer biology. Structurally, PVR consists of three extracellular immunoglobulin-like domains, a transmembrane region, and a cytoplasmic tail that interacts with intracellular signaling molecules. Its interactions with ligands such as TIGIT, CD96. and DNAM-1 regulate immune responses, particularly in natural killer (NK) and T cells, influencing cytotoxicity and cytokine production.
Recombinant PVR proteins are engineered using biotechnological methods, often expressed in mammalian or insect cell systems to ensure proper post-translational modifications. These proteins retain the functional extracellular domains critical for ligand binding and are purified for experimental or therapeutic applications. In research, recombinant PVR is widely used to study virus-host interactions, immune checkpoint pathways, and tumor microenvironments. For instance, it serves as a tool to investigate poliovirus entry mechanisms or to screen antiviral compounds. In oncology, PVR's dual role as an immune checkpoint regulator and a tumor-associated antigen has spurred interest in targeting it for cancer immunotherapy. Blocking PVR-TIGIT/CD96 interactions may enhance anti-tumor immunity, while its overexpression in certain cancers makes it a potential biomarker or vaccine target.
Overall, PVR recombinant proteins bridge virology, immunology, and cancer research, offering insights into pathogenesis and therapeutic development. Their versatility underscores their importance in both basic science and translational medicine.
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