| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PVRL1 |
| Uniprot No | Q15223 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-355aa |
| 氨基酸序列 | QVVQVNDSMY GFIGTDVVLH CSFANPLPSV KITQVTWQKS TNGSKQNVAI YNPSMGVSVL APYRERVEFL RPSFTDGTIR LSRLELEDEG VYICEFATFP TGNRESQLNL TVMAKPTNWI EGTQAVLRAK KGQDDKVLVA TCTSANGKPP SVVSWETRLK GEAEYQEIRN PNGTVTVISR YRLVPSREAH QQSLACIVNY HMDRFKESLT LNVQYEPEVT IEGFDGNWYL QRMDVKLTCK ADANPPATEY HWTTLNGSLP KGVEAQNRTL FFKGPINYSL AGTYICEATN PIGTRSGQVE VNITEFPYTP SPPEHGRRAG PVPTA |
| 预测分子量 | 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篇关于PVRL1(Nectin-1)重组蛋白的参考文献及摘要概括：
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1. **文献名称**: *"Structural and functional analysis of nectin-1/CD111 herpesvirus entry mediator"*
**作者**: Zhang N. et al. (2019)
**摘要**: 该研究通过重组表达PVRL1胞外域蛋白，解析其晶体结构，揭示了其与单纯疱疹病毒gD蛋白结合的分子机制，为抗病毒药物设计提供了结构基础。
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2. **文献名称**: *"Recombinant nectin-1 protein as a therapeutic target for alphaherpesvirus infection"*
**作者**: Campadelli-Fiume G. et al. (2020)
**摘要**: 研究团队利用昆虫细胞系统表达PVRL1重组蛋白，验证其作为疱疹病毒受体阻断剂的潜力，实验表明重组蛋白能有效抑制病毒进入宿主细胞。
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3. **文献名称**: *"Expression and characterization of human nectin-1 in mammalian cells for cell adhesion studies"*
**作者**: Takai Y. et al. (2016)
**摘要**: 通过哺乳动物表达系统制备重组PVRL1蛋白，证明其在体外促进细胞间粘附的功能，并发现其与细胞连接蛋白afadin的相互作用对上皮屏障形成至关重要。
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**备注**：以上文献为示例性内容，实际引用需根据具体研究方向选择合适论文(可通过PubMed或Google Scholar搜索关键词"PVRL1 recombinant protein"或"Nectin-1 expression"获取最新研究)。
PVRL1 (Poliovirus Receptor-Related 1), also known as Nectin-1. is a transmembrane glycoprotein belonging to the immunoglobulin superfamily. It plays critical roles in cell-cell adhesion, immune regulation, and viral entry, notably serving as a primary receptor for herpes simplex virus (HSV) types 1 and 2. Structurally, PVRL1 contains extracellular immunoglobulin-like domains that mediate homophilic and heterophilic interactions with other nectins or receptors, a transmembrane region, and a cytoplasmic tail involved in intracellular signaling. Its involvement in forming adherens junctions and immune synapses underscores its importance in tissue integrity and immune responses.
Recombinant PVRL1 protein is engineered using expression systems like mammalian cells, bacteria, or insect cells to produce purified, functional forms of the protein for research and therapeutic applications. Mammalian systems are often preferred to ensure proper glycosylation, which is crucial for ligand binding and viral interaction studies. The recombinant protein typically includes the extracellular domain, enabling in vitro analysis of adhesion mechanisms, viral entry pathways, or receptor-ligand binding assays.
In research, PVRL1 recombinant protein is utilized to study HSV infection mechanisms, screen antiviral compounds, and develop vaccines or neutralizing antibodies. It also aids in exploring its role in cancer, as PVRL1 is overexpressed in某些 tumors and implicated in cell proliferation and metastasis. Additionally, structural studies using recombinant PVRL1 help elucidate interaction interfaces with viral glycoproteins (e.g., HSV gD) or immune checkpoint molecules, informing drug design. Its therapeutic potential extends to being a target for antibody-based therapies or decoy receptors to block viral entry or modulate immune responses in autoimmune diseases.
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