| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NECTIN2 |
| Uniprot No | Q92692 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 32-360aa |
| 氨基酸序列 | QDVRVQVLPEVRGQLGGTVELPCHLLPPVPGLYISLVTWQRPDAPANHQNVAAFHPKMGPSFPSPKPGSERLSFVSAKQSTGQDTEAELQDATLALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRVIAKPKNQAEAQKVTFSQDPTTVALCISKEGRPPARISWLSSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVEHESFEEPALIPVTLSVRYPPEVSISGYDDNWYLGRTDATLSCDVRSNPEPTGYDWSTTSGTFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTNAVGMGRAEQVIFVRETPRASPRDVGPL |
| 预测分子量 | 36.58 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 **NECTIN2(PVRL2/CD112)重组蛋白** 的模拟参考文献示例(实际文献需通过学术数据库查询)：
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1. **文献名称**: *"Expression and Functional Characterization of Recombinant NECTIN2 in Cancer Immunotherapy"*
**作者**: Smith A, et al.
**摘要**: 研究报道了在大肠杆菌中高效表达重组人NECTIN2蛋白，并验证其与免疫检查点分子 **CD226** 的结合能力。实验表明，重组NECTIN2可阻断肿瘤微环境中的免疫抑制信号，增强T细胞抗肿瘤活性。
2. **文献名称**: *"Structural Analysis of NECTIN2 Reveals Key Epitopes for Herpesvirus Entry"*
**作者**: Tanaka K, et al.
**摘要**: 通过X射线晶体学解析了重组NECTIN2的胞外域结构，鉴定出疱疹病毒(如HSV-1)侵入宿主细胞的关键结合位点，为抗病毒药物设计提供了结构基础。
3. **文献名称**: *"Recombinant NECTIN2 as a Biomarker in Autoimmune Diseases"*
**作者**: Lee JH, et al.
**摘要**: 开发了基于重组NECTIN2蛋白的ELISA检测方法，发现类风湿性关节炎患者血清中可溶性NECTIN2水平显著升高，提示其作为疾病活动度生物标志物的潜力。
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**注**：以上为模拟内容，真实文献建议通过 **PubMed/Google Scholar** 检索关键词(如"Nectin2 recombinant protein"、"PVRL2 expression")获取。
Nectin-2. also known as PVRL2 (poliovirus receptor-related 2), is a transmembrane glycoprotein belonging to the nectin family of cell adhesion molecules. It plays a critical role in mediating cell-cell adhesion and communication, particularly in epithelial and endothelial tissues, by forming homophilic or heterophilic interactions with other nectins (e.g., nectin-1 or nectin-3) or the immunoglobulin-like receptor DNAM-1. Structurally, it consists of three extracellular immunoglobulin-like domains, a transmembrane region, and a cytoplasmic tail that interacts with afadin, a scaffold protein linking nectins to the actin cytoskeleton. Beyond its structural functions, nectin-2 is involved in immune regulation, viral entry, and cancer progression.
Recombinant nectin-2 protein is engineered through molecular cloning and expression systems (e.g., mammalian, insect, or bacterial cells) to produce soluble or tagged variants for research and therapeutic applications. This protein is widely used to study nectin-2’s interactions with ligands like DNAM-1. CD96. or viral glycoproteins (e.g., herpes simplex virus glycoprotein D), which exploit nectin-2 as an entry receptor. In cancer biology, nectin-2 is overexpressed in certain malignancies (e.g., breast, ovarian, or lung cancers) and is implicated in tumor immune evasion by modulating T-cell activity via DNAM-1 pathways. Recombinant nectin-2 helps dissect these mechanisms and screen potential inhibitors.
Therapeutic interest in nectin-2 has grown due to its dual role in viral pathogenesis and immune modulation. For instance, blocking nectin-2 interactions may hinder viral infection or enhance antitumor immunity. Recombinant proteins also aid in developing vaccines or antibody-based therapies. Additionally, nectin-2’s involvement in neurological disorders, such as Alzheimer’s disease (via synaptic adhesion), underscores its biomedical relevance. However, challenges remain in optimizing recombinant nectin-2’s stability, binding specificity, and scalability for clinical use. Ongoing research aims to harness its multifaceted biological functions for targeted interventions in cancer, infectious diseases, and neurodegeneration.
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