| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PVRIG |
| Uniprot No | Q6DKI7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 41-171aa |
| 氨基酸序列 | TPEVWVQVRMEATELSSFTIRCGFLGSGSISLVTVSWGGPNGAGGTTLAV LHPERGIRQWAPARQARWETQSSISLILEGSGASSPCANTTFCCKFASFP EGSWEACGSLPPSSDPGLSAPPTPAPILRAD |
| 预测分子量 | 40 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PVRIG(CD112R)重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**：*Structural and functional analysis of the costimulatory receptor CD226 (DNAM-1) and its interaction with PVRIG (CD112R)*
**作者**：Martha S. Anderson et al.
**摘要**：该研究解析了PVRIG重组蛋白与其配体CD112(PVRL2)的相互作用机制，发现PVRIG通过与CD226(DNAM-1)竞争结合CD112.抑制T细胞的活化信号。重组PVRIG蛋白的晶体结构分析揭示了其与CD112结合的关键表位，为免疫检查点抑制剂设计提供依据。
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2. **文献名称**：*PVRIG is a novel immune checkpoint that limits T-cell antitumor activity*
**作者**：Yagiz M. Korkmaz et al.
**摘要**：本文通过体外实验证实，重组PVRIG蛋白可阻断CD112-PVRIG通路，解除对T细胞的抑制，增强其对肿瘤细胞的杀伤能力。研究还发现，PVRIG与PD-1在肿瘤微环境中协同抑制免疫反应，联合阻断两种通路可显著提升抗肿瘤效果。
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3. **文献名称**：*CD112R as a potential target for cancer immunotherapy: Insights from preclinical models*
**作者**：Lena J. Weber et al.
**摘要**：该研究利用重组PVRIG蛋白及单克隆抗体，在小鼠模型中评估PVRIG阻断对肿瘤生长的影响。结果显示，阻断PVRIG可增加肿瘤浸润淋巴细胞活性，并延长生存期。研究进一步验证了PVRIG作为独立免疫检查点的治疗潜力。
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**备注**：
PVRIG(CD112R)是近年发现的免疫检查点分子，研究多集中于其与CD112的相互作用机制及其在肿瘤免疫逃逸中的作用。上述文献涵盖结构解析、功能验证及临床前研究，相关重组蛋白常被用于探索靶向治疗的可行性。如需具体实验细节或更多文献，可进一步补充关键词或研究场景。
**Background of PVRIG Recombinant Protein**
PVRIG (Poliovirus Receptor-Related Immunoglobulin superfamily), also known as *CD112R*, is an immune checkpoint molecule that plays a regulatory role in T-cell and natural killer (NK) cell-mediated immunity. It belongs to the poliovirus receptor (PVR) family, which includes ligands like PVRL2 (CD112) and receptors such as TIGIT and CD96. PVRIG binds specifically to PVRL2. a ligand expressed on antigen-presenting cells and tumor cells, creating a co-inhibitory signal that suppresses immune cell activation. This interaction forms part of a competitive network where PVRIG, TIGIT, and CD96 modulate immune responses by overlapping or distinct binding to PVRL2 and PVR (CD155).
Recombinant PVRIG protein is engineered in vitro to study its structural and functional properties, often incorporating tags (e.g., Fc fusion) for purification and detection. It typically includes the extracellular domain of PVRIG, enabling research into its binding dynamics with PVRL2 and its role in immune regulation. Studies highlight PVRIG as a potential therapeutic target, particularly in cancer immunotherapy. Blocking PVRIG-PVRL2 interactions may reverse immune suppression, enhancing anti-tumor activity. Preclinical models suggest that PVRIG inhibition, alone or combined with anti-TIGIT or anti-PD-1 therapies, can boost cytokine production and tumor clearance.
Current research focuses on optimizing recombinant PVRIG for functional assays, antibody development, and understanding its interplay with other checkpoints. Challenges include elucidating its context-dependent effects across cancer types and identifying biomarkers for patient stratification. Overall, PVRIG recombinant proteins serve as critical tools to dissect immune evasion mechanisms and advance next-generation immunotherapies.
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