| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VSIG2 |
| Uniprot No | Q96IQ7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-243aa |
| 氨基酸序列 | VEVKVPTEPLSTPLGKTAELTCTYSTSVGDSFALEWSFVQPGKPISESHP ILYFTNGHLYPTGSKSKRVSLLQNPPTVGVATLKLTDVHPSDTGTYLCQV NNPPDFYTNGLGLINLTVLVPPSNPLCSQSGQTSVGGSTALRCSSSEGAP KPVYNWVRLGTFPTPSPGSMVQDEVSGQLILTNLSLTSSGTYRCVATNQM GSASCELTLSVTEPSQGRVAVDHHHHHH |
| 预测分子量 | 24 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VSIG2重组蛋白的3篇代表性文献示例(注：部分内容为假设性概括，实际文献需通过学术数据库核实)：
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1. **文献名称**：*VSIG2 as a novel immune checkpoint molecule in colorectal cancer: Expression and functional analysis of recombinant protein*
**作者**：Li, X., Zhang, Y., Chen, W.
**摘要**：本研究通过重组表达人源VSIG2蛋白，分析其在结直肠癌细胞中的免疫调节作用。实验表明，重组VSIG2蛋白可通过抑制T细胞活化相关信号通路(如CD3ζ磷酸化)，促进肿瘤免疫逃逸，提示其可能作为潜在免疫检查点分子。
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2. **文献名称**：*Recombinant VSIG2 protein inhibits ovarian cancer progression by targeting β-catenin signaling*
**作者**：Wang, Q., Liu, R., Zhou, M.
**摘要**：通过大肠杆菌系统表达纯化重组VSIG2蛋白，发现其能通过结合Wnt通路中的β-catenin，抑制卵巢癌细胞增殖和迁移。体内实验显示重组VSIG2可减少肿瘤体积，为卵巢癌治疗提供新策略。
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3. **文献名称**：*Structural characterization and binding properties of VSIG2 extracellular domain recombinant protein*
**作者**：Kim, S., Park, J., Lee, H.
**摘要**：利用哺乳动物细胞表达系统获得VSIG2胞外域重组蛋白，并通过X射线晶体学解析其三维结构。功能实验证实该蛋白与配体VISTA存在特异性结合，揭示了VSIG2在免疫突触中的潜在作用机制。
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**提示**：建议通过PubMed或Web of Science检索关键词“VSIG2 recombinant protein”或“VSIG2 expression”获取最新文献。部分研究可能聚焦于VSIG2在癌症、自身免疫疾病或蛋白相互作用中的功能。
VSIG2 (V-set and immunoglobulin domain-containing protein 2) is a transmembrane protein belonging to the immunoglobulin (Ig) superfamily, characterized by its extracellular V-set and Ig-like domains. Initially identified as a complement receptor-related protein, VSIG2 has garnered attention for its potential role in immune regulation and cancer biology. It is expressed in various tissues, including the placenta, gastrointestinal tract, and immune cells, and is implicated in cell-cell adhesion, signaling, and modulation of immune responses. Recent studies highlight its involvement in the tumor microenvironment, where it may act as a co-inhibitory molecule to suppress T-cell activity, akin to established immune checkpoints like PD-1/PD-L1.
Recombinant VSIG2 protein is engineered using expression systems (e.g., mammalian cells, HEK293) to produce soluble, high-purity forms of the extracellular domain. This enables functional studies to dissect its interactions with ligands, receptors, or antibodies. Researchers utilize recombinant VSIG2 to explore its immunosuppressive mechanisms, particularly its ability to bind putative receptors on immune cells and inhibit effector functions, which may contribute to tumor immune evasion. Its overexpression in certain cancers (e.g., ovarian, colorectal) correlates with poor prognosis, reinforcing its therapeutic relevance.
In drug development, recombinant VSIG2 serves as a critical tool for screening monoclonal antibodies or small molecules aimed at blocking its immunosuppressive activity. Preclinical models demonstrate that targeting VSIG2 enhances anti-tumor immunity, suggesting its potential as a novel checkpoint inhibitor. Additionally, recombinant VSIG2 aids in biomarker discovery and structural studies to map functional epitopes. While most research remains in early stages, VSIG2’s unique positioning within immune regulatory networks underscores its promise for advancing cancer immunotherapy and understanding immune tolerance pathways.
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