| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VTCN1 |
| Uniprot No | Q7Z7D3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-258aa |
| 氨基酸序列 | FGISGRHSITVTTVASAGNIGEDGILSCTFEPDIKLSDIVIQWLKEGVLGLVHEFKEGKDELSEQDEMFRGRTAVFADQVIVGNASLRLKNVQLTDAGTYKCYIITSKGKGNANLEYKTGAFSMPEVNVDYNASSETLRCEAPRWFPQPTVVWASQVDQGANFSEVSNTSFELNSENVTMKVVSVLYNVTINNTYSCMIENDIAKATGDIKVTESEIKRRSHLQLLNSKA |
| 预测分子量 | 27.2 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VTCN1(B7-H4)重组蛋白的模拟参考文献示例(注：文献为示例性概括，非真实存在)：
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1. **文献名称**: *Recombinant VTCN1 Protein Suppresses T-cell Activation in Autoimmune Disease Models*
**作者**: Chen, L., et al.
**摘要**: 研究团队通过哺乳动物细胞表达系统制备了功能性VTCN1重组蛋白，并在类风湿性关节炎小鼠模型中验证其免疫抑制效果。实验表明，重组VTCN1可显著降低促炎细胞因子水平，提示其在自身免疫疾病治疗中的潜力。
2. **文献名称**: *Structural and Functional Characterization of B7-H4/VTCN1 Recombinant Protein*
**作者**: Patel, R., & Kim, H.
**摘要**: 该研究利用X射线晶体学解析了重组VTCN1蛋白的胞外结构域三维结构，并揭示其与受体相互作用的分子机制。体外实验证实，重组蛋白可有效抑制T细胞增殖，为靶向免疫检查点的药物设计提供结构基础。
3. **文献名称**: *Optimization of Escherichia coli Expression System for High-Yield VTCN1 Production*
**作者**: Zhang, Y., et al.
**摘要**: 通过密码子优化和发酵条件调控，成功在大肠杆菌中实现可溶性VTCN1重组蛋白的高效表达，纯度达95%以上。该方法为低成本规模化生产VTCN1用于临床前研究提供了可行方案。
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如需真实文献，建议在PubMed或Web of Science中使用关键词“VTCN1 recombinant protein”或“B7-H4 protein expression”进行检索。
VTCN1 (V-Set Domain Containing T-Cell Activation Inhibitor 1), also known as B7-H4 or B7S1. is an immune checkpoint protein belonging to the B7 family of co-stimulatory/co-inhibitory molecules. It plays a critical role in modulating T-cell-mediated immune responses, primarily functioning as a negative regulator of T-cell activation and proliferation. Structurally, VTCN1 is a transmembrane glycoprotein containing extracellular immunoglobulin variable (IgV) and immunoglobulin constant (IgC) domains, which mediate its interaction with potential receptors on immune cells. While its physiological receptor remains under investigation, studies suggest it may suppress T-cell function by inhibiting early activation signals, cytokine production, and cell cycle progression.
In normal tissues, VTCN1 expression is tightly regulated and often restricted to specific cell types. However, it is frequently overexpressed in various cancers, including breast, ovarian, lung, and pancreatic carcinomas, where it contributes to tumor immune evasion. This overexpression correlates with poor prognosis, increased metastatic potential, and resistance to therapies. Beyond oncology, aberrant VTCN1 expression has been implicated in autoimmune disorders and chronic inflammatory conditions, highlighting its dual role in immune homeostasis and pathology.
Recombinant VTCN1 proteins are engineered to study its biological functions and therapeutic potential. Typically produced in mammalian expression systems (e.g., HEK293 or CHO cells), these proteins retain post-translational modifications essential for receptor binding and functional activity. Researchers utilize purified VTCN1 extracellular domains to investigate immune checkpoint mechanisms, develop blocking antibodies, or design fusion proteins for immunotherapy. Recent advances include its incorporation into bispecific antibodies and chimeric antigen receptor (CAR) T-cell strategies aimed at reversing immune suppression in tumors. As an emerging therapeutic target, VTCN1 continues to attract attention for its tissue-specific expression pattern and potential to minimize systemic immune-related adverse effects compared to broader checkpoint inhibitors.
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