纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | B7H4 |
Uniprot No | Q7Z7D3 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 26-258aa |
氨基酸序列 | IIGFGISGRHSITVTTVASAGNIGEDGILSCTFEPDIKLSDIVIQWLKEGVLGLVHEFKEGKDELSEQDEMFRGRTAVFADQVIVGNASLRLKNVQLTDAGTYKCYIITSKGKGNANLEYKTGAFSMPEVNVDYNASSETLRCEAPRWFPQPTVVWASQVDQGANFSEVSNTSFELNSENVTMKVVSVLYNVTINNTYSCMIENDIAKATGDIKVTESEIKRRSHLQLLNSKA |
预测分子量 | 52.6 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B7H4重组蛋白的3篇参考文献,按文献名称、作者和摘要内容简要整理:
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1. **文献名称**:*B7-H4 facilitates tumor cell immune evasion through regulation of T-cell activation*
**作者**:Zang, X., et al.
**摘要**:
该研究探讨了B7H4重组蛋白在肿瘤免疫逃逸中的作用。通过体外实验发现,B7H4通过与T细胞表面受体结合,抑制T细胞活化和细胞因子分泌,揭示了其在肿瘤微环境中介导免疫抑制的机制。
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2. **文献名称**:*Development of a recombinant B7-H4 protein-based ELISA for cancer biomarker detection*
**作者**:Chen, Y., et al.
**摘要**:
研究团队成功表达并纯化了重组B7H4蛋白,并基于此开发了一种高灵敏度的ELISA检测方法。实验验证了其在卵巢癌和乳腺癌患者血清中的高表达水平,表明其作为肿瘤诊断标志物的潜力。
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3. **文献名称**:*Targeting B7-H4 with a novel recombinant antibody enhances antitumor immunity in preclinical models*
**作者**:Smith, J., et al.
**摘要**:
该研究构建了针对B7H4的重组单克隆抗体,并在小鼠肿瘤模型中评估其疗效。结果显示,该抗体能阻断B7H4的免疫抑制功能,显著增强CD8+ T细胞活性并抑制肿瘤生长,为临床免疫治疗提供了新策略。
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**备注**:以上文献信息为示例,实际引用时需根据具体研究来源调整。建议通过PubMed或Google Scholar搜索关键词“B7H4 recombinant protein”或“B7-H4 immunotherapy”获取最新文献。
B7H4 (B7 homolog 4), also known as VTCN1 or B7x, is a transmembrane protein belonging to the B7 immune checkpoint family. Discovered in 2003. it shares structural homology with other B7 family members like B7-1 (CD80) and B7-H1 (PD-L1), featuring extracellular IgV and IgC domains. Unlike classical co-stimulatory molecules, B7H4 primarily delivers co-inhibitory signals to suppress T-cell activation, proliferation, and cytokine production, though its receptor remains incompletely characterized.
Recombinant B7H4 proteins are engineered for functional studies and therapeutic development. Produced in mammalian (e.g., CHO cells) or bacterial expression systems, these proteins typically include the extracellular domain (ECD) fused with Fc tags or histidine tags to facilitate purification and detection. Structural studies using recombinant B7H4 have revealed its role in immune evasion, particularly in cancers.
B7H4 is overexpressed in diverse malignancies (e.g., breast, ovarian, lung cancers) and correlates with poor prognosis. Its expression in tumor cells and tumor-associated macrophages creates an immunosuppressive microenvironment, making it a promising therapeutic target. Recombinant B7H4 serves as a critical tool for screening monoclonal antibodies, bispecific antibodies, and antibody-drug conjugates (ADCs) in preclinical research. Notably, B7H4-targeted therapies are being explored in combination with PD-1/PD-L1 inhibitors to overcome resistance to existing checkpoint blockade.
Despite therapeutic potential, challenges persist, including understanding B7H4’s ligand-receptor interactions and managing its heterogeneous expression patterns. Recombinant protein-based assays continue to advance mechanistic insights and drug discovery for this emerging immune checkpoint.
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