| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | BST2 |
| Uniprot No | Q10589 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 40-180aa |
| 氨基酸序列 | PLIIFTIKANSEACRDGLRAVMECRNVTHLLQQELTEAQKGFQDVEAQAA TCNHTVMALMASLDAEKAQGQKKVEELEGEITTLNHKLQDASAEVERLRR ENQVLSVRIADKKYYPSSQDSSSAAAPQLLIVLLGLSALLQ |
| 预测分子量 | 41 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BST2重组蛋白的3篇参考文献示例(注：以下信息为示例，建议通过学术数据库获取真实文献)：
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1. **文献名称**: "Structural characterization of recombinant BST2 and its role in viral restriction"
**作者**: Neil, S. et al.
**摘要**: 该研究通过重组表达人源BST2蛋白，解析其跨膜结构域与病毒包膜蛋白的相互作用机制，证实BST2通过物理束缚病毒粒子抑制HIV-1释放。
2. **文献名称**: "Recombinant BST2 protein enhances innate immune signaling in dendritic cells"
**作者**: Garcia-Beltran, W. et al.
**摘要**: 研究利用重组BST2蛋白刺激树突状细胞，发现其通过激活NF-κB通路促进干扰素分泌，揭示了BST2在抗病毒免疫中的双重功能(抑制病毒释放和调控免疫应答)。
3. **文献名称**: "Expression and purification of functional BST2 extracellular domain for therapeutic antibody development"
**作者**: Zhang, Y. et al.
**摘要**: 开发了一种高效重组表达系统，纯化出具有生物活性的BST2胞外段蛋白，并用于筛选靶向BST2的单克隆抗体，为抗病毒药物研发提供新策略。
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如需真实文献，建议在PubMed或Google Scholar检索关键词：**BST2 recombinant protein**, **Tetherin expression**, **CD317 purification**。
**Background on BST2 Recombinant Protein**
BST2 (Bone Marrow Stromal Cell Antigen 2), also known as CD317 or HM1.24 antigen, is a type II transmembrane glycoprotein implicated in innate immunity and viral restriction. It is broadly expressed in immune cells, including dendritic cells, B cells, and macrophages, and functions as a host restriction factor by inhibiting the release of enveloped viruses, such as HIV-1. through a process termed "tethering." BST2 anchors nascent viral particles to the cell membrane, physically blocking their dissemination. However, viruses like HIV-1 counteract this via accessory proteins (e.g., Vpu), which degrade BST2 or sequester it away from budding sites.
Structurally, BST2 features an N-terminal cytoplasmic domain, a transmembrane region, an extracellular coiled-coil domain, and a C-terminal glycosylphosphatidylinositol (GPI) anchor, enabling dual membrane attachment. This unique topology supports its antiviral activity and cellular localization. Beyond virology, BST2 participates in immune signaling, cell adhesion, and cancer progression, with overexpression observed in certain malignancies.
Recombinant BST2 proteins are engineered using expression systems like *E. coli*, mammalian cells, or insect cells to ensure proper post-translational modifications. These proteins retain functional domains critical for studying BST2-ligand interactions, antiviral mechanisms, or therapeutic targeting. Purified recombinant BST2 is utilized in structural studies, antibody development, and high-throughput screens to identify inhibitors or enhancers of its antiviral activity. Additionally, it serves as a tool to dissect BST2’s role in immune regulation and cancer biology.
Overall, BST2 recombinant protein is a vital resource for advancing research in virology, immunology, and oncology, bridging mechanistic insights with translational applications.
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