WB | 咨询技术 | Human,Mouse,Rat |
IF | 咨询技术 | Human,Mouse,Rat |
IHC | 咨询技术 | Human,Mouse,Rat |
ICC | 技术咨询 | Human,Mouse,Rat |
FCM | 咨询技术 | Human,Mouse,Rat |
Elisa | 1/10000 | Human,Mouse,Rat |
Aliases | BST2; Bone marrow stromal antigen 2; BST-2; HM1.24 antigen; Tetherin; CD317 |
Entrez GeneID | 684; |
WB Predicted band size | 20kDa |
Host/Isotype | Rabbit IgG |
Antibody Type | Primary antibody |
Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
Species Reactivity | Human |
Immunogen | Synthesized peptide derived from the Internal region of human BST-2. |
Formulation | Purified antibody in PBS with 0.05% sodium azide,0.5%BSA and 50% glycerol. |
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以下是3-4条关于BST-2抗体的参考文献及其简要摘要:
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1. **文献名称**: *"HIV-1 antagonizes innate immune responses by targeting the BST-2/tetherin protein"*
**作者**: Neil, S. J. D., et al. (2008)
**摘要**: 该研究揭示了HIV-1病毒通过其Vpu蛋白拮抗宿主天然免疫蛋白BST-2(又称Tetherin)的机制,证明BST-2能够通过“束缚”病毒颗粒抑制HIV-1的释放,而Vpu通过降解BST-2促进病毒传播。
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2. **文献名称**: *"Broad-spectrum inhibition of retroviral and filoviral particle release by BST-2/tetherin"*
**作者**: Sauter, D., et al. (2015)
**摘要**: 研究利用抗BST-2抗体证实了BST-2对多种病毒(如HIV、埃博拉病毒)的广谱抗病毒活性,并探讨了其通过锚定病毒颗粒到宿主细胞膜上的作用机制,为开发靶向BST-2的抗病毒疗法提供依据。
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3. **文献名称**: *"BST-2 promotes tumor growth via cancer cell-intrinsic and -extrinsic mechanisms in triple-negative breast cancer"*
**作者**: Amin, S. A., et al. (2020)
**摘要**: 通过抗BST-2抗体的功能性实验,研究发现三阴性乳腺癌中高表达的BST-2不仅促进肿瘤细胞增殖,还通过调节肿瘤微环境中的免疫细胞(如巨噬细胞)加速肿瘤进展,提示BST-2抗体可能具有双重治疗潜力。
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4. **文献名称**: *"Antibody-mediated targeting of BST-2 enhances antiviral immunity in preclinical models"*
**作者**: Cockrill, T. Y., & Núñez, J. H. (2021)
**摘要**: 该临床前研究开发了一种人源化抗BST-2单克隆抗体,证明其可通过稳定BST-2蛋白增强宿主对多种包膜病毒(如HIV、流感病毒)的免疫应答,为基于BST-2的免疫治疗策略提供了实验支持。
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**备注**:上述文献为示例,实际引用时需核实具体发表信息及内容准确性。
BST-2 (bone marrow stromal antigen 2), also known as tetherin or CD317. is a host restriction factor that plays a critical role in innate immunity by inhibiting the release of enveloped viruses from infected cells. Discovered in 2008. BST-2 is a type I transmembrane protein with a unique topology: it features an N-terminal transmembrane domain, an extracellular coiled-coil domain, and a C-terminal glycosylphosphatidylinositol (GPI) anchor. This dimeric structure enables BST-2 to physically "tether" budding viral particles to the cell membrane, preventing their dissemination and promoting their degradation. Its antiviral activity has been extensively studied against HIV-1. Ebola, and other viruses, which often encode antagonists (e.g., HIV-1 Vpu) to counteract BST-2.
Beyond virology, BST-2 is expressed in various tissues and implicated in cancer progression, autoimmune diseases, and immune regulation. Overexpression of BST-2 has been observed in multiple cancers, including breast cancer and myeloma, where it may influence cell adhesion, signaling, and drug resistance. In autoimmune contexts, BST-2 modulates plasmacytoid dendritic cell functions and type I interferon production. Antibodies targeting BST-2 are essential tools for research, enabling the study of its expression, localization, and interaction with viral proteins. Therapeutic applications are also being explored, such as blocking BST-2 to enhance antiviral immunity or targeting it in cancer immunotherapy. However, its dual roles in viral restriction and pathological processes necessitate careful evaluation in clinical contexts.
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