| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 1/50-1/100 | Human,Mouse,Rat |
| ICC | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | CIG5; Radical S-adenosyl methionine domain-containing protein 2; Cytomegalovirus-induced gene 5 protein; Viperin; Virus inhibitory protein endoplasmic reticulum-associated interferon-inducible |
| Entrez GeneID | 91543; |
| WB Predicted band size | 42kDa |
| 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 | KLH-conjugated synthetic peptide encompassing a sequence within the N-term region of human RSAD2. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于RSAD2(viperin)抗体的3篇参考文献及其摘要概括：
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1. **文献名称**: *Viperin (RSAD2) is induced by influenza virus and inhibits viral replication by modulating the cellular lipid metabolism*
**作者**: Chin KC, Cresswell P (2009)
**摘要**: 该研究通过Western blot和免疫荧光技术，利用RSAD2抗体证实流感病毒可诱导宿主细胞中viperin的表达上调，并发现其通过干扰细胞膜脂质代谢抑制病毒出芽，揭示了viperin的广谱抗病毒机制。
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2. **文献名称**: *The antiviral protein viperin interacts with the viral NS5A protein and inhibits hepatitis C virus replication*
**作者**: Seo JY, Yaneva R, Cresswell P (2011)
**摘要**: 研究利用RSAD2特异性抗体进行免疫共沉淀实验，发现viperin直接与丙型肝炎病毒(HCV)的NS5A蛋白结合，阻碍病毒复制复合体的形成，为靶向宿主因子的抗病毒策略提供了依据。
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3. **文献名称**: *Structural basis of the antiviral activity of viperin against flaviviruses*
**作者**: Duschene LJ, et al. (2020)
**摘要**: 通过抗体验证RSAD2在登革热病毒(DENV)感染中的表达定位，结合冷冻电镜技术解析viperin与病毒NS3蛋白互作的结构，阐明其通过抑制病毒RNA解旋酶活性发挥抗黄病毒作用。
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**备注**：上述研究均依赖RSAD2抗体进行蛋白表达检测或功能机制解析，建议通过PubMed或Google Scholar输入标题进一步获取全文及实验细节。
The RSAD2 (Radical S-Adenosyl Methionine Domain-Containing 2) gene encodes viperin (virus inhibitory protein, endoplasmic reticulum-associated), a multifunctional protein central to innate immunity. Initially identified for its antiviral activity, viperin is induced by interferons (IFNs), pathogen-associated molecular patterns (PAMPs), and direct viral infections. It restricts diverse viruses (e.g., influenza, HIV, Zika) by disrupting viral replication through mechanisms like lipid raft perturbation, synthesis of antiviral nucleotides, or interactions with viral/host proteins. Beyond antivirals, viperin regulates immune signaling (e.g., modulating TLR7/9. RIG-I pathways), influences metabolic pathways (e.g., cholesterol synthesis), and exhibits context-dependent roles in cancer, inflammation, and autoimmune diseases.
RSAD2 antibodies are essential tools for studying viperin's expression, localization, and function. They enable detection via Western blot, immunofluorescence, or immunohistochemistry in infected, inflamed, or transformed tissues. Research applications include exploring host-pathogen interactions, metabolic-immune crosstalk, and viperin's dual roles in promoting or suppressing disease. Commercial antibodies vary in specificity (monoclonal/polyoclonal), epitope targets, and host species compatibility. Validation is critical, as viperin’s expression can be low under basal conditions but highly induced during immune activation. Current studies leverage RSAD2 antibodies to dissect its therapeutic potential as a biomarker or target in infectious diseases, cancer immunotherapy, and chronic inflammatory disorders.
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