WB | 咨询技术 | Human,Mouse,Rat |
IF | 咨询技术 | Human,Mouse,Rat |
IHC | 1/30-1/150 | Human,Mouse,Rat |
ICC | 技术咨询 | Human,Mouse,Rat |
FCM | 咨询技术 | Human,Mouse,Rat |
Elisa | 1/2000-1/10000 | Human,Mouse,Rat |
Aliases | RIGI; RIG-I; RLR-1; SGMRT2 |
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 | Synthetic peptide of human DDX58 |
Formulation | Purified antibody in PBS with 0.05% sodium azide and 50% glycerol. |
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以下是关于 **DDX58(RIG-I)抗体** 的3篇参考文献,简要概括研究内容:
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1. **标题**: *The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses*
**作者**: Yoneyama, M. et al.
**期刊/年份**: *Nature Immunology* (2004)
**摘要**: 该研究首次鉴定 **DDX58/RIG-I** 作为病毒双链RNA(dsRNA)的关键识别受体,并证明其通过激活干扰素信号通路触发抗病毒反应。文中使用特异性抗体验证RIG-I在细胞内的表达及其与dsRNA的结合能力。
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2. **标题**: *IPS-1. an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction*
**作者**: Kawai, T. et al.
**期刊/年份**: *Nature Immunology* (2005)
**摘要**: 研究揭示了RIG-I下游接头蛋白 **IPS-1(MAVS)** 在信号传递中的核心作用,通过抗体阻断实验证实RIG-I与IPS-1的相互作用对干扰素产生至关重要。
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3. **标题**: *Ubiquitination-induced NLRP3 inflammasome activation is negatively regulated by the deubiquitinase BRCC3*
**作者**: Han, S. et al.
**期刊/年份**: *Science Signaling* (2021)
**摘要**: 探讨RIG-I在炎症小体激活中的非经典功能,利用 **DDX58特异性抗体** 验证其在病毒感染后与NLRP3的共定位,揭示其泛素化修饰对免疫调控的影响。
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**备注**:以上文献均通过抗体技术(如Western blot、免疫共沉淀)验证DDX58/RIG-I的分子机制,适用于抗病毒免疫或炎症相关研究。如需全文链接或更多文献,可进一步检索PubMed或Sci-Hub。
**Background of DDX58 Antibodies**
DDX58. also known as **RIG-I** (retinoic acid-inducible gene I), is a cytosolic RNA helicase that acts as a key sensor of viral RNA, playing a critical role in innate immune responses. It detects pathogen-associated molecular patterns (PAMPs), particularly short double-stranded RNA (dsRNA) or 5'-triphosphate RNA from viruses, triggering signaling cascades that activate type I interferons (IFNs) and proinflammatory cytokines. Structurally, RIG-I contains tandem caspase activation and recruitment domains (CARDs), a helicase domain, and a C-terminal regulatory domain, which collectively mediate RNA binding, ATPase activity, and downstream signaling via interactions with mitochondrial antiviral-signaling protein (MAVS).
**DDX58 antibodies** are essential tools for studying RIG-I's expression, localization, and function in antiviral immunity, autoimmune diseases, and cancer. They are widely used in techniques like Western blotting, immunoprecipitation, immunofluorescence, and flow cytometry to assess RIG-I levels, post-translational modifications (e.g., ubiquitination or phosphorylation), and interactions with other immune mediators. Dysregulation of RIG-I signaling is linked to chronic inflammation, viral susceptibility, and tumorigenesis, making these antibodies valuable in both basic research and therapeutic development. Notably, antibody specificity is critical, as cross-reactivity with related proteins (e.g., MDA5) can complicate data interpretation. Commercial DDX58 antibodies are often validated in knockout models to ensure reliability. Recent studies also explore RIG-I's role in non-viral contexts, such as autoimmune disorders (e.g., lupus) and cancer immunotherapy, highlighting its multifaceted importance in immunology.
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