|Application ||WB, IHC-P, E|
|Other Accession||O95786, 81170421|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||106600 Da|
|Application Notes||RIG-1 antibody can be used for the detection of RIG-1 by Western blot at 0.5 - 2 µg/mL. Antibody can also be used for immunohistochemistry starting at 5 µg/mL.|
|Other Names||RIG-1 Antibody: RIGI, RIG-I, RLR-1, Probable ATP-dependent RNA helicase DDX58, DEAD box protein 58, DEAD (Asp-Glu-Ala-Asp) box polypeptide 58|
|Reconstitution & Storage||RIG-1 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||RIG-1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. Its ligands include: 5'- triphosphorylated ssRNA and dsRNA and short dsRNA (<1 kb in length). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential. Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity. A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity. Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK- related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV). It also detects rotavirus and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration.|
|Cellular Location||Cytoplasm. Cell projection, ruffle membrane. Cytoplasm, cytoskeleton. Cell junction, tight junction Note=Colocalized with TRIM25 at cytoplasmic perinuclear bodies Associated with the actin cytoskeleton at membrane ruffles|
|Tissue Location||Present in vascular smooth cells (at protein level).|
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Provided below are standard protocols that you may find useful for product applications.
RIG-1 Antibody: The innate immune system detects viral infection by recognizing various viral components and triggers antiviral responses. Like the toll-like receptor 3 (TLR3), the cytoplasmic helicase retinoic acid inducible gene protein 1 (RIG-1) recognizes double-stranded (ds) RNA, a molecular pattern associated with viral infection. Unlike TLR3 however, RIG-1 activates the kinases TBK1 and IKKε through the adaptor protein IPS-1. These kinases then phosphorylate the transcription factors IRF-3 and IRF-7 which are essential for the expression of type-I interferons. RIG-1 is required for the production of interferons in response to RNA viruses including paramyxoviruses, influenza virus, and Japanese encephalitis virus.
Akira S, Uematsu S, and Takeuchi O. Pathogen recognition and innate immunity. Cell 2006; 124:783-801.
Yoneyama M, Kikuchi M, Natsukawa T, et al. The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat. Immunol. 2004; 5:730-7.
Alexopoulou L, Holt AC, Medzhitov R, et al. Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3. Nature 2001; 413:732-8.
Sharma S, tenOever BR, Grandvaux N, et al. Triggering the interferon antiviral response through an IKK-related pathway. Science 2003; 300:1148-51.
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