- CITATIONS: 9
|Application ||WB, E|
|Calculated MW||106600 Da|
|Antigen Region||894-925 aa|
|Other Names||Probable ATP-dependent RNA helicase DDX58, DEAD box protein 58, RIG-I-like receptor 1, RLR-1, Retinoic acid-inducible gene 1 protein, RIG-1, Retinoic acid-inducible gene I protein, RIG-I, DDX58|
|Target/Specificity||This RIG-I antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 894-925 amino acids from the C-terminal region of human RIG-I.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||RIG-I Antibody (C-term) 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).|
Provided below are standard protocols that you may find useful for product applications.
DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases which are implicated in a number of cellular processes involving RNA binding and alteration of RNA secondary structure. RIG-I contains RNA helicase-DEAD box protein motifs and a caspase recruitment domain (CARD). It is involved in viral double-stranded (ds) RNA recognition and the innate immune defense against viruses. Upon interaction with intracellular dsRNA produced during viral replication, RIG-I triggers a transduction cascade involving MAVS/IPS1, which results in the activation of NF-kappa-B, IRF3 and IRF7 and the induction of the expression of antiviral cytokines such as IFN-beta and RANTES (CCL5). This protein is essential for the production of interferons in response to RNA viruses including paramyxoviruses, influenza viruses, Japanese encephalitis virus and HCV.
Li, K., et al., J. Biol. Chem. 280(17):16739-16747 (2005). Breiman, A., et al., J. Virol. 79(7):3969-3978 (2005). Cui, X.F., et al., Biochem. Cell Biol. 82(3):401-405 (2004). Imaizumi, T., et al., Life Sci. 75(10):1171-1180 (2004). Imaizumi, T., et al., Endothelium 11 (3-4), 169-173 (2004) (): ().
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