RIG-I helicase domain (human, recombinant)

Retinoic acid-inducible gene I (RIG-I), also known as DDX58, is a cytosolic DExD/H-box RNA helicase and an immune sensing receptor encoded by DDX58 in humans. It is composed of a C-terminal repressor domain, a central RNA helicase domain, and two N-terminal caspase recruitment domains (CARDs). Following recognition of viral dsRNA by the C-terminal and helicase domains, the helicase domain induces an ATP-dependent conformational change, allowing for interaction of the CARD domains with mitochondrial antiviral-signaling protein (MAVS) and induction of a type I interferon (IFN) response. A single amino acid substitution of phenylalanine for cysteine at position 268 in the RIG-I helicase domain (RIG-IC268F) leads to enhanced NF-kappaB activity and expression of IFN-beta in basal and poly (I:C)-stimulated cells. Overexpression of RIG-IC268F in human trabecular meshwork (HTM) cells induces cell death and is positively correlated with glaucoma, a core symptom in the type I interferonopathy atypical Singleton-Merten syndrome.Synonyms: DEAD Box Protein 58, Probable ATP-dependent RNA Helicase DDX58, Retinoic Acid-inducible Gene 1 Protein. Purity: >80% estimated by SDS-PAGE. Source: Recombinant N-terminal histidine-tagged RIG-I helicase domain purified from E. coli. Amino Acids: 232-794. MW: 66.47 kDa. Formulation: (Request formulation change), 50 mM HEPES, pH 8.0, with 150 mM sodium chloride and 10% glycerol. UniProt Accession #: O95786.