Probable ATP-dependent RNA helicase DDX58 (DDX58) Recombinant Protein | DDX58 recombinant protein

Recombinant Pig Probable ATP-dependent RNA helicase DDX58 (DDX58), partial

Cat. Num. AAA1424419

• Gene Names: DDX58; RIG-1; RIG-I; RLR-1; RHIV-1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Probable ATP-dependent RNA helicase DDX58 (DDX58); Recombinant Pig Probable ATP-dependent RNA helicase DDX58 (DDX58); partial; DDX58 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 249-428; Provide the Helicase ATP-binding region
• Sequence: ALPAQNGKNTIICAPTGCGKTFVSLLICEHHLKKFPRGRKGKVVFFAIQLPVYEQQKSVFSKHFERLGYKVAGISGATSDTVCVEQIVENSDIIILTPQILVNCLTNGTIPSLSVFTLMIFDECHNTSKQHPYNVIMFSYLDRKLGGSSDSLPQVIGLTASVGVGDAKNKAEATEYICKL
• Sequence Length: 428

• Species: Sus scrofa (Pig)
• Preparation and Storage: Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

Related Product Information for DDX58 recombinant protein

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. This gene encodes a protein containing RNA helicase-DEAD box protein motifs and a caspase recruitment domain (CARD). It is involved in viral double-stranded (ds) RNA recognition and the regulation of immune response.

NCBI and Uniprot Product Information

• NCBI GI #: 75050051
• NCBI GeneID: 396723
• UniProt Accession #: Q9GLV6
• Molecular Weight: 107,584 Da
• NCBI Official Full Name: Probable ATP-dependent RNA helicase DDX58
• NCBI Official Symbol: DDX58
• NCBI Official Synonym Symbols: RIG-1; RIG-I; RLR-1; RHIV-1
• NCBI Protein Information: probable ATP-dependent RNA helicase DDX58
• UniProt Protein Name: Probable ATP-dependent RNA helicase DDX58
• Protein Family: Probable ATP-dependent RNA helicase
• UniProt Gene Name: DDX58
• UniProt Synonym Gene Names: RLR-1; RIG-1; RIG-I

Uniprot Description

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.