• STJ73481 Immunofluorescence analysis of paraformaldehyde fixed A431 cells, permeabilized with 0. 15% Triton. Primary incubation 1hr (10ug/ml) followed by Alexa Fluor 488 secondary antibody (2ug/ml) , showing cytoplasmic staining. The nuclear stain is DAPI (blue). Negative control: Unimmunized goat IgG (10ug/ml) followed by Alexa Fluor 488 secondary antibody (2ug/ml).
  • STJ73481 Immunofluorescence analysis of paraformaldehyde fixed HeLa cells, permeabilized with 0. 15% Triton. Primary incubation 1hr (10ug/ml) followed by Alexa Fluor 488 secondary antibody (2ug/ml) , showing cytoplasmic staining. The nuclear stain is DAPI (blue). Negative control: Unimmunized goat IgG (10ug/ml) followed by Alexa Fluor 488 secondary antibody (2ug/ml).
  • STJ73481 Flow cytometric analysis of paraformaldehyde fixed U937 cells (blue line) , permeabilized with 0. 5% Triton. Primary incubation 1hr (10ug/ml) followed by Alexa Fluor 488 secondary antibody (2ug/ml). IgG control: Unimmunized goat IgG (black line) followed by Alexa Fluor 488 secondary antibody.

Anti-DDX58 antibody (C-Term) (STJ73481)

SKU:
STJ73481-100

£303.50
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Host: Goat
Applications: Pep-ELISA/FC/IF/IHC
Reactivity: Human/Mouse
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Goat polyclonal antibody anti-DDX58 (C-Term) is suitable for use in ELISA, Flow Cytometry, Immunofluorescence and Immunohistochemistry research applications.
Clonality: Polyclonal
Conjugation: Unconjugated
Isotype: IgG
Formulation: 0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin. NA
Purification: Purified from goat serum by ammonium sulphate precipitation followed by antigen affinity chromatography using the immunizing peptide.
Concentration: 0.5 mg/mL
Dilution Range: IHC-3.75µg/ml
IF-Strong expression of the protein seen in the cytoplasm of A431 and HeLa cells. 10µg/ml
ELISA-antibody detection limit dilution 1:32000.
Storage Instruction: Store at-20°C on receipt and minimise freeze-thaw cycles.
Gene Symbol: RIGI
Gene ID: 23586
Uniprot ID: RIGI_HUMAN
Immunogen Region: C-Term
Accession Number: NP_055129.2
Immunogen Sequence: KDFHFEKIPFDPAE
Post Translational Modifications Phosphorylated in resting cells and dephosphorylated in RNA virus-infected cells. Phosphorylation at Thr-770, Ser-854 and Ser-855 results in inhibition of its activity while dephosphorylation at these sites results in its activation. Ubiquitinated. 'Lys-63' ubiquitination by RNF135, which occurs after RNA-binding and homodimerization, releases the autoinhibition of the CARD domains by the RLR CTR domain, an essential step in the activation of the RIG-I signaling pathway. Lys-172 is the critical site of ubiquitination for MAVS/IPS1 binding and to induce anti-viral signal transduction. Lys-154, Lys-164 and Lys-172 are shared sites for RNF135-mediated and TRIM4-mediated ubiquitination. Also undergoes 'Lys-48' ubiquitination at Lys-181 by RNF125 that leads to proteasomal degradation. 'Lys-48' ubiquitination follows viral infection and is enhanced by 'Lys-63'-linked ubiquitination of the CARD domains that promotes interaction with VCP/p97 and subsequent recruitment of RNF125. Within a negative feedback loop involving SIGLEC10 and PTPN11, 'Lys-48' ubiquitination at Lys-812 by CBL also elicits the proteasomal degradation of RIGI. Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains. Also probably deubiquitinated by USP17L2/USP17 that cleaves 'Lys-48'- and 'Lys-63'-linked ubiquitin chains and positively regulates the receptor. Ubiquitinated by TRIM40 via 'Lys-48'-linked ubiquitination.leading to proteasomal degradation. Deubiquitinated by USP27X that cleaves 'Lys-63'-linked ubiquitin chains and inhibits the innate immune receptor activity. ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation negatively regulates its function in antiviral signaling response. Sumoylated, probably by MUL1.inhibiting its polyubiquitination. (Microbial infection) Deamidated on Asn-495 and Asn-549 by herpes simplex virus 1 protein UL37. These modifications eliminate RIGI detection of viral RNA and restriction of viral replication. Degraded via selective autophagy following interaction with IRGM. IRGM promotes RIGI recruitment to autophagosome membranes, promoting its SQSTM1/p62-dependent autophagic degradation. (Microbial infection) Cleaved by the protease 3C of coxsackievirus B3, poliovirus and enterovirus 71 allowing the virus to disrupt the host type I interferon production. (Microbial infection) Phosphorylated at Ser-8 by herpes simplex virus 1 protein US3 leading to inhbition of critical RIGI activation steps.
Function Innate immune receptor that senses cytoplasmic viral nucleic acids and activates a downstream signaling cascade leading to the production of type I interferons and pro-inflammatory cytokines. Forms a ribonucleoprotein complex with viral RNAs on which it homooligomerizes to form filaments. The homooligomerization allows the recruitment of RNF135 an E3 ubiquitin-protein ligase that activates and amplifies the RIG-I-mediated antiviral signaling in an RNA length-dependent manner through ubiquitination-dependent and -independent mechanisms. Upon activation, associates with mitochondria antiviral signaling protein (MAVS/IPS1) that activates the IKK-related kinases TBK1 and IKBKE which in turn phosphorylate the interferon regulatory factors IRF3 and IRF7, activating transcription of antiviral immunological genes including the IFN-alpha and IFN-beta interferons. Ligands include 5'-triphosphorylated ssRNAs and dsRNAs but also short dsRNAs (<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. 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 rotaviruses and reoviruses. Detects and binds to SARS-CoV-2 RNAs which is inhibited by m6A RNA modifications (Ref.68). 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.
Protein Name Antiviral Innate Immune Response Receptor Rig-I
Atp-Dependent Rna Helicase Ddx58
Dead Box Protein 58
Rig-I-Like Receptor 1
Rlr-1
Rna Sensor Rig-I
Retinoic Acid-Inducible Gene 1 Protein
Rig-1
Retinoic Acid-Inducible Gene I Protein
Rig-I
Database Links Reactome: R-HSA-1169408
Reactome: R-HSA-168928
Reactome: R-HSA-5689880
Reactome: R-HSA-5689896
Reactome: R-HSA-8983711
Reactome: R-HSA-918233
Reactome: R-HSA-933541
Reactome: R-HSA-933542
Reactome: R-HSA-933543
Reactome: R-HSA-936440
Reactome: R-HSA-9692916
Reactome: R-HSA-9705671
Cellular Localisation Cytoplasm
Cell Projection
Ruffle Membrane
Cytoskeleton
Cell Junction
Tight Junction
Colocalized With Trim25 At Cytoplasmic Perinuclear Bodies
Associated With The Actin Cytoskeleton At Membrane Ruffles
Alternative Antibody Names Anti-Antiviral Innate Immune Response Receptor Rig-I antibody
Anti-Atp-Dependent Rna Helicase Ddx58 antibody
Anti-Dead Box Protein 58 antibody
Anti-Rig-I-Like Receptor 1 antibody
Anti-Rlr-1 antibody
Anti-Rna Sensor Rig-I antibody
Anti-Retinoic Acid-Inducible Gene 1 Protein antibody
Anti-Rig-1 antibody
Anti-Retinoic Acid-Inducible Gene I Protein antibody
Anti-Rig-I antibody
Anti-RIGI antibody
Anti-DDX58 antibody

Information sourced from Uniprot.org

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