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DEAD (Asp-Glu-Ala-Asp) Box Polypeptide 58 (DDX58) (N-Term) antibody

Details for Product No. ABIN965986, Supplier: Log in to see
Antigen
  • RIG-I
  • RIGI
  • RLR-1
  • 6430573D20Rik
  • C330021E21
  • RHIV-1
  • RIG-1
Epitope
N-Term
14
9
8
5
5
5
3
3
3
2
2
2
2
1
1
1
1
Reactivity
Human
132
59
25
1
Host
Rabbit
108
20
8
8
Clonality
Polyclonal
Conjugate
Un-conjugated
11
7
5
3
2
2
2
2
2
2
2
2
Application
Immunohistochemistry (IHC)
98
35
29
28
24
10
10
3
3
3
2
2
Supplier
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Immunogen Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to N-terminal residues of human DDX58(Probable ATP-dependent RNA helicase DDX58)(DEAD-box protein 58)
Alternative Name DDX58 (DDX58 Antibody Abstract)
Background DDX58(Probable ATP-dependent RNA helicase DDX58)(DEAD-box protein 58) is involved in innate immune defense against viruses. Upon interaction with intracellular dsRNA produced during viral replication, 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). DDX58 detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). DDX58 is essential for the production of interferons in response to RNA viruses including paramyxoviruses, influenza viruses, Japanese encephalitis virus and HCV. DDX58 is maintained as a monomer in an autoinhibited state. Upon viral dsRNA binding and conformation shift, homomultimerizes and interacts with MAVS. DDX58 interacts with DHX58/LGP2, IKBKE, TBK1 and TMEM173/STING. DDX58 is present in vascular smooth cells. The repressor domain controls homomultimerization and interaction with MAVS. The helicase domain is responsible for dsRNA recognition. The 2 CARD domains are responsible for interaction with and signaling through MAVS. DDX58 is conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. DDX58 belongs to the helicase family and contains 2 CARD domains, 1 helicase ATP-binding domain and 1 helicase C-terminal domain.
Synonyms: RIG-1 (Retinoic acid-inducible gene 1 protein)
Research Area Immunology, Chromatin Binding Proteins, DNA/RNA, Transcription Factors
Pathways
Restrictions For Research Use only
Product cited in: "Outbreak news. Rift Valley fever, Sudan." in: Relevé épidémiologique hebdomadaire / Section d'hygiène du Secrétariat de la Société des Nations = Weekly epidemiological record / Health Section of the Secretariat of the League of Nations, Vol. 82, Issue 46, pp. 401-2, 2007 (PubMed).

Huang, Liu, Xu et al.: "SIKE is an IKK epsilon/TBK1-associated suppressor of TLR3- and virus-triggered IRF-3 activation pathways." in: The EMBO journal, Vol. 24, Issue 23, pp. 4018-28, 2005 (PubMed).

Seth, Sun, Ea et al.: "Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3." in: Cell, Vol. 122, Issue 5, pp. 669-82, 2005 (PubMed).

Sumpter, Loo, Foy et al.: "Regulating intracellular antiviral defense and permissiveness to hepatitis C virus RNA replication through a cellular RNA helicase, RIG-I." in: Journal of virology, Vol. 79, Issue 5, pp. 2689-99, 2005 (PubMed).

Cui, Imaizumi, Yoshida et al.: "Retinoic acid-inducible gene-I is induced by interferon-gamma and regulates the expression of interferon-gamma stimulated gene 15 in MCF-7 cells." in: Biochemistry and cell biology = Biochimie et biologie cellulaire, Vol. 82, Issue 3, pp. 401-5, 2004 (PubMed).

Imaizumi, Aratani, Nakajima et al.: "Retinoic acid-inducible gene-I is induced in endothelial cells by LPS and regulates expression of COX-2." in: Biochemical and biophysical research communications, Vol. 292, Issue 1, pp. 274-9, 2002 (PubMed).

Background publications Xu, Wang, Han et al.: "VISA is an adapter protein required for virus-triggered IFN-beta signaling." in: Molecular cell, Vol. 19, Issue 6, pp. 727-40, 2005 (PubMed).

Yoneyama, Kikuchi, Natsukawa et al.: "The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses." in: Nature immunology, Vol. 5, Issue 7, pp. 730-7, 2004 (PubMed).