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Acts as a regulator of DDX58/RIG-I and IFIH1/MDA5 mediated antiviral signaling. Additionally we are shipping DHX58 Kits (11) and DHX58 Proteins (4) and many more products for this protein.
Showing 10 out of 96 products:
Human Polyclonal DHX58 Primary Antibody for ELISA, WB - ABIN1002729
Yoneyama, Kikuchi, Natsukawa, Shinobu, Imaizumi, Miyagishi, Taira, Akira, Fujita: The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. in Nature immunology 2004
Show all 4 Pubmed References
Human Polyclonal DHX58 Primary Antibody for ELISA, WB - ABIN1002730
Andrejeva, Childs, Young, Carlos, Stock, Goodbourn, Randall: The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter. in Proceedings of the National Academy of Sciences of the United States of America 2004
Show all 4 Pubmed References
Human Polyclonal DHX58 Primary Antibody for ELISA, WB - ABIN1002731
Akira, Uematsu, Takeuchi: Pathogen recognition and innate immunity. in Cell 2006
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Human Polyclonal DHX58 Primary Antibody for WB - ABIN2475326
Raz, Torres, Acker: Age-related shrinkage of the mamillary bodies: in vivo MRI evidence. in Neuroreport 1992
Show all 3 Pubmed References
Human Polyclonal DHX58 Primary Antibody for ELISA, WB - ABIN449720
Saito, Hirai, Loo, Owen, Johnson, Sinha, Akira, Fujita, Gale: Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2. in Proceedings of the National Academy of Sciences of the United States of America 2007
Human Polyclonal DHX58 Primary Antibody for ICC, IF - ABIN4305195
Sanchez David, Combredet, Sismeiro, Dillies, Jagla, Coppée, Mura, Guerbois Galla, Despres, Tangy, Komarova: Comparative analysis of viral RNA signatures on different RIG-I-like receptors. in eLife 2016
MDA5 (show IFIH1 Antibodies) and LGP2 act as independent positive regulators of the IFN response in fish. the LGP2 variant with a deletion of 54 amino acids at the C terminus acts as a negative regulator for LGP2-elicited antiviral signaling.
study documents that recombinant measles virus produce defective interfering genomes that have high immunostimulatory properties via their binding to RIG-I (show DDX58 Antibodies) and LGP2 proteins, both of which are cytosolic nonself RNA sensors of innate immunity.
Data support a new model where an LGP2-MDA5 oligomer shuttles NS3 to the mitochondria to block antiviral signaling
essential role in activating interferon (show IFNA Antibodies) signaling against hepatitis C virus (HCV) infection by promoting MDA5 (show IFIH1 Antibodies) recognition of HCV pathogen-associated molecular patterns
This review briefly summarizes the RLR system, and focuses on the relationship between LGP2 and MDA5 (show IFIH1 Antibodies), describing in detail how these two proteins work together to detect foreign RNA and generate a fully functional antiviral response.
L region antisense RNA of EMCV is a key determinant of innate immunity to the virus and represents an RNA that activates LGP2 associated MDA5 (show IFIH1 Antibodies) in virally-infected cells.
LGP2 did not reveal significant single-SNP associations with multiple sclerosis risk.
LGP2 increases the initial rate of MDA5 (show IFIH1 Antibodies)-RNA interaction and regulates MDA5 (show IFIH1 Antibodies) filament assembly.
Experiments with paramyxovirus V protein-insensitive proteins revealed that the primary outcome of LGP2 interference is suppression of its ability to synergize with MDA5 (show IFIH1 Antibodies).
Data show that LGP2 is able to synergize with melanoma differentiation associated gene-5 (mda-5 (show IFIH1 Antibodies)) to render cells to induction by poly(I:C), but did not enhance retinoic acid-inducible gene-I (RIG-I (show DDX58 Antibodies)) to induce type I interferon (show IFNA Antibodies) in response to poly(I:C).
results demonstrate previously unrecognized properties of LGP2 ATP hydrolysis and RNA interaction and provide a mechanistic basis for a positive regulatory role for LGP2 in antiviral signaling
This in vivo study reveals that LGP2 is a major downregulator of the influenza A virus-triggered detrimental inflammatory response.
Enhanced expression of LGP2 suppresses the IFN stimulated genes associated with cytotoxic stress by turning off the expression of IFNbeta
LGP2, a host protein induced during influenza A virus infection, downregulates the host antiviral IFN response
LGP2 promotes an essential prosurvival signal in response to antigen stimulation to confer CD8 (show CD8A Antibodies)+ T cell-number expansion and effector functions against divergent RNA viruses, including West Nile virus and lymphocytic choriomeningitis virus.
findings demonstrate a regulatory role for LGP2 in the response to cytosolic DNA, an intracellular bacterial pathogen, and a DNA virus, and provide a plausible mechanistic hypothesis as the basis for this activity
data suggest that LGP2 facilitates viral RNA recognition by RIG-I (show DDX58 Antibodies) and MDA5 (show IFIH1 Antibodies) through its ATPase (show DNAH8 Antibodies) domain.
Lgp2 acts as a negative feedback regulator of antiviral signaling by sequestering double-stranded RNA from retinoic acid-inducible gene-I (RIG-I (show DDX58 Antibodies)).
Functional analysis of the human LGP2 ortholog.
Study indicates that DHX58 is an important gene that is associated with the immune response in swine.
Acts as a regulator of DDX58/RIG-I and IFIH1/MDA5 mediated antiviral signaling. Cannot initiate antiviral signaling as it lacks the CARD domain required for activating MAVS/IPS1- dependent signaling events. Can have both negative and positive regulatory functions related to DDX58/RIG-I and IFIH1/MDA5 signaling and this role in regulating signaling may be complex and could probably depend on characteristics of the infecting virus or target cells, or both. Its inhibitory action on DDX58/RIG-I DDX58/RIG-I for binding to the viral RNA, binding to DDX58/RIG-I and inhibiting its dimerization and interaction with MAVS/IPS1, competing with IKBKE in its binding to MAVS/IPS1 thereby inhibiting activation of interferon regulatory factor 3 (IRF3). Its positive regulatory role may involve unwinding or stripping nucleoproteins of viral RNA thereby facilitating their recognition by DDX58/RIG-I and IFIH1/MDA5. Involved in the innate immune response to various RNA viruses and some DNA viruses such as poxviruses, and also to the bacterial pathogen Listeria monocytogenes. Can bind both ssRNA and dsRNA, with a higher affinity for dsRNA. Shows a preference to 5'-triphosphorylated RNA, although it can recognize RNA lacking a 5'-triphosphate.
DEXH (Asp-Glu-X-His) box polypeptide 58
, probable ATP-dependent RNA helicase DHX58
, probable ATP-dependent RNA helicase DHX58-like
, Probable ATP-dependent RNA helicase DHX58
, RIG-I-like receptor 3
, RIG-I-like receptor LGP2
, RNA helicase LGP2
, ortholog of mouse D11lgp2
, probable ATP-dependent helicase LGP2
, protein D11Lgp2 homolog
, RIG-I-like receptor Lgp2
, protein D11Lgp2
, ATP-dependent RNA helicase DHX58