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MAVS encodes an intermediary protein necessary in the virus-triggered beta interferon signaling pathways. Additionally we are shipping MAVS Proteins (8) and MAVS Kits (7) and many more products for this protein.
Showing 10 out of 185 products:
Human Polyclonal MAVS Primary Antibody for WB - ABIN657705
Graef, Vreede, Lau, McCall, Carr, Subbarao, Fodor: The PB2 subunit of the influenza virus RNA polymerase affects virulence by interacting with the mitochondrial antiviral signaling protein and inhibiting expression of beta interferon. in Journal of virology 2010
Show all 4 references for ABIN657705
Human Monoclonal MAVS Primary Antibody for ICC, IP - ABIN1169132
Michallet, Meylan, Ermolaeva, Vazquez, Rebsamen, Curran, Poeck, Bscheider, Hartmann, König, Kalinke, Pasparakis, Tschopp: TRADD protein is an essential component of the RIG-like helicase antiviral pathway. in Immunity 2008
Show all 3 references for ABIN1169132
Human Polyclonal MAVS Primary Antibody for EIA, IF - ABIN501118
Seth, Sun, Chen: Antiviral innate immunity pathways. in Cell research 2006
Show all 3 references for ABIN501118
Human Polyclonal MAVS Primary Antibody for EIA, IHC (p) - ABIN501120
Xu, Wang, Han, Li, Zhai, Shu: VISA is an adapter protein required for virus-triggered IFN-beta signaling. in Molecular cell 2005
Show all 3 references for ABIN501120
Human Polyclonal MAVS Primary Antibody for ELISA, IF - ABIN4332859
Klarquist, Hennies, Lehn, Reboulet, Feau, Janssen: STING-mediated DNA sensing promotes antitumor and autoimmune responses to dying cells. in Journal of immunology (Baltimore, Md. : 1950) 2014
Human Polyclonal MAVS Primary Antibody for WB - ABIN2783803
Lad, Yang, Scott, Chao, Correia, de la Torre, Li: Identification of MAVS splicing variants that interfere with RIGI/MAVS pathway signaling. in Molecular immunology 2008
Mouse (Murine) Polyclonal MAVS Primary Antibody for WB - ABIN1881530
Ichinohe, Pang, Iwasaki: Influenza virus activates inflammasomes via its intracellular M2 ion channel. in Nature immunology 2010
The authors determined that porcine reproductive and respiratory syndrome virus 3C protease cleaved MAVS at Glu268.
Real-time quantitative PCR analysis indicated that Tibetan porcine IPS-1 (show ISYNA1 Antibodies) mRNA was most abundant in the liver and kidney.
Pyruvate carboxylase (show PC Antibodies) activates the RIG-I (show DDX58 Antibodies)-like receptor-mediated antiviral immune response by targeting the MAVS signalosome.
results suggest that PPIP5K1 (show PPIP5K1 Antibodies) might play an important role in regulating function of exocyst complex in establishing cellular polarity and directional migration of cells
This study identified new functional alterations in antiviral signalling based on MAVS polymorphisms
Data show that the NS3 protein of dengue virus bound to 14-3-3 epsilon protein (14-3-3varepsilon) and prevented translocation of retinoic acid-inducible gene-I protein (RIG-I (show DDX58 Antibodies)) to the adaptor MAVS protein and thereby blocked antiviral signaling.
These results demonstrate that poliovirus infection actively suppresses the host type I interferon (show IFNA Antibodies) response by blocking activation of IRF-3 (show IRF3 Antibodies) and suggests that this is not mediated by cleavage of MDA-5 (show IFIH1 Antibodies) or IPS-1.
Using bone marrow derived macrophages from knockout mice we demonstrate that hBD3 (show DEFB103A Antibodies) suppresses the polyI:C-induced TLR3 (show TLR3 Antibodies) response mediated by TICAM1 (TRIF (show TICAM1 Antibodies)), while exacerbating the cytoplasmic response through MDA5 (IFIH1 (show IFIH1 Antibodies)) and MAVS (IPS1/CARDIF).
Results show MAVS-transmembrane domain is shown to oligomerize in response to changes in the outer mitochondrial lipid membrane properties caused by treatment with mitochondrial reactive oxygen species inducers or by Sendai virus infection.
MARCH5 (show MARCH5 Antibodies) binds MAVS only during viral stimulation when MAVS forms aggregates, and these interactions require the RING domain of MARCH5 (show MARCH5 Antibodies) and the CARD domain of MAVS.
An autoinhibitory mechanism modulates MAVS activity in unstimulated cells and, on viral infection, individual regions of MAVS are released following MAVS filament formation to activate antiviral signalling cascades.
indicate comparable activation of the IFN response by pex (show PHEX Antibodies)- and mito-mitochondrial antiviral-signaling protein in hepatocytes and efficient counteraction of both MAVS species by the HCV nonstructural protein 3 (show HSPB3 Antibodies) protease
Hepatitis C virus NS3 (show MAL Antibodies)-4A inhibits the peroxisomal MAVS-dependent antiviral signaling response.
Rotavirus infection in macrophages depend on MAVS but not involve the NLRP3 (show NLRP3 Antibodies) inflammasome nor JNK (show MAPK8 Antibodies) and p38 (show CRK Antibodies) signal pathway.
Transmembrane motif T6BM2-mediated TRAF6 (show TRAF6 Antibodies) binding is required for MAVS-related antiviral response.
Data show that intracellular adaptor protein Cardif-/- natural killer cells (NK cells) are more apoptotic and less proliferative.
Elucidate the structural mechanism of MAVS polymerization, and explain how an alpha-helical domain uses distinct chemical interactions to form self-perpetuating filaments.
MAVS plays an essential role in host immunity against metapneumovirus infection.
results indicate that Lyn (show LYN Antibodies) plays a positive regulatory role in RIG-I (show DDX58 Antibodies)-mediated interferon (show IFNA Antibodies) expression as a downstream component of IPS-1 (show ISYNA1 Antibodies)
This gene encodes an intermediary protein necessary in the virus-triggered beta interferon signaling pathways. It is required for activation of transcription factors which regulate expression of beta interferon and contributes to antiviral immunity. Multiple transcript variants encoding different isoforms have been found for this gene.
virus-induced signaling adapter
, mitochondrial antiviral-signaling protein
, mitochondrial IFN-beta promoter stimulator 1
, IP6 kinase
, VIP1 homolog
, histidine acid phosphatase domain containing 2A
, histidine acid phosphatase domain-containing protein 2A
, inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1
, inositol pyrophosphate synthase 1
, insP6 and PP-IP5 kinase 1
, CARD adapter inducing interferon beta
, CARD adaptor inducing IFN-beta
, IFN-B promoter stimulator 1
, interferon beta promoter stimulator protein 1
, putative NF-kappa-B-activating protein 031N
, virus-induced signaling adaptor
, virus-induced-signaling adapter
, IFN-beta promoter stimulator-1
, mitochondrial anti-viral signaling protein
, interferon-beta promoter stimulator protein 1