Recombinant Human MAVS protein
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Recombinant Human MAVS protein is a Human Fragment protein, in the 1 to 513 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.
View Alternative Names
IPS1, KIAA1271, VISA, MAVS, Mitochondrial antiviral-signaling protein, CARD adapter inducing interferon beta, Interferon beta promoter stimulator protein 1, Putative NF-kappa-B-activating protein 031N, Virus-induced-signaling adapter, Cardif, IPS-1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human MAVS protein (AB139779)
3ug by SDS-PAGE under reducing conditions and visualized by coomassie blue stain.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The MAVS protein activates important signaling cascades to produce type I interferons and other cytokines which are essential in the antiviral response. MAVS forms a complex with other proteins on the mitochondrial membrane helping to coordinate a rapid immune reaction to viral pathogens. It acts by amplifying the signal from RIG-I and MDA5 facilitating their role in the recognition of viral RNA. By recruiting downstream signaling molecules MAVS enables the activation of transcription factors like IRF3 and NF-kB.
Pathways
MAVS plays a central role in the signaling pathways that regulate innate immunity including the RIG-I-like receptor signaling pathway and the NF-kB pathway. It interacts with various proteins such as TRIF and STING in the pathways to modulate immune responses. These pathways help trigger the production of antiviral substances and maintain homeostasis within the body's defense mechanisms. MAVS provides a platform for the assembly of signaling complexes which are necessary for the propagation and amplification of the immune response signal.
Specifications
Form
Liquid
Additional notes
ab139779 is purified using conventional chromatography techniques.
General info
Function
Adapter required for innate immune defense against viruses (PubMed : 16125763, PubMed : 16127453, PubMed : 16153868, PubMed : 16177806, PubMed : 19631370, PubMed : 20127681, PubMed : 20451243, PubMed : 21170385, PubMed : 23087404, PubMed : 27992402, PubMed : 33139700, PubMed : 37582970). Acts downstream of DHX33, RIGI and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFNB and RANTES (CCL5) (PubMed : 16125763, PubMed : 16127453, PubMed : 16153868, PubMed : 16177806, PubMed : 19631370, PubMed : 20127681, PubMed : 20451243, PubMed : 20628368, PubMed : 21170385, PubMed : 23087404, PubMed : 25636800, PubMed : 27736772, PubMed : 33110251). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state (PubMed : 20451243). Upon viral infection, peroxisomal MAVS induces the rapid interferon-independent expression of defense factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon-dependent signaling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response (PubMed : 20451243). May activate the same pathways following detection of extracellular dsRNA by TLR3 (PubMed : 16153868). May protect cells from apoptosis (PubMed : 16125763). Involved in NLRP3 inflammasome activation by mediating NLRP3 recruitment to mitochondria (PubMed : 23582325).
Post-translational modifications
Following activation, phosphorylated by TBK1 at Ser-442 in the pLxIS motif (PubMed:25636800, PubMed:27302953). The phosphorylated pLxIS motif constitutes an IRF3-binding motif, leading to recruitment of the transcription factor IRF3 to induce type-I interferons and other cytokines (PubMed:25636800).. Ubiquitinated (PubMed:19881509, PubMed:23087404, PubMed:25636800, PubMed:38016475). Undergoes 'Lys-48'-linked polyubiquitination catalyzed by ITCH; ITCH-dependent polyubiquitination is mediated by the interaction with PCBP2 and leads to MAVS/IPS1 proteasomal degradation (PubMed:19881509). Ubiquitinated by RNF125, leading to its degradation by the proteasome (PubMed:17460044). Undergoes 'Lys-48'-linked ubiquitination catalyzed by SMURF1 (PubMed:23087404). Ubiquitinated via 'Lys-63'-linked ubiquitination at Lys-10, Lys-311 and Lys-461 by UBE2N and TRIM31, promoting MAVS polymerization and formation of three-stranded helical filaments on mitochondria (PubMed:27992402, PubMed:37582970). Undergoes 'Lys-63'-linked ubiquitination leading to enhanced interaction between MAVS and TRAF2 (PubMed:34880843). Undergoes 'Lys-27'-linked ubiquitination by TRIM21 leading to enhanced interaction between MAVS and TBK1 (PubMed:29743353, PubMed:36943869). Deubiquitinated by USP10 leading to attenuation of RIGI-mediated MAVS aggregation and production of type I interferon (PubMed:37582970). Undergoes 'Lys-48'-linked polyubiquitination catalyzed by RNF115 leading to its degradation (PubMed:33139700).. Palmitoylated by ZHDDC4. Palmitoylation promotes MAVS stabilization and activation by inhibiting 'Lys-48'- but facilitating 'Lys-63'-linked ubiquitination.. Proteolytically cleaved by apoptotic caspases during apoptosis, leading to its inactivation (PubMed:30878284). Cleavage by CASP3 during virus-induced apoptosis inactivates it, preventing cytokine overproduction (PubMed:30878284).. (Microbial infection) Cleaved and degraded by hepatitis A virus (HAV) protein 3ABC allowing the virus to disrupt the activation of host IRF3 through the MDA5 pathway.. (Microbial infection) Cleaved by the protease 2A of coxsackievirus B3, poliovirus and enterovirus 71 allowing the virus to disrupt the host type I interferon production.. (Microbial infection) Cleaved by Seneca Valley virus protease 3C allowing the virus to suppress interferon type-I production.. (Microbial infection) Cleaved by HCV protease NS3/4A, thereby preventing the establishment of an antiviral state.. (Microbial infection) UFMylated by ULF1 in association with Epstein-Barr virus BILF1; leading to MAVS routing to the lysosome.
Subcellular localisation
Mitochondrion outer membrane
Product protocols
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Target data
Product promise
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