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Mouse Anti-MAVS (AA 93-276 ) Recombinant Antibody (58N3B6) (CBMAB-M0199-FY)

This product is mouse antibody that recognizes MAVS. The antibody 58N3B6 can be used for immunoassay techniques such as: WB, IHC, IHC-P.
See all MAVS antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
58N3B6
Antibody Isotype
IgG2b, k
Application
WB, IHC, IHC-P

Basic Information

Immunogen
Amino acids 93-276 of human MAVS (isoform 1)
Specificity
Human
Antibody Isotype
IgG2b, k
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 93-276

Target

Full Name
Mitochondrial Antiviral Signaling Protein
Introduction
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.
Entrez Gene ID
57506
UniProt ID
Q7Z434
Alternative Names
Mitochondrial Antiviral Signaling Protein; Interferon Beta Promoter Stimulator Protein 1; Putative NF-Kappa-B-Activating Protein 031N; CARD Adapter Inducing Interferon Beta; Virus-Induced Signaling Adaptor; Virus-Induced-Signaling Adapter; CARD Adaptor Inducing IFN-Beta; IFN-B Promoter Stimulator 1
Function
Required for innate immune defense against viruses (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20451243, PubMed:23087404, PubMed:20127681, PubMed:21170385).

Acts downstream of DHX33, DDX58/RIG-I 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:20451243, PubMed:23087404, PubMed:25636800, PubMed:20127681, PubMed:21170385, PubMed:20628368, 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).
Biological Process
Activation of innate immune response Source: UniProtKB
Cellular response to exogenous dsRNA Source: UniProtKB
Defense response to bacterium Source: UniProtKB
Defense response to virus Source: UniProtKB
Innate immune response Source: UniProtKB
Negative regulation of viral genome replication Source: UniProtKB
Positive regulation of chemokine (C-C motif) ligand 5 production Source: BHF-UCL
Positive regulation of defense response to virus by host Source: UniProtKB
Positive regulation of DNA-binding transcription factor activity Source: BHF-UCL
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Positive regulation of interferon-alpha production Source: BHF-UCL
Positive regulation of interferon-beta production Source: UniProtKB
Positive regulation of interleukin-6 production Source: UniProtKB
Positive regulation of interleukin-8 production Source: BHF-UCL
Positive regulation of IP-10 production Source: BHF-UCL
Positive regulation of myeloid dendritic cell cytokine production Source: UniProtKB
Positive regulation of protein import into nucleus Source: BHF-UCL
Positive regulation of protein phosphorylation Source: BHF-UCL
Positive regulation of response to cytokine stimulus Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: BHF-UCL
Positive regulation of tumor necrosis factor production Source: BHF-UCL
Positive regulation of type I interferon-mediated signaling pathway Source: UniProtKB
Regulation of peroxisome organization Source: UniProtKB
Signal transduction Source: UniProtKB
Type I interferon signaling pathway Source: ComplexPortal
Cellular Location
Mitochondrion
Mitochondrion outer membrane
Peroxisome
Topology
Cytoplasmic: 1-513
Helical: 514-534
Mitochondrial intermembrane: 535-540
PTM
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). 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). Undergoes 'Lys-63'-linked ubiquitination leading to enhanced interaction between MAVS and TRAF2 (PubMed:34880843).
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.

Trishna, S., Lavon, A., Shteinfer-Kuzmine, A., Dafa-Berger, A., & Shoshan-Barmatz, V. (2023). Overexpression of the mitochondrial anti-viral signaling protein, MAVS, in cancers is associated with cell survival and inflammation. Molecular Therapy-Nucleic Acids, 33, 713-732.

Wu, M., Pei, Z., Long, G., Chen, H., Jia, Z., & Xia, W. (2023). Mitochondrial antiviral signaling protein: a potential therapeutic target in renal disease. Frontiers in Immunology, 14.

Fu, J., Hu, F., Ma, T., Zhao, W. J., Tian, H., Zhang, Y., ... & Li, H. (2022). A conventional immune regulator mitochondrial antiviral signaling protein blocks hepatic steatosis by maintaining mitochondrial homeostasis. Hepatology, 75(2), 403-418.

Qu, C., Li, Y., Li, Y., & Pan, Y. (2022). Full-length MAVS, a mitochondrial antiviral-signaling protein, inhibits hepatitis E virus replication, requiring JAK-STAT signaling. Archives of Virology, 167(5), 1293-1300.

Kim, S. H., Lee, J. Y., Yoon, C. M., Shin, H. J., Lee, S. W., Rosas, I., ... & Kang, M. J. (2021). Mitochondrial antiviral signaling protein is crucial for the development of pulmonary fibrosis. European Respiratory Journal, 57(4).

Hanada, Y., Ishihara, N., Wang, L., Otera, H., Ishihara, T., Koshiba, T., ... & Nomura, M. (2020). MAVS is energized by Mff which senses mitochondrial metabolism via AMPK for acute antiviral immunity. Nature communications, 11(1), 5711.

Ren, Z., Ding, T., Zuo, Z., Xu, Z., Deng, J., & Wei, Z. (2020). Regulation of MAVS expression and signaling function in the antiviral innate immune response. Frontiers in immunology, 11, 1030.

Refolo, G., Vescovo, T., Piacentini, M., Fimia, G. M., & Ciccosanti, F. (2020). Mitochondrial interactome: a focus on antiviral signaling pathways. Frontiers in cell and developmental biology, 8, 8.

Refolo, G., Ciccosanti, F., Di Rienzo, M., Basulto Perdomo, A., Romani, M., Alonzi, T., ... & Fimia, G. M. (2019). Negative regulation of mitochondrial antiviral signaling protein–mediated antiviral signaling by the mitochondrial protein LRPPRC during Hepatitis C virus infection. Hepatology, 69(1), 34-50.

Feng, H., Sander, A. L., Moreira-Soto, A., Yamane, D., Drexler, J. F., & Lemon, S. M. (2019). Hepatovirus 3ABC proteases and evolution of mitochondrial antiviral signaling protein (MAVS). Journal of hepatology, 71(1), 25-34.

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For research use only. Not intended for any clinical use.

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