Recombinant Human Mitochondrial antiviral-signaling protein(MAVS),partial

Code CSB-YP772018HU
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Source Yeast
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Code CSB-EP772018HU
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Source E.coli
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Code CSB-EP772018HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP772018HU
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Source Baculovirus
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Code CSB-MP772018HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names MAVS
Uniprot No. Q7Z434
Alternative Names CARD adapter inducing interferon beta; CARD adaptor inducing IFN beta; Cardif; DKFZp666M015; FLJ27482; FLJ41962; IFN B promoter stimulator 1; Interferon beta promoter stimulator protein 1; Ips 1; IPS-1; Ips1; KIAA1271; MAVS; MAVS_HUMAN; Mitochondrial anti viral signaling protein; Mitochondrial Antiviral Signaling; Mitochondrial antiviral signaling protein; Mitochondrial antiviral-signaling protein; Putative NF kappa B activating protein 031N; Putative NF-kappa-B-activating protein 031N; Virus induced signaling adapter; virus induced signaling adaptor; Virus-induced-signaling adapter; VISA
Species Homo sapiens (Human)
Protein Length Partial
Tag Info The following tags are available.
N-terminal His-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Background

Required for innate immune defense against viruses. 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). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state. 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. May activate the same pathways following detection of extracellular dsRNA by TLR3. May protect cells from apoptosis.
Gene References into Functions
  1. The mitochondrial antiviral signaling adaptor protein (MAVS) oligomers and high MW aggregates coexist upon constitutively active retinoic acid-inducible gene I (RIG-I) ectopic expression and virus infection. Anchoring of MAVS to intracellular membranes is essential for an appropriate polymerization process allowing functional high MW aggregates to occur. PMID: 29385716
  2. MAVS isoforms are truncated, which prevents its spontaneous aggregation in antiviral innate immune signalling PMID: 28607490
  3. these results demonstrated that HAUS8 may function as a positive regulator of RLRVISA dependent antiviral signaling by targeting the VISA complex, providing a novel regulatory mechanism of antiviral responses PMID: 29916539
  4. results suggest that ASC, as a negative regulator of the MAVS-mediated innate immunity, may play an important role in host protection upon virus infection PMID: 29280086
  5. Using MAVS as a platform, NLRP11 degrades TRAF6 to attenuate the production of type I IFNs as well as virus-induced apoptosis. Our findings reveal the regulatory role of NLRP11 in antiviral immunity by disrupting MAVS signalosome. PMID: 29097393
  6. Low MAVS expression is associated with RNA virus infections. PMID: 29743353
  7. The down regulation of TRIF, TLR3, and mitochondrial antiviral signaling protein (MAVS) expressions in chronic hepatitis C correlates with the disease severity and the outcome of hepatitis C virus infection PMID: 28480979
  8. Taken together, these findings reveal an essential role of CypA in boosting RIG-I-mediated antiviral immune responses by controlling the ubiquitination of RIG-I and MAVS. PMID: 28594325
  9. Data show that human cytomegalovirus (HCMV; human betaherpesvirus 5) glycoprotein US9 inhibits the IFN-beta response by targeting the mitochondrial antiviral-signaling protein (MAVS) and stimulator of interferon genes (STING)-mediated signaling pathways. PMID: 29317664
  10. our results demonstrate that miR-22 negatively regulates poly(I:C)-induced production of type I interferon and inflammatory cytokines via targeting MAVS. PMID: 27705941
  11. this analysis did not indicate the association of the MAVS locus with susceptibility to Addison's disease and type 1 diabetes PMID: 27652379
  12. In the late phase of RNA viral infection, iRhom2 mediates proteasome-dependent degradation of the E3 ubiquitin ligase MARCH5 and impairs mitochondria-associated degradation (MAD) of VISA. PMID: 29155878
  13. findings suggest that oxidative stress-induced MAVS oligomerization in SLE patients may contribute to the type I IFN signature that is characteristic of this syndrome. PMID: 27899525
  14. findings reveal a negative feedback loop of RLR signaling generated by Tetherin-MARCH8-MAVS-NDP52 axis and provide insights into a better understanding of the crosstalk between selective autophagy and optimal deactivation of type I IFN signaling. PMID: 28965816
  15. Studied association of genetic variants of the MAVS, MITA and MFN2 genes with leprosy in Han Chinese from Southwest China; found no association between the variants and susceptibility to leprosy. PMID: 27553710
  16. Mechanistic studies showed that HACE1 exerts its inhibitory role on virus-induced signaling by disrupting the MAVS-TRAF3 complex. PMID: 27213432
  17. this study shows that keratinocytes are an important source of IFN-beta and MAVS is critical to this function, and demonstrates how the epidermis triggers unwanted skin inflammation under disease conditions PMID: 27438769
  18. Herpes simplex virus 1 blocks MAVS-Pex mediated early interferon-stimulated gene activation through VP16 to dampen the immediate early antiviral innate immunity signaling from peroxisomes. PMID: 28222744
  19. This study demonstrates a novel pathway for elevated IFNbeta signaling in SLE that is not dependent on stimulation by immune complexes but rather is cell intrinsic and critically mediated by IFNbeta and MAVS. PMID: 28471483
  20. TTLL12 as a negative regulator of RNA-virus-induced type I IFN expression by inhibiting the interaction of VISA with other proteins. PMID: 28011935
  21. Therefore, Seneca Valley virus suppressed antiviral interferon production to escape host antiviral innate immune responses by cleaving host adaptor molecules MAVS, TRIF, and TANK by its 3C protease. PMID: 28566380
  22. GPATCH3 interacts with VISA and disrupts the assembly of virus-induced VISA signalosome therefore acts as a negative regulator of RLR-mediated innate antiviral immune responses. PMID: 28414768
  23. this study shows that MAVS silencing upregulates IFN-beta production via upregulation of NF-kappaB and IRF3 signaling PMID: 27593154
  24. DDX3 directly regulates TRAF3 ubiquitination and acts as a scaffold to co-ordinate assembly of signaling complexes downstream from MAVS. PMID: 27980081
  25. this study identified three single nucleotide polymorphisms within MAVS that showed significant differences in plasma HIV-1 viral load PMID: 28024153
  26. Results indicate that TAX1BP1 functions as an adaptor molecule for Itch to target MAVS during RNA virus infection and thus restrict virus-induced apoptosis. PMID: 27736772
  27. Deficiency of MAVS in hematopoietic cells resulted in increased mortality and delayed West Nile Virus clearance from the brain. PMID: 27226371
  28. Can activate the RLR/MAVS pathway. PMID: 27605671
  29. deliberately targeting the evolutionarily conserved MDA-5-IPS-1 antiviral pathway in tumors can provoke parallel tumoricidal and immunostimulatory effects that bridge innate and adaptive immune responses for the therapeutic treatment of cancer PMID: 26893477
  30. Pyruvate carboxylase activates the RIG-I-like receptor-mediated antiviral immune response by targeting the MAVS signalosome. PMID: 26906558
  31. This study identified new functional alterations in antiviral signalling based on MAVS polymorphisms PMID: 26954674
  32. 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) to the adaptor MAVS protein and thereby blocked antiviral signaling. PMID: 26998762
  33. These results demonstrate that poliovirus infection actively suppresses the host type I interferon response by blocking activation of IRF-3 and suggests that this is not mediated by cleavage of MDA-5 or IPS-1. PMID: 26437794
  34. 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. PMID: 26317833
  35. These results suggest that vIRF-1 is the first example of a viral protein to inhibit mitochondrial antiviral signaling through lipid raft-like microdomains. PMID: 26512076
  36. 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. PMID: 26183716
  37. indicate comparable activation of the IFN response by pex- and mito-mitochondrial antiviral-signaling protein in hepatocytes and efficient counteraction of both MAVS species by the HCV nonstructural protein 3 protease PMID: 26588843
  38. MAVS50, exposing a degenerate TRAF-binding motif within its N-terminus, effectively competed with full-length MAVS for recruiting TRAF2 and TRAF6 PMID: 26221961
  39. IPS-1 induces anticancer activity through upregulation of pro-apoptotic gene TRAIL and downregulation of the anti-apoptotic genes BCL2, BIRC3 and PRKCE via IRF3 and IRF7 in type I interferon-dependent and -independent manners. PMID: 25950488
  40. Transmembrane motif T6BM2-mediated TRAF6 binding is required for MAVS-related antiviral response. PMID: 26385923
  41. During Crimean-Congo hemorrhagic fever virus infection, RIG-I mediated a type I interferon response via MAVS. PMID: 26223644
  42. Polymorphisms in IPS1 are independently associated with treatment response to PEG-IFN among Chinese HBeAg-positive CHB patients. PMID: 25640825
  43. Elucidate the structural mechanism of MAVS polymerization, and explain how an alpha-helical domain uses distinct chemical interactions to form self-perpetuating filaments. PMID: 24569476
  44. pVHL Negatively Regulates Antiviral Signaling by Targeting MAVS for Proteasomal Degradation PMID: 26179906
  45. Notably, in Lymphocytic Choriomeningitis Virus-infected cells, RIG-I was dispensable for virus-induced apoptosis via MAVS. PMID: 25833049
  46. Hepatitis C virus NS3-4A similarly diminished both human and mouse MAVS-dependent signaling in human and mouse cells and MAVS induces both type I and type III interferons, which together control the hepatitis C virus replication. PMID: 25609814
  47. plays an essential role in stress granule formation PMID: 24659800
  48. findings show MAVS and STING harbor 2 conserved serine and threonine clusters that are phosphorylated by IKK and/or TBK1 in response to stimulation; results reveal phosphorylation of innate adaptor proteins is an essential and conserved mechanism that selectively recruits IRF3 to activate the type I IFN pathway PMID: 25636800
  49. MAVS did not reveal significant single-SNP associations with multiple sclerosis risk. PMID: 25288302
  50. Data indicate that DEAH-box RNA helicase DHX15/PRP43 stimulates the NF-kappaB and MAPK pathways downstream of virus-induced signaling adapter protein MAVS and contributes to MAVS-mediated cytokine production and apoptosis. PMID: 24782566

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Subcellular Location Mitochondrion outer membrane. Mitochondrion. Peroxisome.
Tissue Specificity Present in T-cells, monocytes, epithelial cells and hepatocytes (at protein level). Ubiquitously expressed, with highest levels in heart, skeletal muscle, liver, placenta and peripheral blood leukocytes.
Database Links

HGNC: 29233

OMIM: 609676

KEGG: hsa:57506

STRING: 9606.ENSP00000401980

UniGene: Hs.570362

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