Recombinant Human Mitochondrial Antiviral-Signaling Protein (MAVS) Protein (His-SUMO)

Name: Recombinant Human Mitochondrial Antiviral-Signaling Protein (MAVS) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-07140P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Mitochondrial Antiviral-Signaling Protein (MAVS) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q7Z434
Target Symbol	MAVS
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MPFAEDKTYKYICRNFSNFCNVDVVEILPYLPCLTARDQDRLRATCTLSGNRDTLWHLFNTLQRRPGWVEYFIAALRGCELVDLADEVASVYQSYQPRTSDRPPDPLEPPSLPAERPGPPTPAAAHSIPYNSCREKEPSYPMPVQETQAPESPGENSEQALQTLSPRAIPRNPDGGPLESSSDLAALSPLTSSGHQEQDTELGSTHTAGATSSLTPSRGPVSPSVSFQPLARSTPRASRLPGPTGSVVSTGTSFSSSSPGLASAGAAEGKQGAESDQAEPIICSSGAEAPANSLPSKVPTTLMPVNTVALKVPANPASVSTVPSKLPTSSKPPGAVPSNALTNPAPSKLPINSTRAGMVPSKVPTSMVLTKVSASTVPTDGSSRNEETPAAPTPAGATGGSSAWLDSSSENRGLGSELSKPGVLASQVDSPFSGCFEDLAISASTSLGMGPCHGPEENEYKSEGTFGIHVAENPSIQLLEGNPGPPADPDGGPRPQADRKFQEREVPCHRPSP
Expression Range	1-513aa
Protein Length	Partial
Mol. Weight	66.4 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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.
Subcellular Location	Mitochondrion outer membrane. Mitochondrion. Peroxisome.
Database References	HGNC: 29233 OMIM: 609676 KEGG: hsa:57506 STRING: 9606.ENSP00000401980 UniGene: PMID: 29385716 MAVS isoforms are truncated, which prevents its spontaneous aggregation in antiviral innate immune signalling PMID: 28607490 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 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 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 Low MAVS expression is associated with RNA virus infections. PMID: 29743353 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 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 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 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 this analysis did not indicate the association of the MAVS locus with susceptibility to Addison's disease and type 1 diabetes PMID: 27652379 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 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 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 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 Mechanistic studies showed that HACE1 exerts its inhibitory role on virus-induced signaling by disrupting the MAVS-TRAF3 complex. PMID: 27213432 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 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 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 TTLL12 as a negative regulator of RNA-virus-induced type I IFN expression by inhibiting the interaction of VISA with other proteins. PMID: 28011935 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 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 this study shows that MAVS silencing upregulates IFN-beta production via upregulation of NF-kappaB and IRF3 signaling PMID: 27593154 DDX3 directly regulates TRAF3 ubiquitination and acts as a scaffold to co-ordinate assembly of signaling complexes downstream from MAVS. PMID: 27980081 this study identified three single nucleotide polymorphisms within MAVS that showed significant differences in plasma HIV-1 viral load PMID: 28024153 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 Deficiency of MAVS in hematopoietic cells resulted in increased mortality and delayed West Nile Virus clearance from the brain. PMID: 27226371 Can activate the RLR/MAVS pathway. PMID: 27605671 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 Pyruvate carboxylase activates the RIG-I-like receptor-mediated antiviral immune response by targeting the MAVS signalosome. PMID: 26906558 This study identified new functional alterations in antiviral signalling based on MAVS polymorphisms PMID: 26954674 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 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 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 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 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 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 MAVS50, exposing a degenerate TRAF-binding motif within its N-terminus, effectively competed with full-length MAVS for recruiting TRAF2 and TRAF6 PMID: 26221961 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 Transmembrane motif T6BM2-mediated TRAF6 binding is required for MAVS-related antiviral response. PMID: 26385923 During Crimean-Congo hemorrhagic fever virus infection, RIG-I mediated a type I interferon response via MAVS. PMID: 26223644 Polymorphisms in IPS1 are independently associated with treatment response to PEG-IFN among Chinese HBeAg-positive CHB patients. PMID: 25640825 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 pVHL Negatively Regulates Antiviral Signaling by Targeting MAVS for Proteasomal Degradation PMID: 26179906 Notably, in Lymphocytic Choriomeningitis Virus-infected cells, RIG-I was dispensable for virus-induced apoptosis via MAVS. PMID: 25833049 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 plays an essential role in stress granule formation PMID: 24659800 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 MAVS did not reveal significant single-SNP associations with multiple sclerosis risk. PMID: 25288302 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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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