Recombinant Dengue virus type 1 Genome polyprotein ,partial

Code CSB-YP323802DBV
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Source Yeast
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Code CSB-EP323802DBV
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Source E.coli
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Code CSB-EP323802DBV-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-BP323802DBV
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Source Baculovirus
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Code CSB-MP323802DBV
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Uniprot No. P17763
Alternative Names Genome polyprotein [Cleaved into: Capsid protein C; Capsid protein; Core protein); Protein prM; Precursor membrane protein); Peptide pr; Peptide precursor); Small envelope protein M; Matrix protein); Envelope protein E; Non-structural protein 1; NS1); Non-structural protein 2A; NS2A); Serine protease subunit NS2B; Flavivirin protease NS2B regulatory subunit; Non-structural protein 2B); Serine protease NS3; EC 3.4.21.91; EC 3.6.1.15; EC 3.6.4.13; Flavivirin protease NS3 catalytic subunit; Non-structural protein 3); Non-structural protein 4A; NS4A); Peptide 2k; Non-structural protein 4B; NS4B); RNA-directed RNA polymerase NS5; EC 2.1.1.56; EC 2.1.1.57; EC 2.7.7.48; Non-structural protein 5)]
Species Dengue virus type 1 (strain Nauru/West Pac/1974) (DENV-1)
Protein Length Partial
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
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
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.
Troubleshooting
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

Function
(From Uniprot)
Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway.; Inhibits RNA silencing by interfering with host Dicer.; Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.; Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.; May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M extodomain. May display a viroporin activity.; Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is ineficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.; Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).; Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease.; Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.; Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins.; Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.; Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles.; Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.; Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of a cellular antiviral state by blocking the IFN-alpha/beta pathway.; Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.
Gene References into Functions
  1. The secreted, hexameric form of NS1 has a systemic toxic effect, inducing inflammatory cytokines and acting directly on endothelial cells to produce the hallmark of dengue disease, vascular leak.[review] PMID: 29845527
  2. The multifunctional NS3 and NS5 contain all the enzymatic activities required to synthesize the viral RNA genome.[review] PMID: 29845531
  3. Product release is rate-limiting for catalytic processing by the Dengue virus two-component protease NS2b-NS3. PMID: 27897196
  4. This study reports a novel set of Dengue virus (DENV) NS1-interacting host cell proteins in the HepG2 cell line and proposes possible roles for human NEK2, TAO1, and COG1 in DENV infection. PMID: 27108190
  5. Data indicate that envelope (E) protein-specific IgM and IgG produced by antibody-secreting cells (ASC) were highly cross-reactive among the four virus serotypes. PMID: 27560782
  6. data suggests an evolutionarily conserved function for NS5 Cter18, possibly in RNA interactions that are critical for replication, that is independent of its role in subcellular localization. PMID: 27622521
  7. study describes time dynamic trafficking of NS5 to the subnuclear compartment, the nucleolus; demonstrate that NS5's targeting to the nucleolus occurs in response to acidic pH, identify the key amino acid residues within NS5 that are responsible, and demonstrate that their mutation severely impairs production of infectious DENV PMID: 27076639
  8. identified a novel N-terminal unstructured region of the nonstructural protein 3 (NS3) as crucial for production of viral particles; propose new ideas that include NS3 as a possible scaffold for the viral assembly process PMID: 27009958
  9. anti-DENV NS1 Abs has a role in the pathogenesis of thrombocytopenia in dengue disease by enhancing platelet phagocytosis by macrophages PMID: 26632672
  10. data presented suggest that the NS3 helicase domain is an important virulence factor PMID: 26340409
  11. Dengue NS1 antigen contributes to disease severity by inducing IL-10 by monocytes. PMID: 26621477
  12. Drosophila transgenic flies expressing NS3 were more susceptible to bacterial infections than control flies. PMID: 26267447
  13. The B Cell Neutralizing Epitopes was located at amino acid residues 329-348 of E proteins. PMID: 26951013
  14. The present study deals with the molecular modeling of the viral protein (NS3 of DENV1-4), the host protein (NRBP) and their interactions through protein-protein docking study. PMID: 24910013
  15. these results are the first report showing that highly conserved MH domain residues, located at 20-38 amino acids downstream from the prM cleavage site, can modulate the prM cleavage, maturation of particles, and virus entry. PMID: 25326389
  16. Dengue virus protease interacts with both NF-kappaB inhibitor alpha (IkappaBalpha) and NF-kappaB inhibitor beta (IkappaBbeta) cleaving them in a mouse hemorrhage model. PMID: 24973451
  17. A highly conserved region between amino acids 221 and 266 of dengue virus non-structural protein 1 is a major epitope region in infected patients. PMID: 24778195
  18. DENV1 NS5 protein expression suppressed HIV replication in a CD4+ T-cell line. PMID: 24470566
  19. Antibody successfully blocks the glycosylation site ASN 67 and other conserved residues present at DC-SIGN-Dengue-E complex interface. PMID: 23527139
  20. The multiple conformations of NS5 observed in solution result from weak interactions between the protein's two NS5 globular domains and flexibility of the linker in the absence of other components of the replication complex. PMID: 22757685
  21. This work demonstrates the interaction between DENV NS5 and Daxx and the role of the interaction on the modulation of RANTES production. PMID: 22664104
  22. The results demonstrated that paired mutations in the envelope protein (E) and in the helicase domain of the NS3 (NS3(hel)) protein had a synergistic effect enhancing viral fitness in human and mosquito derived cell lines. PMID: 22530074
  23. The positively charged N-terminal region of C protein prompts the interaction with negatively charged lipid droplets (LD), after which a conformational rearrangement enables the access of the central hydrophobic patch to the LD surface. PMID: 22428600
  24. The NS1 of dengue virus 1 increases NF-kappaB transcriptional activity. PMID: 21424730
  25. This study identified human Sec3 exocyst protein (hSec3p) as a novel interacting partner of West Nile virus and Dengue virus C protein. PMID: 19889084
  26. study reports the 2.1-A crystal structure of the DEN1 NS2B hydrophilic core (residues 49 to 95) in complex with the NS3 protease domain (residues 1 to 186) carrying an internal deletion in the N terminus (residues 11 to 20) PMID: 20042502
  27. mapping of immunodominant and conserved serotype- and group-specific B-cell epitopes PMID: 20079511
  28. The results demonstrate that (73)KK and (85)RK of dengue virus capsid protein are important for its nuclear localization, interaction with DAXX and induction of apoptosis. PMID: 19944121
  29. dengue virus nonstructural protein 5 nuclear localization through its importin alpha/beta-recognized nuclear localization sequences is integral to viral infection PMID: 17537211
  30. results suggest that Asn130 of the DENV-1 NS1 is important for dengue virus replication in both mammalian and mosquito cells PMID: 18288598
  31. These results indicate an association of a minor subpopulation of NS1 with lipid rafts during dengue virus infection. [NS1] PMID: 18796718
  32. study reports the crystal structure of a soluble fragment of the envelope protein ein PMID: 19244332
  33. This is the first study that enlightens the interaction of DENV NS4A protein with PTB, in addition to demonstrating the novel role of PTB in relation to mosquito-borne flavivirus life-cycle. PMID: 19450550

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Subcellular Location [Capsid protein C]: Virion. Host nucleus. Host cytoplasm. Host cytoplasm, host perinuclear region.; [Peptide pr]: Secreted.; [Small envelope protein M]: Virion membrane; Multi-pass membrane protein. Host endoplasmic reticulum membrane; Multi-pass membrane protein.; [Envelope protein E]: Virion membrane; Multi-pass membrane protein. Host endoplasmic reticulum membrane; Multi-pass membrane protein.; [Non-structural protein 1]: Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side.; [Non-structural protein 2A]: Host endoplasmic reticulum membrane; Multi-pass membrane protein.; [Serine protease subunit NS2B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein.; [Serine protease NS3]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.; [Non-structural protein 4A]: Host endoplasmic reticulum membrane; Multi-pass membrane protein. Host mitochondrion.; [Non-structural protein 4B]: Host endoplasmic reticulum membrane; Multi-pass membrane protein.; [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus.
Protein Families Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family
Database Links

KEGG: vg:5075725

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