Genome polyprotein Antibody

Code CSB-PA18549A0Rb
Size US$166
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Product Details

Uniprot No.
Alternative Names
Genome polyprotein [Cleaved into: Capsid protein C antibody; Capsid protein antibody; Core protein); Protein prM antibody; Precursor membrane protein); Peptide pr antibody; Peptide precursor); Small envelope protein M antibody; Matrix protein); Envelope protein E; Non-structural protein 1 antibody; NS1); Non-structural protein 2A antibody; NS2A); Serine protease subunit NS2B antibody; Flavivirin protease NS2B regulatory subunit antibody; Non-structural protein 2B); Serine protease NS3 antibody; EC 3.4.21.91 antibody; EC 3.6.1.15 antibody; EC 3.6.4.13 antibody; Flavivirin protease NS3 catalytic subunit antibody; Non-structural protein 3); Non-structural protein 4A antibody; NS4A); Peptide 2k; Non-structural protein 4B antibody; NS4B); RNA-directed RNA polymerase NS5 antibody; EC 2.1.1.56 antibody; EC 2.1.1.57 antibody; EC 2.7.7.48 antibody; Non-structural protein 5)] antibody
Raised in
Rabbit
Species Reactivity
Dengue virus type 1
Immunogen
Recombinant Dengue virus type 1 Genome polyprotein protein
Immunogen Species
Dengue virus type 1
Conjugate
Non-conjugated

The Genome polyprotein Antibody (Product code: CSB-PA18549A0Rb) is Non-conjugated. For Genome polyprotein Antibody with conjugates, please check the following table.

Available Conjugates
Conjugate Product Code Product Name Application
HRP CSB-PA18549B0Rb Genome polyprotein Antibody, HRP conjugated ELISA
FITC CSB-PA18549C0Rb Genome polyprotein Antibody, FITC conjugated
Biotin CSB-PA18549D0Rb Genome polyprotein Antibody, Biotin conjugated ELISA
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Form
Liquid
Tested Applications
ELISA
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Function
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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