Genome polyprotein Antibody

Code CSB-PA36438ZA01GOZ
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Product Details

Full Product Name Rabbit anti-Zika virus (ZIKV) Genome polyprotein,partial Polyclonal antibody
Uniprot No. Q32ZE1
Target Names Genome polyprotein,partial
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 (EC (EC (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 (EC (EC (NS5)]
Raised in Rabbit
Species Reactivity Zika virus
Immunogen Recombinant Zika virus Genome polyprotein protein
Immunogen Species Zika virus (ZIKV)
Conjugate Non-conjugate
Clonality Polyclonal
Isotype IgG
Purification Method Protein A/G
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, WB (ensure identification of antigen)
Protocols ELISA Protocol
Troubleshooting and FAQs Antibody FAQs
Storage Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Value-added Deliverables ① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);
Quality Guarantee ① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;
Lead Time Made-to-order (12-14 weeks)

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Target Background

(From Uniprot)
Plays a role in virus budding by binding to the host cell membrane and packages the viral RNA into a nucleocapsid that forms the core of the 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.; 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 pH 6.0. After virion release in extracellular space, gets dissociated from E dimers.; Plays a role in host immune defense modulation and protection of envelope protein E during virion synthesis. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion. Contributes to fetal microcephaly in humans. 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.; May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.; Binds to host cell surface receptors and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HAVCR1 in a cell-type specific manner. In addition, host NCAM1 can also be used as entry receptor. Interaction with host HSPA5 plays an important role in the early stages of infection as well. Envelope protein is synthesized in the endoplasmic reticulum and forms a heterodimer with protein prM. The heterodimer plays a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimers between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes the dissociation of PrM-E heterodimers and formation of E homodimers. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion.; Plays a role in the inhibition of host RLR-induced interferon-beta activation by targeting TANK-binding kinase 1/TBK1. In addition, recruits the host deubiquitinase USP8 to cleave 'Lys-11'-linked polyubiquitin chains from caspase-1/CASP1 thus inhibiting its proteasomal degradation. In turn, stabilized CASP1 promotes cleavage of cGAS, which inhibits its ability to recognize mitochondrial DNA release and initiate type I interferon signaling.; Component of the viral RNA replication complex that recruits genomic RNA, the structural protein prM/E complex, and the NS2B/NS3 protease complex to the virion assembly site and orchestrates virus morphogenesis. Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response. May disrupt adherens junction formation and thereby impair proliferation of radial cells in the host cortex.; Required cofactor for the serine protease function of NS3.; 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. Leads to translation arrest when expressed ex vivo.; Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Cooperatively with NS4B suppresses the Akt-mTOR pathway and leads to cellular dysregulation. By inhibiting host ANKLE2 functions, may cause defects in brain development, such as microcephaly. Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response. Leads to translation arrest when expressed ex vivo.; 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. Plays also a role in the inhibition of host RLR-induced interferon-beta production at TANK-binding kinase 1/TBK1 level. Cooperatively with NS4A suppresses the Akt-mTOR pathway and leads to cellular dysregulation.; Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. Methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Once sufficient NS5 is expressed, binds to the cap-proximal structure and inhibits further translation of the viral genome. Besides its role in RNA genome replication, also prevents the establishment of a cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Mechanistically, interferes with host kinases TBK1 and IKKE upstream of interferon regulatory factor 3/IRF3 to inhibit the RIG-I pathway. Antagonizes also type I interferon signaling by targeting STAT2 for degradation by the proteasome thereby preventing activation of JAK-STAT signaling pathway. Within the host nucleus, disrupts host SUMO1 and STAT2 co-localization with PML, resulting in PML degradation. May also reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes.
Gene References into Functions
  1. Here, by mutagenesis, the authors found a major role of the N-glycosylation of flavivirus E protein in its transmission circle, facilitating its survival against the vector immune system during invasion of the mosquito midgut while blood feeding on the host. PMID: 29463651
  2. In complex with an inhibitor, the protease adopts a closed, "active" conformation with the NS2B chain wrapped around the NS3(pro) and contributing to the S2 pocket.[review] PMID: 29845530
  3. crystal structure of the apo ZIKV NS2B-NS3pro complex in a monomeric form; structure reveals a molecular mechanism for ZIKV NS3pro inhibition and identifies a new target for rational drug design against flavivirus PMID: 27752039
  4. Data indicate a crystal structure at 1.84 A resolution of ZIKV non-structural protein NS2B-NS3 protease with the last four amino acids of the NS2B cofactor bound at the NS3 active site. PMID: 27845325
  5. The potential roles of NS2B and NS4A Zika virus proteins in its global pandemic has been reported. PMID: 29428601
  6. The mutation enables NS1 binding to TBK1 and reduces TBK1 phosphorylation and inhibit interferon-beta induction. PMID: 29379028
  7. The Zika virus envelope protein glycan loop modulates antigenicity. PMID: 29304471
  8. Structural docking suggests that temoporfin potentially binds NS3 pockets that hold critical NS2B residues, thus inhibiting flaviviral polyprotein processing in a non-competitive manner. PMID: 28685770
  9. Sustained Specific and Cross-Reactive T Cell Responses to Zika and Dengue Virus NS3 in West Africa PMID: 29321308
  10. Based on the proposition that the Zika virus NS5 protein utilizes SIAH2-mediated proteasomal degradation of STAT2, an in-silico study was carried out to characterize the protein-protein interactions between NS5, SIAH2 and STAT2 proteins. PMID: 28365387
  11. As the NS2B co-factor is involved in substrate binding of flaviviral NS2B-NS3 proteases, the destabilization of the closed conformation in the linked construct makes it an attractive tool to search for inhibitors that interfere with the formation of the enzymatically active, closed conformation. PMID: 28336347
  12. Here, we solved the crystal structure of full-length NS1 protein, and found an extended membrane association interface contributed by the hydrophobic "spike" of a long intertwined loop, providing important information for ZIKV pathogenesis and development of diagnostic tools. PMID: 27578809
  13. When Zika virus NS5 was expressed, the formation of STAT1-STAT1 homodimers and their recruitment to IFN-gamma-stimulated genes, such as the gene encoding the proinflammatory cytokine CXCL10, were augmented. PMID: 28468880
  14. NS4A and NS4B, cooperatively suppress the Akt-mTOR pathway and lead to cellular dysregulation. PMID: 27524440
  15. The immature ZIKV contains a partially ordered capsid protein shell that is less prominent in other immature flaviviruses. PMID: 28067914
  16. The crystal structure of a C-terminal fragment of ZIKV nonstructural protein 1 (NS1), a major host-interaction molecule that functions in flaviviral replication, pathogenesis and immune evasion. PMID: 27088990
  17. the crystal structure of full-length Zika virus NS1 PMID: 27455458
  18. Study present the crystal structures of ZIKV NS5 N-terminal methyltransferase in complex with an RNA cap analogue ((m7)GpppA) and the free NS5 C-terminal RNA-dependent RNA polymerase. PMID: 28254839
  19. A high-resolution (1.62-A) crystal structure of the RNA helicase from the French Polynesia strain of Zika virus. PMID: 27399257
  20. The structure of ZIKV helicase-RNA has revealed that upon RNA binding, rotations of the motor domains can cause significant conformational changes. Strikingly, although ZIKV and dengue virus (DENV) apo-helicases share conserved residues for RNA binding, their different manners of motor domain rotations result in distinct individual modes for RNA recognition. PMID: 27430951

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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 cytoplasm. Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.; [Non-structural protein 4A]: Host endoplasmic reticulum membrane; Multi-pass membrane protein.; [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.
Database Links

KEGG: vg:7751225

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