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AB253236

Anti-West Nile Virus NS1 antibody [IC12.E7.G9/01]

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(1 Publication)

Mouse Monoclonal POLG antibody. Suitable for ELISA and reacts with West Nile virus samples. Cited in 1 publication.

View Alternative Names

Genome polyprotein

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ELISA - Anti-West Nile Virus NS1 antibody [IC12.E7.G9/01] (AB253236)
  • ELISA

Supplier Data

ELISA - Anti-West Nile Virus NS1 antibody [IC12.E7.G9/01] (AB253236)

ELISA plates coated on bench overnight in 0.1M carbonate pH 9.6, 100 μl/well, washed once in wash buffer 300 μl/well (TBS + 0.1% tween 20) and blocked 2 hrs in 1% BSA in D-PBS 300 μl/well. Antibodies diluted to working strength in diluent (DPBS + 1% BSA + 0.05% Tween 20 + 0.2% Proclin 950). Added at 100 μl/well and incubated 2 hrs shaken at ambient temperature. Washed 3 x 300 μl/well. Goat anti Mouse IgG-HRP diluted 1/2500 in diluent, added at 100 μl/well and incubated with shaking 1 hr at ambient. Plate washed 6X300 μl/well. TMB added at 100 μl/well. Reaction for screening assay stopped by addition of 1M HCl 100 μl/well.

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

IC12.E7.G9/01

Isotype

IgG1

Carrier free

No

Reacts with

West Nile virus

Applications

ELISA

applications

Specificity

This antibody is specific for the NS1 protein of West Nile virus, and does not cross-react with NS1 from other flaviviruses, including Dengue virus serotypes 1- 4, Zika virus, Yellow Fever virus and Japanese Encephalitis virus. No cross-reactivity is seen with Chikungunya virus E1, E2 or C proteins.

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Purification notes
Purified from tissue culture supernatant.
Storage buffer
pH: 7 - 8 Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The West Nile Virus NS1 protein is a nonstructural protein with a molecular weight of approximately 46 kDa. This protein is often referred to simply as NS1 and it plays an important role in the viral replication process. It is expressed both intracellularly and extracellularly during infection with the West Nile Virus. Intracellularly it functions in the replication complex within the host cell while extracellularly it is secreted as a hexamer.
Biological function summary

The NS1 protein aids in immune evasion by interfering with the host's complement system. This protein forms a homodimer in the endoplasmic reticulum which is part of its functional form in the host cell. It also interacts with other viral proteins to form complexes that facilitate viral replication. NS1 modulates the immune response hampering the host's ability to mount an effective defense against the virus.

Pathways

The NS1 protein is part of the viral replication and assembly pathway in infected cells. It interacts with other nonstructural proteins such as NS4A and NS4B which are part of the replication complex. NS1 assists in creating an environment favorable for the virus by altering host cell processes and pathways ensuring efficient viral genome replication and assembly.

The NS1 protein has a significant association with West Nile Fever and neuroinvasive disease. It contributes to the pathogenesis of these diseases by disrupting the host's immune response which allows the virus to persist and cause more severe symptoms. The NS1 protein has connections with inflammatory proteins and complement components which it binds to in order to avoid immune elimination playing an essential role in the severity of the disease presentations.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Capsid protein C. 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 (By similarity). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins (By similarity). Can migrate to the cell nucleus where it modulates host functions (By similarity). Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway (PubMed : 23522008).. Capsid protein C. Inhibits RNA silencing by interfering with host Dicer.. Peptide pr. 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.. Protein prM. 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.. Small envelope protein M. May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.. Envelope protein E. Binds to host cell surface receptor and mediates fusion between viral and cellular membranes (PubMed : 15367621). Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM (By similarity). 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 (By similarity). The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers (By similarity). prM-E cleavage is inefficient, and many virions are only partially matured (By similarity). These uncleaved prM would play a role in immune evasion (By similarity).. Non-structural protein 1. 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).. Non-structural protein 2A. Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response.. Serine protease subunit NS2B. Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).. Serine protease/Helicase 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 (By similarity). NS3 supports the separation of RNA daughter and template strands during viral replication. The helicase part is involved in the inhibition of phosphorylation of host STAT1, and thereby inhibition of host type-I IFN signaling (By similarity). In addition, NS3 assists the initiation of replication by unwinding the RNA secondary structure in the 3' non-translated region (NTR). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity).. Non-structural protein 4A. Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.. Peptide 2k. Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.. Non-structural protein 4B. 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 cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment.. RNA-directed RNA polymerase NS5. Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (PubMed : 17267492). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (PubMed : 17267492). 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 (By similarity). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity).
See full target information Genome polyprotein

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

PeerJ 13:e19215 PubMed40183048

2025

Temporal and spatial distribution of histone acetylation in mouse molar development.

Applications

Unspecified application

Species

Unspecified reactive species

Wen Du,Wanyi Luo,Liwei Zheng,Xuedong Zhou,Wei Du
View all publications

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