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.
其他:
在線留言
中文名稱:
Recombinant West Nile virus Genome polyprotein ,partial
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.
產品提供形式:
Lyophilized
powder
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Note: We will
preferentially ship the format that we have in stock, however,
if you have any special requirement for the format, please
remark your requirement when placing the order, we will prepare
according to your demand.
復溶:
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.
儲存條件:
Store at -20°C/-80°C upon receipt, aliquoting is
necessary for
mutiple use. Avoid repeated freeze-thaw cycles.
保質期:
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.
貨期:
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.
注意事項:
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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 ectodomain. 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 inefficient, 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).; Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral 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. 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. 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.; Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.; 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 cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment.; 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.
基因功能參考文獻:
evidence of the intrinsic flexibility and conformational heterogeneity of the NS2B chain of the WNV protease in the absence of substratelike ligands, which should be considered during antiviral drug discovery and development efforts PMID: 24015950
Mass spectrometry and coimmunoprecipitation studies established a novel physical interaction between NS1 and NS4B, suggesting a mechanism for how luminal NS1 conveys signals to the cytoplasm to regulate RNA replication. PMID: 22553322
NS4B P38G substitution was associated with both temperature-sensitive and small-plaque phenotypes. PMID: 22314017
KAWGKSILFA is a novel epitope of NS1 protein recognized by the NS1 mAb. PMID: 21918007
West Nile virus specific B-cell epitopes located at aa 21-36, 101-116, 191-206 and 261-276 of NS1. PMID: 21940411
The combined effects of proline and negatively charged residues within the PEPE peptide are essential to promote the cleavage of 2K from NS4A, which is a prerequisite for efficient West Nile virus replication. PMID: 21880777
Results highlights the importance of specific functional groups for the binding of the purine substrate, and reveals the complexity of the active site of the NS3 protein. PMID: 20421212
The authors showed that the combination of the residues 156 and 159 of the E protein plays an important role in the transport of West Nile virus virus-like particles across endothelial cells. PMID: 20529314
Dissociation of the C-terminal of the NS2B cofactor from the NS3 protease occurs in the presence and the absence of inhibitors. PMID: 19997625
MKRN1 could induce WNV capsid protein ubiquitination and degradation in a proteasome-dependent manner. PMID: 19846531
characterization and homology model of West Nile virus NS3 protease PMID: 15322074
mutagenesis and kinetic studies of the West Nile Virus NS3 protease PMID: 15494419
comparative studies revealed differential expression of epitopes within the E protein domain III of ten naturally occurring strains representing major subtypes of genetic lineages 1 and 2 PMID: 15823609
NS3 alone triggers the apoptotic pathways involving caspases-8 and -3 PMID: 16243374
A30P mutation results in virus which elicits more rapid induction & higher levels of synthesis of IFN-alpha/beta in infected cells than wild-type; results confirm & extend previous findings on role of NS2A in inhibition of host antiviral response PMID: 16474146
cleavage of the Australian strain of West Nile virus, Kunjin virus (KUNV), polyprotein NS4A-4B by the viral protease is the key initiation event in the induction of membrane rearrangement PMID: 16611922
the C102S mutation of NS4B was associated with a temperature-sensitive phenotype at 41 degrees C as well as attenuation of the neuroinvasive and neurovirulence phenotypes in mice. PMID: 16624366
NS5 sequentially catalyzes guanine-N-7 and ribose 2'-O methylations invovled in RNA cap formation [NS5] PMID: 16912287
crystal structure of a soluble fragment of West Nile virus E; structure adopts the same overall fold as that of E proteins from dengue and tick-borne encephalitis viruses; conformation of domain II is different from that in other prefusion E structures PMID: 16943291
results disclosed the strict substrate specificity of the WNV NS2B-NS3 proteases for which the (K/R)(K/R)R/GG amino acid motifs was optimal PMID: 17067286
established for the first time that the RNA-dependent RNA polymerase NS5 is located in flavivirus-induced membranes, including the site of viral RNA replication PMID: 17374759
WNV-mediated neuroinflammation and cell death occurred through WNV infection of both glia and neurons, which was driven in part by WNV capsid protein expression PMID: 17670819
WNV envelope protein (WNV-E) specifically blocks the production of antiviral and proinflammatory cytokines induced by dsRNA in murine macrophages. PMID: 18056386
Molecular modelling studies suggest a difference in local structure of the E protein associated with either an asparagine or serine residue at position 155 compared with the tyrosine found in the virulent parental WN-Israel virus. [E protein] PMID: 18272752
Two novel NS2B functional determinants critical for NS3pro activation were identified. [NS2B] PMID: 18272753
The results further confirm the role of NS2A in virus assembly, demonstrate the importance of hydrophobic residues at codon 59 in this process, implicate the involvement of NS2A in the biogenesis of virus-induced membranes PMID: 18337583
analysis of the two-component NS2B-NS3 proteinase represses DNA unwinding activity of the West Nile virus NS3 helicase PMID: 18442976
The linker region plays a critical role in determining the NS3 oligomerization that leads to the formation of the active ATPase/helicase oligomer. PMID: 18448185
West Nile virus NS5 binds specifically to the 5'-terminal stem-loop (SL1) of the genomic RNA and this structure is essential for WNV replication. PMID: 18799181
data demonstrate that an intact West Nile virus fusion loop peptide of the envelope protein is critical for virulence, and that human mAb11 targeting this region is efficacious against West Nile virus infection PMID: 19535627
These data support a structural model of the full-length NS5 molecule that predicts a physical interaction between the MTase and the RdRp domains. [[NS5] PMID: 19710254
These results do not support a requirement for any single histidine as a pH-sensing "switch," and they suggest that additional features of the E protein are involved in triggering pH-dependent steps in the flavivirus life cycle. PMID: 19776132