anti-Genome Polyprotein (LOC100493440) Antibodies

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. Additionally we are shipping Genome Polyprotein Proteins (3) and many more products for this protein.

list all antibodies Gene Name GeneID
LOC100493440  
LOC100493440  
LOC100493440  
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Top anti-Genome Polyprotein Antibodies at antibodies-online.com

Showing 10 out of 17 products:

Catalog No. Reactivity Host Conjugate Application Images Quantity Supplier Delivery Price Details
Virus Rabbit HRP ELISA   100 μg Log in to see 11 to 18 Days
$412.19
Details
Virus Rabbit FITC ELISA   100 μg Log in to see 11 to 18 Days
$412.19
Details
Virus Rabbit Biotin ELISA   100 μg Log in to see 11 to 18 Days
$412.19
Details
Virus Rabbit Biotin ELISA   100 μg Log in to see 11 to 16 Days
$426.40
Details
Virus Rabbit FITC ELISA   100 μg Log in to see 11 to 16 Days
$426.40
Details
Virus Rabbit HRP ELISA   100 μg Log in to see 11 to 16 Days
$426.40
Details
Virus Rabbit Un-conjugated ELISA   100 μg Log in to see 11 to 18 Days
$412.19
Details
Virus Rabbit Un-conjugated ELISA   100 μg Log in to see 11 to 16 Days
$426.40
Details
Virus Rabbit Biotin ELISA   100 μg Log in to see 11 to 16 Days
$426.40
Details
REACT_Human rhinovirus A Rabbit HRP ELISA, WB   100 μg Log in to see 13 to 16 Days
$328.90
Details

More Antibodies against Genome Polyprotein Interaction Partners

Yellow Fever Virus Genome Polyprotein (LOC100493440) interaction partners

  1. adaptive genetic diversification has occurred on viral nonstructural protein 5 (show CAPS Antibodies) in African and South American yellow fever virus populations

  2. This suggests that DNAJC14's folding activity normally modulates yellow fever virus NS3/4A/2K cleavage events to liberate appropriate levels of NS3 and NS4A and promote replication complex formation.

  3. These data support a complex interplay between yellow fever virus NS2A and NS3 in virion assembly and identify a basic cluster in the NS2A N terminus to be critical in this process.[NS2A, NS3]

  4. Binding of Yellow fever virus NS5 (show RAF1 Antibodies) to the IFN-activated transcription factor STAT2 (show STAT2 Antibodies) only in cells that have been stimulated with IFN-beta (show IFNB1 Antibodies).

  5. While the increase of the positive charge in the envelope protein domain III may reduce the virulence of YFV in mice, this mutation favored the establishment of the viral infection in Aedes aegypti.

  6. These results indicate an interaction of human eIF3L (show EIF3L Antibodies) with yellow fever virus NS5 (show RAF1 Antibodies) and that eIF3L (show EIF3L Antibodies) overexpression facilitates translation, which has potential implications for virus replication.

  7. study shows that the yellow fever virus (YFV) NS5 (show RAF1 Antibodies) protein is able to interact with U1A (show SNRPA Antibodies), a protein involved in splicing and polyadenylation; a region between amino acids 368 and 448 was identified as the site of interaction of the NS5 (show RAF1 Antibodies) protein with U1A (show SNRPA Antibodies)

  8. By binding C1s and C4 in a complex, NS1 promotes efficient degradation of C4 to C4b. Through this mechanism, NS1 protects flavivirus from complement-dependent neutralization. (NS1)

  9. These data indicate that certain mutations that reduce NS2B-NS3 protease cleavage activity cause growth restriction of yellow fever virus in cell culture.

  10. analysis of the yellow fever virus capsid protein

Genome Polyprotein (LOC100493440) Antigen Profile

Protein Summary

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. 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. {ECO:0000250|UniProtKB:P17763}. Capsid protein C: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000269|PubMed:27849599}. 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. {ECO:0000250|UniProtKB:P17763}. 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. {ECO:0000250|UniProtKB:P17763}. 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. {ECO:0000250|UniProtKB:P17763}. Envelope protein E: 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 particule 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. {ECO:0000250|UniProtKB:P17763}. Non-structural protein 1: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the 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). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:9371625}. Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}. Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE- ProRule:PRU00859}. Serine protease NS3: Displays three enzymatic protease, in association with NS2B, performs its autocleavage and 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. Also plays a role in virus assembly (PubMed:18199634). {ECO:0000255|PROSITE-ProRule:PRU00860, ECO:0000269|PubMed:18199634}. Non-structural protein 4A: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. Peptide 2k: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}. 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 (PubMed:15956546). {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:15956546}. RNA-directed RNA polymerase NS5: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (PubMed:19850911). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (PubMed:19850911). 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 (PubMed:25211074). IFN-I induces binding of NS5 to host IFN- activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition (PubMed:25211074). {ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:25211074}.

Gene names and symbols associated with LOC100493440

  • polyprotein precursor (YFVgp1) antibody
GENE ID SPECIES
1502173 Yellow fever virus
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