Anti-Yellow fever virus envelope glycoprotein E Polyclonal Antibody is a Rabbit antibody targeting Yellow fever virus envelope glycoprotein E. Anti-Yellow fever virus envelope glycoprotein E Polyclonal Antibody can be used in WB.

IgG

Yellow fever virus

Sample:
Lane 1: Recombinant YFV Envelope protein E, Trx & His
Primary: Anti-Yellow fever virus envelope glycoprotein E (TMAB-14230) at 1/1000 dilution
Secondary: IRDye800CW Goat Anti-Rabbit IgG at 1/20000 dilution
Predicted band size: 54/375 kDa
Observed band size: 30 kDa

WB: 1:500-2000

Polyclonal

KLH conjugated synthetic peptide: Yellow fever virus envelope glycoprotein E

Genome polyprotein

Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA.
prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated.
Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes.
Non-structural protein 1 is involved in virus replication and regulation of the innate immune response.
Non-structural protein 2A may be involved viral RNA replication and capsid assembly (Potential).
Non-structural protein 2B is a required cofactor for the serine protease function of NS3.
Serine protease 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).
Non-structural protein 4A induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functioning as a replication complex. NS4A might also regulate the ATPase activity of the NS3 helicase (By similarity).
Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.
Non-structural protein 4B 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 (By similarity).
RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) 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 genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway