Thermo Fisher Scientific Yellow fever virus envelope glycoprotein E Polyclonal Antibody

Applications

• ELISA (ELISA)
  Tested Dilution: 1:500–1:1,000

Product Specifications

Target Information

Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter, encapsulating the genomic RNA. The prM protein acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating the fusion peptide of envelope protein E.
In the final step of virion assembly, prM is matured to prevent premature activation of the viral fusion peptide in the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released extracellularly, allowing dissociation of small envelope protein M and envelope protein E homodimers.
Envelope protein E mediates host cell receptor binding and subsequent clathrin-mediated endocytosis, followed by membrane fusion with host late endosomes. Synthesized as a homodimer with prM, envelope protein E later dissociates and homodimerizes after prM cleavage.
Non-structural proteins (NS1–NS5) are involved in viral replication, immune regulation, and polyprotein processing. NS3, in complex with NS2B, exhibits serine protease, NTPase, and RNA helicase activities, essential for polyprotein cleavage and RNA unwinding. NS4A induces endoplasmic reticulum membrane rearrangements to form replication complexes.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.