[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. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway (By similarity). Inhibits the integrated stress response (ISR) in the infected cell by binding to host CAPRIN1 (By similarity). .; [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. 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. .

p0dok8

Structural polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1'' (NS1'')],Structural polyprotein, Non-structural protein 1, NS1

Japanese encephalitis virus (strain M28) (JEV)

WB,IHC,ELISA

WB 1:500-1:2000
IHC 1:50-1:300
ELISA 1:5000-1:20000

132kD

Rabbit

Recombinant Japanese encephalitis virus (JEV) Capsid protein C/Core protein (Lys18-Lys104).

Polyclonal

IgG

Antigen affinity purification.

0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300.

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Store at 4℃ short term (1-2 weeks). Store at -20℃ 12 months.