[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. .; [Non-structural protein 1]: 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). .; [Non-structural protein 1]: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. .

p18356

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

Dengue virus type 2 (strain Thailand/PUO-218/1980) (DENV-2),Dengue virus type 2 (strain Jamaica/1409/1983) (DENV-2)

ELISA,Neutralization

ELISA 1:5000-1:20000
Neutralization,The optimal dilutions should be determined by the end user.

75kD

Human

Monoclonal

H268

IgG1, kappa

Protein A/G purified from cell culture supernatant.

>95% as determined by SDS-PAGE.

0.01M PBS, pH 7.4.

1 mg/ml

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

For research use only. Not suitable for clinical or therapeutic use.