Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.
Concentration：
1mg/ml
Clonality：
Polyclonal
Isotype：
IgG
Applications：
WB=1:500-2000ELISA=1:5000-10000not yet tested in other applications.optimal dilutions/concentrations should be determined by the end user.
Host：
Goat
Product Overview：
Sample: Lane 1: Recombinant CSFV E2 protein Primary: Anti-CSFV E2 (SL20116G) at 1/1000 dilutionSecondary: IRDye800CW Donkey anti-Goat IgG at 1/20000 dilutionPredicted band size: 42 kDaObserved band size: 32 kDa
Classical swine fever(CSF) is a kind of acute and intense contagious disease in swine, it material damages swine industry. CSF could cause swine appearing disseminated hemorrhage in systemic organ and tissue, degeneration and necrosis in small vascular and capillary endothelial cells. Classical swine fever virus (CSFV) belongs to genera Pestivirus, family Flaviviridae, it’s genome total length is 12.3Kb,including a big ORF, encoding 11 structural and nonstructural proteins.
Function: E(rns), E1 and E2 are responsible of cell attachment and subsequent fusion of viral and cellular membrane.
P7 forms a leader sequence to properly orient NS2 in the membrane.
Uncleaved NS2-3 is required for production of infectious virus.
NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus.
NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase.
NS4A is a cofactor for the NS3 protease activity.
RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome.
Subunit: The E(rns) glycoprotein is found as a homodimer; disulfide-linked. The E1 and E2 envelope glycoproteins form disulfide-linked homodimers as well as heterodimers.
Subcellular Location: Host cell surface.
Post-translational modifications: The E(rns) glycoprotein is heavily glycosylated.
The viral RNA of pestiviruses is expressed as a single polyprotein which undergoes post-translational proteolytic processing resulting in the production of at least eleven individual proteins. The N-terminal protease cleaves itself from the nascent polyprotein autocatalytically and thereby generates the N-terminus of the adjacent viral capsid protein C.
Cleavage between E2 and p7 is partial.
