Mouse Anti-Crimean-Congo Hemorrhagic Fever Virus Nucleoprotein Antibody (BA11)
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Mouse anti Crimean Congo Hemorrhagic Fever Virus (CCHFV) Nucleoprotein (clone BA11). Antibody shows no cross-reactivity with CCHFV Gn protein in ELISA or Western blot.
MOUSE ANTI-CRIMEAN-CONGO HEMORRHAGIC FEVER VIRUS NUCLEOPROTEIN ANTIBODY (BA11)
Mouse anti CCHFV Nucleoprotein is a monolonal antibody against Crimean Congo Hemorrhagic Fever Virus (CCHFV) Nucleoprotein. The antibody was raised against The Native Antigen Company’s recombinant CCHF virus Gn and Nucleoprotein, expressed in mammalian HEK293 cells.
PRODUCT DETAILS – MOUSE ANTI-CRIMEAN-CONGO HEMORRHAGIC FEVER VIRUS NUCLEOPROTEIN ANTIBODY (BA11)
- Mouse anti Crimean Congo Hemorrhagic Fever Virus Nucleoprotein (clone BA11).
- Immugen comprised an equal mix of Crimean Congo Hemorrhagic Fever Virus Gn protein and Nucleoprotein.
- Antibody shows no cross-reactivity with CCHFV Gn protein in ELISA.
- The antibody is specific for NP by Western blot.
Crimean Congo hemorrhagic fever (CCHF) virus is a tick-borne enveloped single stranded RNA virus that belongs to the genus Nairovirus and a member of the Bunyaviridae family. CCHF virus causes a hemorrhagic disease in humans with up to 80% case fatality. Although the virus has only caused sporadic disease in the past, the expansion of the range of its vector, the Hyalomma tick, is causing increasing concern that case numbers will continue to rise. Since CCHF was first described in Crimea in 1944, sporadic outbreaks have occurred globally. In 2015, CCHFV was identified by the WHO as an emerging virus which is likely to cause a severe epidemic and which may present a public health emergency.
Research into diagnosis of the illness, and also into vaccine development is increasing.The CCHF virus Nucleoprotein is a potential target for vaccine development, although efficacy has not yet been demonstrated. CCHF virus Nucleoprotein consists of a large, globular domain, plus a protrusion that contains a conserved caspase-3 cleavage site The globular region is responsible for RNA binding, while the role of the caspase-3 cleavage site is currently unclear. The X-ray crystallographic structure of CCHFV N protein at 2.3 Å resolution revealed the presence of head and stalk domains in the N protein structure which is more closely related to the nucleocapsid protein of Arenaviruses compared to the nucleocapsid protein of other Bunyaviruses.