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Mouse Anti-Rift Valley Fever Virus Nucleoprotein (M979)

$406.78$1,020.72 excl. VAT

Mouse anti Rift Valley Fever Nucleoprotein (M979) recognises RVFV N protein and is suitable for use in ELISA. Greater than 90% purity by SDS-PAGE.


Rift Valley Fever Nucleoprotein (M979) antibody recognises RVFV N protein and is suitable for use as in ELISA.



  • Mouse anti Rift Valley Fever Nucleoprotein (M979). Recognises RVFV N protein in ELISA.
  • Purified by Ion Exchange. >90% purity by SDS-PAGE.
  • Presented in phosphate buffered saline, pH 7.2 with 0.05% sodium azide.



The Mucleoprotein forms a filamentous ring that encapsulates viral RNA and is necessary for replication and transcription of its genome by the viral polymerase. A crystal structure produced by Ferron et al. shows the Nucleoprotein as forming a homohexameric ring. Within the inner side of the ring, positive residues are shown to bind RNA for various putative functions and are conserved across Phlebovirus species. Xu et al. demonstrate that the Nucleoprotein is a key immunogen during mouse infection and surmise that RVFV N-subunit vaccines are able to induce CD8 responses that protect against RVFV.

Rift Valley Fever was first recorded in the early 1930s, in the Rift Valley region of Kenya as a result of a large outbreak among livestock. RVFV is an enveloped, negative-sense, single-stranded RNA virus that belongs to the genus Phlebovirus, of the Bunyaviridae family. Bunyaviruses have tripartite genomes that consist of large, medium and small RNA segments – each coding different viral proteins. The small, (S) segment is responsible for encoding Nucleoprotein, which is responsible for the formation of ribonucleoprotein complexes that are essential in the RVFV life cycle and for the replication of its genome (Mottram et al., 2017).

RVFV is an arbovirus, transmitted to livestock by the Aedes and Culex genera of mosquitoes. Sheep, cattle, camels and goats are particularly susceptible to Rift Valley Fever and act as amplifying hosts for RVFV (WHO). RVFV circulates in sub-Saharan Africa, and has more recently been found in Egypt, Saudi-Arabia, Yemen, Mayotte and Madagascar. The geographical expansion of the virus also threatens Europe, where RVFV outbreaks in the region have raised concerns that it may spread to more temperate climates.

Rift Valley Fever infection results in several syndromes that range from a febrile illness to blindness, encephalitis, or lethal hemorrhagic fever. RVFV vaccines are only partially attenuated, are cost-prohibitive and only induce short-lived immunity. No specific drugs are available to treat Rift Valley Fever and preventive efforts against outbreaks are mostly based on monitoring mosquito distribution.



  • Ferron et al. (2011). The Hexamer Structure of the Rift Valley Fever Virus Nucleoprotein Suggests a Mechanism for its Assembly into Ribonucleoprotein Complexes. Pathogens.
  • Mottram et al. (2017). Mutational analysis of Rift Valley fever phlebovirus nucleocapsid protein indicates novel conserved, functional amino acids. Neglected Tropical Diseases.
  • World health organisation (WHO). Rift Valley fever.
  • Xu et al. (2013) The Nucleocapsid Protein of Rift Valley Fever Virus Is a Potent Human CD8 T Cell Antigen and Elicits Memory Responses. PLoS ONE 8(3).

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