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Explore how neutrophils shape the immune response in health and disease. This poster highlights neutrophil pathogen defense mechanisms, including phagocytosis, degranulation, and NETosis, as well as neutrophil roles in inflammation and NET-associated pathologies.
DOWNLOAD NOWRift Valley fever virus (RVFV) is a single-stranded negative-sense RNA virus, member of the Phlebovirus genus, and mosquito-transmitted pathogen endemic to sub-Saharan Africa and the Arabian peninsula.1,2,3 The tripartite RNA genome of RVFV is composed of three segments: L, which encodes L protein, a single-polypeptide RNA-dependent RNA polymerase (RdRp), M, which encodes a single open reading frame (ORF) that produces the envelope glycoproteins Gn and Gc and non-structural proteins NSm and Gn/NSm fusion protein, and S, which is ambisense, encoding the nucleoprotein N in the genomic sense orientation, and the non-structural protein and major virulence factor NSs in the antigenomic orientation.3,2 RVFV L protein is composed of an N-terminal endonuclease domain linked to a PA-C-like domain, an RdRp core, a PB2-N-like domain, a CBD domain, and a C-terminal lariat domain.4 The N-terminal endonuclease domain is essential for cap-snatching during host mRNA transcription, and the RdRp core is essential for viral RNA production. Expression of a dominant-negative L protein mutant inhibits viral gene expression in RVFV-infected BHK/T7-9 cells.5 Cayman’s Rift Valley Fever Virus L protein (TAN/Dod-002/07) (recombinant) consists of 256 amino acids and has a calculated molecular weight of 29.4 kDa.
WARNING This product is not for human or veterinary use.
1. Structure of Rift Valley Fever Virus RNA-
2. Rift Valley fever virus structural and nonstructural proteins: recombinant protein expression and immunoreactivity against antisera from sheep. Vector Borne Zoonotic Dis. 13(9), 619-629 (2013).
3. Molecular aspects of Rift Valley fever virus and the emergence of reassortants. Virus Genes 55(1), (2019).
4. Structural elucidation of rift valley fever virus L protein towards the discovery of its potential inhibitors. Pharmaceuticals (Basel) 15(6), 659 (2022).
5. Rift valley fever virus L protein forms a biologically active oligomer. J. Virol. 83(24), 12779-12789 (2009).