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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 NOWEbola virus (EBOV) is an enveloped and negative-stranded RNA virus, a member of the Ebolavirus genus, and the causative agent of Ebola virus disease (EVD), a condition characterized by a hemorrhagic fever and a high mortality rate, that is endemic to western and equatorial Africa.1 The single-stranded RNA genome of EBOV encodes seven proteins: nucleoprotein (NP), virion protein 40 (VP40), VP35, VP30, VP24, glycoprotein (GP), and an RNA-dependent RNA polymerase (L).1,2 EBOV VP24 is a monomeric structural protein that is composed of N- and C-terminal domains that form a pyramidal structure.3 It functions with VP35 and NP in nucleocapsid formation, and both N- and C-terminal domains of VP40 are required for proper nucleocapsid structure.4,1 EBOV VP24 disrupts the innate immune viral response by inhibiting expression of the gene encoding IFN-λ1 and prevents phosphorylated STAT1 nuclear translocation and transcriptional activity in mammalian cells expressing VP40.1,5,3 Cayman's Ebola Virus VP24 (subtype Zaire, strain H. sapiens-wt/GIN/2014/Kissidougou-C15) (recombinant) protein consists of 233 amino acids and has a calculated molecular weight of 28.5 kDa.
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1. Ebola virus disease: An emerging and re-
2. Ebola virus entry: From molecular characterization to drug discovery. Viruses 11(3), 274 (2019).
3. The ebola virus interferon antagonist VP24 directly binds STAT1 and has a novel, pyramidal fold. PLoS Pathog. 8(2), e1002550 (2012).
4. Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and genome packaging. Sci. Rep. 7(1), 7698 (2017).
5. Ebolavirus protein VP24 interferes with innate immune responses by inhibiting interferon-