Ebola virus is one of the deadliest viruses known to man, causing infrequent outbreaks of hemorrhagic disease with case fatality rates up to 90%. (Lehrer et al., 2019).
Ebola virus particles comprise seven structural proteins of which four (nucleoprotein (NP), VP35, VP30, and the RNA-dependent RNA polymerase (L)) are components of the ribonucleoprotein complex that is responsible for viral genome replication. Glycoprotein (GP), VP40, and VP24 are membrane-associated proteins and VP24 is believed to be involved in nucleocapsid formation. VP40 (viral protein 40kD) is the most abundantly expressed viral protein during filoviral infection. It is a major structural protein that plays a central role in virus assembly and budding at the plasma membrane of infected cells. VP40 proteins associate with cellular membranes, interacting with the cytoplasmic tails of glycoproteins and binding to the ribonucleoprotein complex.
The VP40 monomer consists of two protein domains connected by a flexible linker; the N-terminal oligomerization domain and the C-terminal membrane-binding domain. VP40 goes through intermediate states of assembly (e.g. octamers) (Silva et al., 2012) but both domains fold into beta sandwich structures of similar topology (Dessen et al., 2000). Within the N-terminal domain there are two overlapping L-domains (PTAP and PPEY, residues 7 to 13), which are required for efficient budding (Timmins et al., 2003) by interacting with specific host cellular proteins, such as tsg101 and vps-4 (Licata et al., 2003).
Vaccine candidates have been described containing the EBOV glycoprotein with matrix proteins VP24 and VP40 (Lehrer et al., 2019). Indeed, recombinant expression of VP40 in mammalian cells generates virus-like particles that are morphologically similar to live virus, but non-infectious. (Silva et al., 2012). These VLPs have been shown to protect mice from a challenge with a lethal dose of mouse-adapted Ebola Virus (Zaire). Antiviral therapeutics directed against the VP40 domains are also in development (Madara et al., 2015).
Source:Recombinant protein corresponding to 325aa from Ebola Virus VP40, fused to 6xHis-Tag at C-terminal, expressed in E. coli.
Applications:Suitable for use in development of immunoassays. Other applications not tested.
Recommended Dilution:Optimal dilutions to be determined by the researcher.
Storage and Stability:May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 6 months after receipt at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
仕様
Size：100ug
Source Antigen：Recombinant, E. coli
Grade：Highly Purified
Purity：≥95%
Form：Supplied as a liquid in PBS, 25mM arginine, 0.02% sodium azide
