Recombinant Nipah Virus Glycoprotein F (Fc Chimera)
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Recombinant Nipah Virus Glycoprotein F (Fc Chimera) is a Nipah virus Fragment protein, in the 1 to 486 aa range, expressed in HEK 293 cells, with >90%, suitable for SDS-PAGE.
View Alternative Names
Fusion glycoprotein F0, Protein F, F
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Nipah Virus Glycoprotein F (Fc Chimera) (AB256444)
SDS-PAGE analysis of 2 μg (Lane 1) and 0.2 μg (Lane 2) of ab256444 under reducing conditions.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
F protein is involved in the process of infecting host cells by mediating membrane fusion and subsequent viral entry. It functions as a fusogenic protein forming a complex with another viral protein Glycoprotein G during infection. This interaction enhances the efficiency of membrane fusion. The fusion activity of F protein enables the payload of the virus including its genetic material to enter the host cell cytoplasm initiating the replication mechanism of the virus. This biological process is essential for the lifecycle of enveloped viruses like RSV and hMPV.
Pathways
F protein participates in the membrane fusion pathway important for viral entry and infection. This pathway is tightly regulated and involves other host proteins like heparan sulfate proteoglycans that facilitate virus attachment. Additionally F protein's function intersects with the Toll-like receptor signaling pathway where it stimulates immune responses once viral fusion and entry activate these receptors. The interactions with host proteins in these pathways highlight the importance of F protein in the early stages of viral infection and the host's defense response.
Specifications
Form
Liquid
General info
Function
Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states : pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with G at the virion surface. Upon G binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis.
Sequence similarities
Belongs to the paramyxoviruses fusion glycoprotein family.
Post-translational modifications
The inactive precursor F0 is glycosylated and proteolytically cleaved into F1 and F2 to be functionally active. The cleavage is mediated by cellular proteases during the transport and maturation of the polypeptide (By similarity).
Target data
Complementary Products
Proteins & Peptides
AB256429
Recombinant Rubella Virus spike glycoprotein E1 protein (Fc Chimera)
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Product promise
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