Recombinant Nipah Virus Glycoprotein F (Fc Chimera) is a Nipah virus Fragment protein, in the 1 to 486 aa range, expressed in HEK 293, with >90% purity and suitable for SDS-PAGE.
Images
Key facts
- Purity
- >90% SDS-PAGE
- Expression system
- HEK 293 cells
- Tags
- Fc tag C-Terminus
- Applications
- SDS-PAGE
- Biologically active
- No
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Target data
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.
Alternative names
Fusion glycoprotein F0, Protein F, F
Recommended products
Recombinant Nipah Virus Glycoprotein F (Fc Chimera) is a Nipah virus Fragment protein, in the 1 to 486 aa range, expressed in HEK 293, with >90% purity and suitable for SDS-PAGE.
Key facts
- Purity
- >90% SDS-PAGE
- Expression system
- HEK 293 cells
- Tags
- Fc tag C-Terminus
- Applications
- SDS-PAGE
- Biologically active
- No
- Accession
- Q9IH63-1
- Animal free
- No
- Species
- Nipah virus
- Concentration
- Storage buffer
pH: 7 - 8
Constituents: PBS
Sequence info
Amino acid sequence
- Accession
- Q9IH63
- Protein length
- Fragment
- Amino acids
- 1 to 486
- Nature
- Recombinant
- Tags
- Fc tag C-Terminus
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).
Storage
- Shipped at conditions
- Dry Ice
- Appropriate short-term storage conditions
- -80°C
- Appropriate long-term storage conditions
- -80°C
- Storage information
- Avoid freeze / thaw cycle
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
Glycoprotein F also known as F protein is an envelope protein that facilitates membrane fusion. It has a significant role in viral infections particularly where it facilitates entry of virions into host cells. The protein typically has a molecular mass ranging between 60 to 70 kilodaltons and is expressed on the surface of enveloped viruses such as respiratory syncytial virus (RSV) and human metapneumovirus (hMPV). F protein undergoes conformational changes that drive the fusion of viral and cellular membranes which is an important step for viral infection.
- 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.
- Associated diseases and disorders
The role of F protein is significant in respiratory infections particularly in diseases like bronchiolitis and pneumonia caused by RSV and hMPV. Its function influences disease severity as the protein's ability to facilitate viral entry directly affects viral load and subsequent immune response. Studies have linked F protein with interferon regulatory factors proteins involved in the immune response to these infections. Targeting F protein in therapeutic interventions shows potential for reducing infection rates and severity of respiratory illnesses caused by these viruses.
Product promise
We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.
In the unlikely event of one of our products not working as expected, you are covered by our product promise.
Full details and terms and conditions can be found here:
Terms & Conditions.
1 product image
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.
Downloads
Product protocols
- Visit the general protocols
- Visit troubleshooting
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com