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AB256443

Recombinant Nipah Virus Glycoprotein F (Fc Chimera)

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Recombinant Nipah Virus Glycoprotein F (Fc Chimera) is a Henipavirus nipahense Fragment protein, in the 1 to 486 aa range, expressed in HEK 293 cells, with >90%, suitable for SDS-PAGE.
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SDS-PAGE - Recombinant Nipah Virus Glycoprotein F (Fc Chimera) (AB256443)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Nipah Virus Glycoprotein F (Fc Chimera) (AB256443)

SDS-PAGE analysis of 2 μg (Lane 1) and 0.2 μg (Lane 2) of ab256443 under reducing conditions.

Key facts

Purity

>90% SDS-PAGE

Expression system

HEK 293 cells

Tags

Fc tag C-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q9IH63-1

Animal free

No

Carrier free

No

Species

Henipavirus nipahense

Storage buffer

pH: 7 - 8 Constituents: PBS

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"linker":null,"sequence":"MVVILDKRCYCNLLILILMISECSVGILHYEKLSKIGLVKGVTRKYKIKSNPLTKDIVIKMIPNVSNMSQCTGSVMENYKTRLNGILTPIKGALEIYKNNTHDLVGDVRLAGVIMAGVAIGIATAAQITAGVALYEAMKNADNINKLKSSIESTNEAVVKLQETAEKTVYVLTALQDYINTNLVPTIDKISCKQTELSLDLALSKYLSDLLFVFGPNLQDPVSNSMTIQAISQAFGGNYETLLRTLGYATEDFDDLLESDSITGQIIYVDLSSYYIIVRVYFPILTEIQQAYIQELLPVSFNNDNSEWISIVPNFILVRNTLISNIEIGFCLITKRSVICNQDYATPMTNNMRECLTGSTEKCPRELVVSSHVPRFALSNGVLFANCISVTCQCQTTGRAISQSGEQTLLMIDNTTCPTAVLGNVIISLGKYLGSVNYNSEGIAIGPPVFTDKVDISSQISSMNQSLQQSKDYIKEAQRLLDTVNP","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":486,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"Q9IH63","tags":[{"tag":"Fc","terminus":"C-Terminus"}]}]
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Properties and storage information

Form
Liquid
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
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

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.

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.
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Product protocols

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Target data

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.
See full target information Fusion glycoprotein F0

Alternative Names

Fusion glycoprotein F0, Protein F, F
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