Recombinant Human Fragilis protein (Fc Chimera)
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Recombinant Human Fragilis protein (Fc Chimera) is a Human Fragment protein, in the 1 to 57 aa range, expressed in HEK 293 cells, with >99%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.
View Alternative Names
Interferon-induced transmembrane protein 3, Dispanin subfamily A member 2b, Interferon-inducible protein 1-8U, DSPA2b, IFITM3
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Fragilis protein (Fc Chimera) (AB276480)
SDS-PAGE analysis of ab276480
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
IFITM3 acts as an antiviral protein that disrupts the life cycle of viruses entering human cells. It is a part of a family of transmembrane proteins that block viral replication by inhibiting the fusion of viral membranes with endosomal membranes. The presence of Fragilis in respiratory epithelial cells is integral to the immune response against viral infections. The protein acts as a barrier to viruses like influenza providing an innate immune defense mechanism.
Pathways
The involvement of IFITM3 is central to the immune signaling pathways specifically the interferon signaling pathway. Upon viral infection interferons upregulate IFITM3 enhancing its antiviral activities. Other proteins like STAT1 and STAT2 mediate this regulation. Additionally IFITM3 aligns with the pathways regulating cell membrane integrity and remodeling highlighting its multi-functional role beyond just antiviral defense.
Specifications
Form
Lyophilized
General info
Function
IFN-induced antiviral protein which disrupts intracellular cholesterol homeostasis. Inhibits the entry of viruses to the host cell cytoplasm by preventing viral fusion with cholesterol depleted endosomes. May inactivate new enveloped viruses which buds out of the infected cell, by letting them go out with a cholesterol depleted membrane. Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV) (PubMed : 26354436, PubMed : 33239446, PubMed : 33270927). Can inhibit : influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS-CoV and SARS-CoV-2 S protein-mediated viral entry and VSV G protein-mediated viral entry (PubMed : 33270927). Plays a critical role in the structural stability and function of vacuolar ATPase (v-ATPase). Establishes physical contact with the v-ATPase of endosomes which is critical for proper clathrin localization and is also required for the function of the v-ATPase to lower the pH in phagocytic endosomes thus establishing an antiviral state. In hepatocytes, IFITM proteins act in a coordinated manner to restrict HCV infection by targeting the endocytosed HCV virion for lysosomal degradation (PubMed : 26354436). IFITM2 and IFITM3 display anti-HCV activity that may complement the anti-HCV activity of IFITM1 by inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome (PubMed : 26354436). Exerts opposing activities on SARS-CoV-2, including amphipathicity-dependent restriction of virus at endosomes and amphipathicity-independent enhancement of infection at the plasma membrane (PubMed : 33270927).
Sequence similarities
Belongs to the CD225/Dispanin family.
Post-translational modifications
Palmitoylation on membrane-proximal cysteines controls clustering in membrane compartments and antiviral activity against influenza virus and hepatitis C virus (HCV). Has no effect on anti-SARS-CoV-2 activity.. Not glycosylated.. Polyubiquitinated with both 'Lys-48' and 'Lys-63' linkages. Ubiquitination negatively regulates antiviral activity. Lys-24 is the most prevalent ubiquitination site.. Phosphorylation at Tyr-20 is required for endosomal and lysosomal location.
Subcellular localisation
Late endosome membrane
Target data
Complementary Products
Product promise
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