Human Recombinant IFITM3 protein, Fc Tag (V2LY-0526-LY4200)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
Fc Tag
Protein Construction
This product is Human Recombinant IFITM3 protein, Fc Tag consist of Amino Acid: 1-57 and predicts a molecular mass of 32.9 kDa.
Molecule Mass
32.9 kDa
Sequence
Amino Acid: 1-57
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>95% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
interferon induced transmembrane protein 3
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:33270927, PubMed:33239446).

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).
Biological Process
Defense response to virus Source: UniProtKB
Immune response Source: ProtInc
Negative regulation of viral entry into host cell Source: UniProtKB
Negative regulation of viral genome replication Source: UniProtKB
Negative regulation of viral transcription Source: UniProtKB
Response to interferon-alpha Source: UniProtKB
Response to interferon-beta Source: UniProtKB
Response to interferon-gamma Source: UniProtKB
Response to virus Source: UniProtKB
Type I interferon signaling pathway Source: GO_Central
Cellular Location
Lysosome membrane; Late endosome membrane; Early endosome membrane; Cell membrane; Perinuclear region. Co-localizes with BRI3 isoform 1 at the perinuclear region.
Topology
Cytoplasmic: 1-57
Helical: 58-78
Cytoplasmic: 79-107
Helical: 108-128
Extracellular: 129-133
PTM
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.

Schönfelder, K., Breuckmann, K., Elsner, C., Dittmer, U., Fistera, D., Herbstreit, F., ... & Möhlendick, B. (2021). The influence of IFITM3 polymorphisms on susceptibility to SARS-CoV-2 infection and severity of COVID-19. Cytokine, 142, 155492.

Ahi, Y. S., Yimer, D., Shi, G., Majdoul, S., Rahman, K., Rein, A., & Compton, A. A. (2020). IFITM3 reduces retroviral envelope abundance and function and is counteracted by glycoGag. MBio, 11(1), 10-1128.

Lee, J., Robinson, M. E., Ma, N., Artadji, D., Ahmed, M. A., Xiao, G., ... & Müschen, M. (2020). IFITM3 functions as a PIP3 scaffold to amplify PI3K signalling in B cells. Nature, 588(7838), 491-497.

Rajapaksa, U. S., Jin, C., & Dong, T. (2020). Malignancy and IFITM3: friend or foe?. Frontiers in Oncology, 10, 593245.

Hur, J. Y., Frost, G. R., Wu, X., Crump, C., Pan, S. J., Wong, E., ... & Li, Y. M. (2020). The innate immunity protein IFITM3 modulates γ-secretase in Alzheimer’s disease. Nature, 586(7831), 735-740.

Wellington, D., Laurenson-Schafer, H., Abdel-Haq, A., & Dong, T. (2019). IFITM3: How genetics influence influenza infection demographically. Biomedical journal, 42(1), 19-26.

Spence, J. S., He, R., Hoffmann, H. H., Das, T., Thinon, E., Rice, C. M., ... & Hang, H. C. (2019). IFITM3 directly engages and shuttles incoming virus particles to lysosomes. Nature chemical biology, 15(3), 259-268.

Campbell, R. A., Schwertz, H., Hottz, E. D., Rowley, J. W., Manne, B. K., Washington, A. V., ... & Rondina, M. T. (2019). Human megakaryocytes possess intrinsic antiviral immunity through regulated induction of IFITM3. Blood, The Journal of the American Society of Hematology, 133(19), 2013-2026.

Kenney, A. D., McMichael, T. M., Imas, A., Chesarino, N. M., Zhang, L., Dorn, L. E., ... & Yount, J. S. (2019). IFITM3 protects the heart during influenza virus infection. Proceedings of the National Academy of Sciences, 116(37), 18607-18612.

Zani, A., & Yount, J. S. (2018). Antiviral protection by IFITM3 in vivo. Current clinical microbiology reports, 5, 229-237.

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For research use only. Not intended for any clinical use.

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