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Interferon induced transmembrane protein 1 (IFITM1), also known as CD225 or 9-27, is a member of the IFITM family, and for which structure consists of an approximately 14-kDa glycoprotein with signature topology characterized by two membrane-spanning segments with a conserved cytosolic loop. IFITM1 is an early effector of innate immunity that localizes at the plasma membrane and in late endosomes. As one of the first responders to viral invasion, its transcription is rapidly induced by type I and II interferons. This protein performs a ubiquitous antiviral defense by blocking hemifusion of viral envelopes with host membranes, neutralizing threats as diverse as influenza A and SARS-CoV-2 to HIV-1 and Ebola virus. Beyond infectious disease, IFITM1 is implicated in gametogenesis, osteogenesis and carcinogenesis. In solid tumors, it can enhance intercellular adhesion and prevent metastatic dissemination whereas in hematologic malignancies it often correlates with chemoresistance and poor prognosis. This dual-role as a viral entry regulator and general cancer-modulating gene makes IFITM1 an exciting target in antiviral drug discovery, interferon biomarker programs and the study of tumor microenvironment.
Fig.1 IFITMs and their effects against HIV-1.1
IFITM1 as a mere member of the interferon stimulation group which has emerged across studies in various organs and species:
The product portfolio includes full-length and engineered IFITM1 membrane protein constructs designed to support structural and functional research on this compact membrane-associated protein. Because IFITM1 function is closely linked to its membrane localization and lipid environment, appropriate protein format is an important consideration for experimental studies. These products can support structural characterization, lipid-interaction studies, antibody development, and investigation of IFITM1-related antiviral mechanisms. Available construct formats, post-translational modification status, membrane-associated properties, and functional characteristics should be determined according to the corresponding product data and intended research application.
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Panels of accurately modeled human cells are essential to explore IFITM1 biology and develop therapeutic candidates. We created reliable IFITM1 stable cell lines with appropriate membrane localization, interferon-inducible expression and strong antiviral restriction using lentiviral and transposon co-delivery. Our screening platform consists not only of wild-type constructs but also palmitoylation-defective mutants and N-terminal truncations, plus real-time pathway monitoring with a luciferase reporter-modified ISRE. We also provide knockout rescue systems and lines co-expressing viral entry receptors for performing mechanism-of-action studies. Genomic mapping, surface staining and pseudovirus challenge assays authenticate each clone and establish a strong basis for antiviral compound screening and innate immune studies.
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The IFITM1 monoclonal antibody suite that we present was carefully developed with the molecular architecture of this interferon-responsive protein in mind. These clones recognize both native and denatured membrane-embedded epitopes, distinguish IFITM1 from its closely related paralogs (IFITM2) as well as their functional homologs (IFITM3), identify palmitoylation-sensitive epitopes. Pre-validated applications include Western blotting, ELISA (direct and sandwich), flow cytometry of permeabilized cells, imaging by immunofluorescence in membrane vs endosomal pools, IHC on formalin-fixed clinical specimens as well functional blockade for viral restriction. This versatility enables expression profiling at different stages during disease progression, trafficking analysis following interferon stimulation, and the knowledge-based development of therapeutic abs for infectious diseases and cancer.
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Beyond our regular catalog, we offer comprehensive design and engineering services tailored specifically for IFITM1-specific programs:
We offer N-terminal amphipathetic region-deficient constructs, individual transmembrane segments or the cytosolic loop for more detailed structure-function studies.
Analytical profiling during quality control preserves and verifies palmitoylation along with other lipid modifications essential for membrane anchoring and activity.
Because our expression systems are based on mammalian cells, proteins will be incorporated into the plasma membrane and endosomal compartments in a native orientation that should allow for effective function of antiviral proteins as well maintenance of antibody epitopes.
Yes. Here we provide palmitoylation-site mutants, N-terminal deletions and loop substitutions that modulate membrane partitioning and viral restriction. These are provided as either purified proteins or stable cell lines.