IFIT1 Antibodies

Background

IFIT1 is a cytoplasmic protein induced by interferons, mainly present in various cells of mammals. This protein inhibits viral replication and translation by recognizing and binding to viral RNA, thus playing a crucial role in the innate immune defense. During the process of anti-viral infection, IFIT1 helps cells maintain internal environmental stability and cope with molecular changes caused by pathogen invasion. This gene was first identified in interferon research in the 1980s and is one of the early interferon-stimulated genes. The elucidation of its mechanism has deepened our understanding of the host antiviral response pathway. Its specific RNA-binding property has been extensively studied, providing an important model for explaining the interaction between immune proteins and nucleic acids, and the regulation of cellular antiviral signals, etc. in biological processes.

Structure Function Application Advantage Our Products

Structure of IFIT1

IFIT1 is a protein induced by interferon, with a molecular weight of approximately 56 kDa. The molecular weight of IFIT1 varies slightly among different species, mainly due to differences in the splicing variants of its encoding gene or post-translational modifications.

Species	Human	Mouse	Rhesus monkey	Rat	Chicken
Molecular Weight (kDa)	~56	~54	~56	~55	~58
Primary Structural Differences	Identification of 5' un-methylated RNA	Core protein of antiviral response	High homology with humans	Model proteins for studying viral infections	Members of the innate immunity of birds

The IFIT1 protein contains multiple tandem TPR domains, which together form a rigid structural framework. Its tertiary structure constitutes a positively charged RNA-binding pocket that can specifically recognize and bind to viral RNA with unmethylated 5' triphosphate (PPP-RNA) or uncap structure. This protein physically isolates viral messenger RNA, blocking its binding to the cell's translation machinery, thereby establishing an anti-viral barrier within the cell.

Fig. 1 The structure of the human IFIT1 protein complex with RNA (PDB:5UDI).¹

Key structural properties of IFIT1:

Containing multiple tandem TPR domains, it forms a rigid horseshoe-shaped structure
Positively charged RNA binding grooves, with arginine and lysine residues distributed on the surface
Specifically bind to 5' un-methylated or triphosphorylated viral RNA

Functions of IFIT1

The main function of the IFIT1 protein is to recognize and inhibit viral replication in the innate immune response of cells. Additionally, it also participates in regulating the gene expression and signaling pathways of the cells themselves.

Function	Description
Virus RNA Recognition and Binding	Specifically binds to viral RNA with an unmodified 5' cap structure (Cap-0) or 5' terminal triphosphate (PPP), which is the key mechanism for distinguishing "self" from "non-self" RNA.
Translation Inhibition	By physically isolating viral mRNA or competitively binding to components such as eukaryotic translation initiation factor eIF3, the synthesis of viral proteins is directly blocked.
Innate Immune Signal Transduction	As a core member of interferon-stimulated genes (ISGs), its expression itself serves as a marker for the activation of the type I interferon pathway and can enhance the antiviral response state.
Cell Proliferation and Apoptosis Regulation	In certain circumstances, the highly expressed IFIT1 can inhibit cell cycle progression or promote apoptosis, thereby limiting the spread of the virus between cells.
Host RNA Metabolism Regulation	Recent studies have shown that IFIT1 may also participate in regulating the post-transcriptional gene expression of the cells itself by binding to specific endogenous RNA molecules.

Unlike the mechanism by which antibodies specifically recognize antigenic epitopes, IFIT1 recognizes a common set of RNA chemical features (such as 5' modification status) through its conserved domain. This pattern recognition approach enables it to broadly inhibit a variety of viruses with different sequences but similar molecular characteristics, making it an important early line of defense in the host's innate immunity.

Applications of IFIT1 and IFIT1 Antibody in Literature

1. Xie, Shijie, et al. "A poxvirus ankyrin protein LSDV012 inhibits IFIT1 in a host-species-specific manner by compromising its RNA binding ability." PLoS pathogens 21.3 (2025): e1012994. https://doi.org/10.1371/journal.ppat.1012994

This study reveals that the LSDV viral protein LSDV012 interacts with the host protein IFIT1, alters its localization and inhibits its RNA binding ability, thereby antagonizing the antiviral response of type I interferons. It elucidates a new mechanism of the in host-specific immune evasion.

2. Mears, Harriet V., et al. "Ifit1 regulates norovirus infection and enhances the interferon response in murine macrophage-like cells." Wellcome Open Research 4 (2019): 82. https://doi.org/10.12688/wellcomeopenres.15223.1

This study reveals that the translation of the norovirus VPg can resist direct inhibition by IFIT1, but IFIT1 plays a crucial antiviral role by enhancing the expression of interferon in cells upon sensing cytoplasmic RNA.

3. Li, Tian-Hao, et al. "RETRACTED ARTICLE: IFIT1 modulates the proliferation, migration and invasion of pancreatic cancer cells via Wnt/β-catenin signaling." Cellular Oncology 44.6 (2021): 1425-1437. https://doi.org/10.1007/s13402-021-00651-8

The study found that IFIT1 is highly expressed in pancreatic cancer and is associated with poor prognosis. It promotes the proliferation, migration, invasion and epithelial-mesenchymal transition of tumor cells by activating the Wnt/β-catenin pathway.

4. Zan, Xiangyi, et al. "COL8A1 promotes NSCLC progression through IFIT1/IFIT3-mediated EGFR activation." Frontiers in Oncology 12 (2022): 707525. https://doi.org/10.3389/fonc.2022.707525

The study found that COL8A1 in non-small cell lung cancer promotes the activation of the EGFR pathway by upregulating IFIT1 and IFIT3, thereby driving tumor cell proliferation, migration, and inhibiting cell apoptosis.

5. Liu, Yuan-jie, et al. "IFIT1+ neutrophil is a causative factor of immunosuppressive features of poorly cohesive carcinoma (PCC)." Journal of Translational Medicine 22.1 (2024): 580. https://doi.org/10.1186/s12967-024-05389-z

The research has found that IFIT1-positive tumor-associated neutrophils in gastric cancer promote tumor invasion and metastasis by mediating an immunosuppressive microenvironment and upregulating PD-L1 expression, and this leads to drug resistance of PD-1 immunotherapy in patients.

Creative Biolabs: IFIT1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality IFIT1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom IFIT1 Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our IFIT1 antibodies, custom preparations, or technical support, contact us at email.

Reference

Xie, Shijie, et al. "A poxvirus ankyrin protein LSDV012 inhibits IFIT1 in a host-species-specific manner by compromising its RNA binding ability." PLoS pathogens 21.3 (2025): e1012994. https://doi.org/10.1371/journal.ppat.1012994