IFIT3 Antibodies

Structure of IFIT3

The molecular weight of IFIT3 protein is approximately 55 kDa, and it varies slightly among different species due to differences in amino acid sequences.

The IFIT3 protein consists of 478 amino acids. Its core structure is formed by multiple 34-peptide repeating sequences (TPR) arranged in a helix-turn-helix folding pattern. These TPR motifs form protein interaction platforms, enabling IFIT3 to simultaneously bind to multiple signaling molecules. The positively charged regions on the protein surface form RNA binding grooves, mediating its recognition of viral RNA. The C-terminal superhelical domain participates in homodimerization and heterodimerization with IFIT1/IFIT2, while the N-terminal variable region is responsible for binding to immune molecules such as TBK1 and RIG-I, jointly constituting the structural basis for regulating antiviral signal transduction.

Fig. 1 The role of IFIT3 in tumor immunity and the tumor microenvironment (TME).¹

Key structural features of IFIT3:

• Helix-turn-turn fold formed by tandem TPR motifs
• Positive-charged RNA binding groove
• Multiple protein interaction interfaces
• N-terminal and C-terminal functional domains coordinating immune signal transduction

Functions of IFIT3

The main function of IFIT3 is to regulate innate immune responses and viral defense. However, it is also involved in various physiological and pathological processes, including inflammatory responses, tumor progression, and regulation of cell proliferation.

IFIT3 integrates antiviral signals and inflammatory responses through its multi-protein interaction network mediated by the TPR domain. Changes in its expression level are closely related to viral infection, autoimmune diseases, and the prognosis of various cancers.

Applications of IFIT3 and IFIT3 Antibody in Literature

1. Wu, Rihan, Hao Yang, and Chunlei Liu. "IFIT3: a crucial mediator in innate immunity and tumor progression with therapeutic implications." Frontiers in Immunology 16 (2025): 1515718. https://doi.org/10.3389/fimmu.2025.1515718

The article indicates that the interferon-induced protein IFIT3 has dual functions of antiviral and tumor regulation. It regulates immunity through the interferon signal, RIG-I-like receptors, and NF-κB pathways, and affects the tumor microenvironment and immune evasion. As a new target for cancer immunotherapy, IFIT3 has significant clinical translational potential.

2. Sullivan, Owen M., et al. "IFIT3 RNA-binding activity promotes influenza A virus infection and translation efficiency." Journal of Virology 99.7 (2025): e00286-25. https://doi.org/10.1128/jvi.00286-25

The research has found that IFIT3 can directly bind to RNA and promote the expression and translation of the influenza A virus genes. The RNA binding site is composed of conserved amino acids. After mutation, the virus-promoting ability decreases, but it does not affect protein dimerization, revealing the key mechanism by which IFIT3 regulates viral infection.

3. Huang, Xiangyang, et al. "IFIT3 mediates TBK1 phosphorylation to promote activation of pDCs and exacerbate systemic sclerosis in mice." Clinical and Translational Medicine 14.9 (2024): e1800. https://doi.org/10.1002/ctm2.1800

The study found that the IFIT3/TBK1 signaling pathway is involved in the pathogenesis of scleroderma (SSc) by activating plasmacytoid dendritic cells (pDCs). Intervening in this pathway can inhibit the activation of pDCs and the release of cytokines. The IFIT3 knockout mouse model showed that targeting this pathway can alleviate skin and lung fibrosis, providing a new target for the treatment of SSc.

4. Li, Heng, et al. "UBE2O reduces the effectiveness of interferon-α via degradation of IFIT3 in hepatocellular carcinoma." Cell Death & Disease 14.12 (2023): 854. https://doi.org/10.1038/s41419-023-06369-9

The study found that UBE2O inhibits the efficacy of interferon-α by promoting the ubiquitination and degradation of IFIT3. Inhibiting UBE2O can upregulate the expression of IFIT3 and enhance interferon sensitivity. The K236 site of IFIT3 is a key ubiquitination modification site. Arsenic trioxide (ATO) can increase the level of IFIT3 by inhibiting UBE2O, providing a new strategy for enhancing interferon therapy.

5. Xu, Siyi, et al. "IFIT3 is increased in serum from patients with chronic hepatitis B virus (HBV) infection and promotes the anti-HBV effect of interferon alpha via JAK-STAT2 in vitro." Microbiology spectrum 10.6 (2022): e01557-22. https://doi.org/10.1128/spectrum.01557-22

The study found that IFIT3 enhances the antiviral effect of interferon-α against hepatitis B virus through the JAK-STAT pathway. IFIT3 promotes the phosphorylation of STAT2, upregulates the expression of ISGs, and inhibits the levels of hepatitis B surface antigen, e antigen and viral DNA. A decrease in IFIT3 expression weakens the efficacy of interferon, suggesting that it could be a potential target for the treatment of chronic hepatitis B.

Creative Biolabs: IFIT3 Antibodies for Research

Creative Biolabs specializes in the production of high-quality IFIT3 antibodies for research and industrial applications. Our portfolio includes monoclonal and polyclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom IFIT3 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 IFIT3 antibodies, custom preparations, or technical support, contact us at email.