IRF7 Antibodies

Structure of IRF7

The molecular weight of the protein encoded by the IRF7 gene is approximately 55 kDa, and its specific value may fluctuate slightly due to post-translational modifications (such as phosphorylation) and subtype differences. This protein is a transcription factor composed of approximately 450-500 amino acids. Its structural features include the following key parts: its N-terminal has a highly conserved DNA-binding domain (DBD), which uses a helical - turning - helical motif and is responsible for recognizing and binding to interferon-stimulated response elements (ISRE). The C-terminal contains an important protein-protein interaction domain, namely the IRF-associated domain (IAD), which mediates the formation of homologous or heterodimers between IRF7 and other transcription factors (such as IRF3) or coactivators, which is crucial for its nuclear translocation and the initiation of target gene transcription. The active center of the protein contains multiple serine/threonine sites that can be phosphorylated by kinases such as TBK1 and IKKε. Phosphorylation is a key regulatory switch that triggers conformational changes, dimerization, nuclear localization, and ultimately activates the expression of downstream interferon genes.

Fig. 1 Diagrams of the IRF7 isoform domains.¹

Key structural properties of IRF7:

• Contains the typical helix-turn-helix DNA-binding domain
• Irf-associated domains with the ability to mediate protein interactions
• Contains key serine phosphorylation sites for regulatory activity

Functions of IRF7

The core function of the IRF7 gene is to act as the main regulatory factor of the innate immune response, coordinating the body's defense against viral invasion. Its specific functions include:

Unlike many constructively expressed immune factors, IRF7 is usually expressed at a low level in resting cells, and its activity strictly depends on the activation of virus-induced signaling pathways (such as TLR or RIG-I pathways). This regulatory characteristic makes it a key "switch" for rapid and specific antiviral responses.

Applications of IRF7 and IRF7 Antibody in Literature

1. Ma, Wei, et al. "IRF7: role and regulation in immunity and autoimmunity." Frontiers in immunology 14 (2023): 1236923. https://doi.org/10.3389/fimmu.2023.1236923 

The article indicates that IRF7 is a member of the interferon regulatory factor family and was initially identified as a key transcriptional regulator of type I interferons, playing a core role in innate immunity. Recent studies have found that IRF7 has diverse functions and is widely involved in various biological processes such as immune regulation and autoimmune diseases. Its mechanism of action involves multiple levels including signal transduction, transcriptional translation, and post-translational modification.

2. Zhan, Ting, et al. "Single‐cell sequencing combined with spatial transcriptomics reveals that the IRF7 gene in M1 macrophages inhibits the occurrence of pancreatic cancer by regulating lipid metabolism‐related mechanisms." Clinical and Translational Medicine 14.8 (2024): e1799. https://doi.org/10.1002/ctm2.1799

This study reveals that IRF7 of M1-type macrophages in pancreatic cancer tissues can inhibit the transcription of RPS18, reduce the delivery of RPS18 by exosomes, and thereby down-regulate the expression of ILF3 within cancer cells. The IRF7/RPS18 axis inhibits lipid metabolism, proliferation and migration of cancer cells and promotes apoptosis, providing a new target for immunotherapy of pancreatic cancer.

3. Li, Zhikun, et al. "IRF7 inhibits the Warburg effect via transcriptional suppression of PKM2 in osteosarcoma." International Journal of Biological Sciences 18.1 (2022): 30. https://doi.org/10.7150/ijbs.65255 

Studies have shown that interferon regulatory factor 7 (IRF7) is lowly expressed in osteosarcoma, and its high expression is associated with a good prognosis. IRF7 inhibits the growth of osteosarcoma by directly transcriptional inhibiting the key glycolytic gene PKM2, thereby hindering aerobic glycolysis in tumor cells. This discovery reveals a new mechanism by which IRF7 regulates tumor metabolism, suggesting it as a potential therapeutic target.

4. Mayuramart, Oraphan, et al. "IRF7-deficient MDCK cell based on CRISPR/Cas9 technology for enhancing influenza virus replication and improving vaccine production." PeerJ 10 (2022): e13989. https://doi.org/10.7717/peerj.13989 

Researchers used CRISPR/Cas9 to knockout the IRF7 gene in MDCK cells, significantly reducing the interferon response of the cells. The results indicated that IRF7-deficient cells could generate higher viral titers after influenza virus infection, providing a new strategy for the efficient production of cell-based influenza vaccines.

5. Simons, Karin H., et al. "IRF3 and IRF7 mediate neovascularization via inflammatory cytokines." Journal of cellular and molecular medicine 23.6 (2019): 3888-3896. https://doi.org/10.1111/jcmm.14247  

By constructing a mouse model of lower extremity ischemia, the study found that deficiencies in IRF3 and IRF7 would significantly delay postoperative blood flow recovery. The mechanism lies in that the deletion of IRF3/IRF7 weakens the inflammatory response and the expression of pro-angiogenic factors in ischemic tissues, thereby inhibiting the formation of new blood vessels, indicating that IRF3/IRF7 is a key factor in regulating angiogenesis after ischemia.

Creative Biolabs: IRF7 Antibodies for Research

Creative Biolabs specializes in the production of high-quality IRF7 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom IRF7 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 IRF7 antibodies, custom preparations, or technical support, contact us at email.