IRF3 Antibodies

Structure of IRF3

IRF3 is a medium-sized protein with a molecular weight of approximately 48.7 kDa. Its molecular weight is relatively conserved among different mammals, but there are certain interspecies differences.

This protein is composed of approximately 427 amino acids, and its primary structure forms multiple functional domains. The core of IRF3 is a highly conserved DNA-binding domain located at the N-terminal of the protein, which adopts a helical - turning - helical folding pattern and can specifically recognize interferon-stimulated response elements. The regulatory region at the C-terminal contains multiple serine residues. After phosphorylation, it can induce conformational changes in proteins, promote dimerization and nuclear translocation. The nuclear localization signal in the middle section of a protein is crucial for its entry into the nucleus to perform transcriptional functions, while the inhibitory domain at the C-terminal maintains the self-inhibitory state of the protein in the resting state.

Fig. 1 Structural representation of IRF3 monomer (A) or dimer (B).¹

Key structural properties of IRF3:

• Conserved DNA-binding domain that adopts a helix-turn-helix folding mode
• The regulatory region at the carboxyl terminal contains multiple phosphorylation sites
• Nuclear localization signals mediate its entry into the cell nucleus to exert its function

Functions of IRF3

The main function of IRF3 is to mediate signal transduction in the innate immune response. In addition, it is also involved in regulating various physiological and pathological processes such as apoptosis and inflammatory responses.

The signal activation of IRF3 exhibits typical "all or none" binary response characteristics, in contrast to the gradient response of pathways such as NF-κB, which enables it to act as a rapid molecular switch for viral infection and initiate an efficient antiviral state at the first moment.

Applications of IRF3 and IRF3 Antibody in Literature

1. Choi, Young-Ae, et al. "IRF3 activation in mast cells promotes FcεRI-mediated allergic inflammation." Cells 12.11 (2023): 1493. https://doi.org/10.3390/cells12111493

This study reveals the novel non-transcriptional functions of IRF3 in mast cell activation and allergic inflammation. IRF3 is activated by FcεRI signaling, influencing histidine decarboxylase (HDC) activity and particle maturation, and regulating allergic reactions.

2. Basak, Bristy, and Sachiko Akashi-Takamura. "IRF3 function and immunological gaps in sepsis." Frontiers in Immunology 15 (2024): 1336813. https://doi.org/10.3389/fimmu.2024.1336813

The article indicates that LPS triggers sepsis through TLR4/MD-2, and its signaling pathway is complex. Existing research focuses on the crucial role of IRF3 in this process, which not only affects the disease course but is also related to pathogen clearance mediated by the gut microbiota. Clarifying its mechanism will provide a new direction for reducing the mortality rate.

3. Liang, Du W, et al. "Helicobacter pylori promotes gastric intestinal metaplasia through activation of IRF3-mediated kynurenine pathway." Cell Communication and Signaling 21.1 (2023): 141. https://doi.org/10.1186/s12964-023-01162-9

This study reveals for the first time that Helicobacter pylori induces intestinal metaplasia of gastric mucosa by activating the cGAS-IRF3 signaling pathway, promoting the nuclear entry of IRF3 to drive the kynuurine metabolic pathway. Targeting this pathway can provide a new strategy for the prevention and treatment of this precancerous lesion.

4. Wang, Jian, et al. "Human OTUD6B positively regulates type I IFN antiviral innate immune responses by deubiquitinating and stabilizing IRF3." Mbio 14.5 (2023): e00332-23. https://doi.org/10.1128/mbio.00332-23

This study reveals that the deubiquitinating enzyme OTUD6B is a key positive regulatory factor of innate antiviral immunity. OTUD6B enhances the type I interferon signaling pathway and the host's antiviral ability by directly removing the ubiquitination modification of the K33 junction of IRF3, preventing its proteasome degradation.

5. Yu, Jae-Hyun, et al. "Hepatocyte GPCR signaling regulates IRF3 to control hepatic stellate cell transdifferentiation." Cell Communication and Signaling 22.1 (2024): 48. https://doi.org/10.1186/s12964-023-01416-6

This study reveals a new mechanism by which the GPCR-Gαs signaling axis directly phosphorylates IRF3 through the cAMP/PKA pathway, thereby promoting the expression of IL-33 in hepatocytes and ultimately driving the activation of hepatic stellate cells and liver fibrosis.

Creative Biolabs: IRF3 Antibodies for Research

Creative Biolabs specializes in the production of high-quality IRF3 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom IRF3 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 IRF3 antibodies, custom preparations, or technical support, contact us at email.