IFNAR1 Antibodies

Structure of IFNAR1

IFNAR1 is a transmembrane protein with a molecular weight of approximately 60 kDa. The exact value may vary slightly among different species due to glycosylation modifications and differences in amino acid sequences.

This protein is composed of approximately 557 amino acids. Its structural feature is that a single transmembrane region divides the molecule into an extracellular ligand-binding domain and an intracellular signal-transduction domain. The extracellular domain forms a rigid ligand-binding interface through multiple β-sheet structures, while the intracellular domain itself has no kinase activity, but contains conserved Box1/Box2 motifs, which are used to couple JAK kinases (mainly Tyk2), thereby initiating the phosphorylation and nuclear translocation signal cascade of downstream STAT proteins.

Fig. 1 Alignment of human IFNGR-1 with bovine and human IFNAR-1 sequences.¹

Key structural properties of IFNAR1:

• Multidomain extracellular region
• Single transmembrane helix
• Conservative intracellular motif
• No intrinsic kinase activity

Functions of IFNAR1

The core function of the IFNAR1 gene is to mediate the signal transduction of type I interferons, thereby activating the innate immune response of cells. Additionally, it is involved in regulating various physiological and pathological processes such as immune balance, cell proliferation, and differentiation.

Unlike many receptors with enzymatic activity, IFNAR1 itself does not possess catalytic function. Its signal transduction is entirely dependent on the cascade reaction with JAK kinases and STAT transcription factors, which reflects its characteristic as a crucial "hub" rather than an "effector" in the immune signaling network.

Applications of IFNAR1 and IFNAR1 Antibody in Literature

1. Cutrone, Elizabeth Cali, and Jerome A. Langer. "Identification of critical residues in bovine IFNAR-1 responsible for interferon binding." Journal of Biological Chemistry 276.20 (2001): 17140-17148. https://doi.org/10.1074/jbc.M009663200

The article indicates that type I interferon in humans functions through the IFNAR receptor, with the IFNAR-1 subunit playing a crucial role in binding specificity. The study utilized a more affinity-matched bovine IFNAR-1 model to identify five aromatic residues on its surface as forming the ligand binding site. This discovery is consistent with the functional studies of the human receptor and reveals a novel binding topological structure.

2. Wan, Qianya, et al. "PIM1 Attenuates Innate Immunity to Foster Coronavirus Replication through Ubiquitin Ligase β‐TrCP‐Mediated IFNAR1 Degradation." Advanced Science 12.37 (2025): e03487. https://doi.org/10.1002/advs.202503487

The research has found that the novel coronavirus HCoV-OC43 enhances the ubiquitination and degradation of the interferon receptor IFNAR1 by upregulating the host protein PIM1 kinase, thereby weakening the innate immunity. Inhibiting the activity of PIM1 can effectively block this process and suppress viral replication, providing a new target for the development of antiviral drugs.

3. Sun, Yimin, et al. "IFNAR1 gene mutation may contribute to developmental stuttering in the Chinese population." Hereditas 158.1 (2021): 46. https://doi.org/10.1186/s41065-021-00211-y

This study conducted whole-exome sequencing on families with speech disorders and for the first time discovered that variations in the IFNAR1 gene are associated with developmental stuttering. This gene mutation impairs the activity of the type I interferon signaling pathway, suggesting a potential pathogenic mechanism in the onset of stuttering.

4. Li, Huangcan, et al. "Secreted LRPAP1 binds and triggers IFNAR1 degradation to facilitate virus evasion from cellular innate immunity." Signal transduction and targeted therapy 8.1 (2023): 374. https://doi.org/10.1038/s41392-023-01630-1

The research has found that the proteases of the novel coronavirus SARS-CoV-2 and the enterovirus EV71 can upregulate the secretion of the LRPAP1 protein. This protein binds to and degrades the interferon receptor IFNAR1, thereby helping the virus evade the immune system. Inhibiting this pathway can stabilize IFNAR1 and effectively suppress various viruses.

5. Hussain, Timon, et al. "IFNAR1 deficiency impairs immunostimulatory properties of neutrophils in tumor-draining lymph nodes." Frontiers in immunology 13 (2022): 878959. https://doi.org/10.3389/fimmu.2022.878959

The research has found that in the lymph nodes draining head and neck cancer tumors, the absence of the function of type I interferon receptor IFNAR1 leads to the accumulation of neutrophils, but it will weaken their interaction with T cells and activation ability, thereby promoting tumor growth. Activating this pathway can enhance the immune stimulating function of neutrophils and inhibit tumors.

Creative Biolabs: IFNAR1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality IFNAR1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom IFNAR1 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 IFNAR1 antibodies, custom preparations, or technical support, contact us at email.