Dimeric Cytokine Receptors
Native-like Structure. Bioactive Performance. Reliable Results.
Conigen’s recombinant cytokine receptors, including IFNγR1, IL10Rα, IFNαR1/R2, and IL-7Rα/TSLPR mimic native quaternary structures essential for signal transduction and immune regulation. These proteins enable accurate modeling of ligand-induced dimerization and receptor activation.
Cytokine receptors translate extracellular cytokine signals into intracellular responses. Lacking intrinsic kinase activity, they rely on dimerization to activate JAK-STAT and other signaling pathways. Preformed or ligand-induced dimerization drives immune activation, proliferation, and differentiation. Structural fidelity is key to preserving binding specificity and downstream signaling efficiency.
Conigen’s dimeric cytokine receptors support high-sensitivity assays, mechanistic studies, and therapeutic development across autoimmunity, cancer, and inflammation.
Spotlight: IFNαR1/R2
Bioactive Performance
IFNαR1 and IFNαR2 form a heterodimeric receptor complex that mediates type I interferon signaling. Conigen’s IFNαR1/R2 protein heterodimer mimics native structural integrity, showing significantly enhanced binding to type I interferon compared to monomeric forms.
Human IFNαR1/R2 heterodimer, His-Tag (CSP-24025-A1B1), IFNαR1 or IFNαR2 monomer binding to Type I interferon (IFN) as measured by ELISA. IFNαR1/R2 heterodimer significantly enhances the binding to IFN compared to each monomer. The IFN (0.2 μg/ml) was coated on 96-well microtiter plates and detected by serial dilutions of IFNαR heterodimer or monomers.
This structurally optimized IFNαR1/R2 complex provides a superior tool for interferon biology studies, antiviral research, and immunotherapy development.