Interleukin-3 receptor α (IL-3Rα) is the α subunit of the ligand-specific IL-3R and initiates intracellular signaling in response to IL-3. The binding of this protein to IL3 depends on the beta subunit. The beta subunit is activated by the ligand binding, and is required for the biological activities of IL3. IL-3 amplifies proinflammatory signaling and cytokine storm in murine sepsis models. In vitro, IL-3 stimulation promoted IL-3Rα proteasomal degradation dependent on RNFT2 (RING finger transmembrane-domain containing protein 2, also TMEM118), and we identified IL-3Rα lysine 357 as a ubiquitin acceptor site. Researches identify RNFT2 as a negative regulator of IL-3Rα and show a potential role for the RNFT2/IL-3Rα/IL-3 axis in regulating innate immune responses in the lung.
1μg (R: reducing condition, N: non-reducing condition).
The purity of IL-3R alpha/CD123 His Tag Protein, Canine is more than 95% determined by SEC-HPLC.