TGFBR2/TGF-beta RII Protein, Mouse (Biotinylated, HEK293, His-Avi)

The transmembrane serine/threonine kinase, TGFBR2 (TGF-beta RII), forms a non-promiscuous receptor complex with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, serving as the dedicated receptor for the TGF-beta cytokines TGFB1, TGFB2, and TGFB3. This receptor complex translates signals from the cell surface to the cytoplasm, orchestrating a wide range of physiological and pathological processes, such as cell cycle arrest, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression, and carcinogenesis. Upon binding of the cytokine dimer, composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically, TGFBR2 constitutively activates TGFBR1 through phosphorylation. The activated TGFBR1, in turn, phosphorylates SMAD2, leading to its dissociation from the receptor and subsequent interaction with SMAD4. The resulting SMAD2-SMAD4 complex translocates to the nucleus, where it modulates the transcription of TGF-beta-regulated genes, constituting the canonical SMAD-dependent TGF-beta signaling cascade. Additionally, TGFBR2 is involved in non-canonical, SMAD-independent TGF-beta signaling pathways. Overall, TGFBR2 exhibits transforming growth factor beta-activated receptor activity, playing a pivotal role in diverse cellular responses.