Transforming Growth Factor-Beta Receptor Type II/TGFBR2 (C-Fc) (recombinant mouse)

Protein Construction: Recombinant Mouse Transforming Growth Factor-beta Receptor Type II is produced by our Mammalian expression system and the target gene encoding Ile24-Asp184 is expressed with a Fc tag at the C-terminus. Sequence: Ile24-Asp184. Fusion tag: C-Fc Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 60-75 kDa. Protein function: Transforming growth factor-beta (TGF-beta) is an essential regulator in the processes of development, cell proliferation, and extracellular matrix deposition. TGF-beta regulates cellular processes by binding to three high-affinity cell surface receptors: TGF-beta receptor type I (TGF-beta-RI), TGF-beta receptor type II (TGF-beta-RII), and TGF-betabeta receptor type III (TGF-beta-RIII). TGF-beta RII is consists of a C-terminal protein kinase domain and an N-terminal ectodomain and belongs to transforming growth factor-beta (TGF-beta) receptor subfamily. TGF-beta RII has a protein kinase domain which can form a heterodimeric complex with another receptor protein and bind TGF-beta. This receptor/ligand complex phosphorylates protein will enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Protein function: Transmembrane serine/threonine kinase forming with the TGF- beta type I serine/threonine kinase receptor, TGFBR1, the non- promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. [The UniProt Consortium]