Go Back TGF-beta RII - Fc Chimera

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A DNA sequence encoding the signal peptide and extracellular domain of human TGF-beta receptor type II (aa 1-166) was fused to the Fc region of human IgG1 (aa 93-330). The chimeric protein was expressed in modified human 293 cells.

Transforming growth factor-beta (TGF-beta; TGF-b) is a pleiotropic cytokine that controls the growth, survival, motility and differentiation of cells. It is involved in the degradation and remodelling of the extracellular matrix (ECM), and has an important role in development during embryogenesis. TGF-beta is critical in wound healing as well as hematopoiesis, maintaining immune homeostasis by balancing lymphocyte proliferation and apoptosis. The biological effects of TGF-beta are mediated by binding to TGF-beta receptors; TGF-beta RI, TGF-beta RII (TGF-beta R2 ) , and TGF-beta RIII ( TGF-beta R3 ). TGF-beta initially binds to TGF-beta RII, which in turn complexes with TGF-beta RI. TGF-beta RII autophosphorylates and in turn phosphorylates serine residues on SMAD signaling proteins, activating the downstream intracellular signaling cascade through the cytoplasm and into the nucleus. TGF-beta RII is synthesized as a 567 amino acid protein including a 22 amino acid signal sequence, a 144 amino acid extracellular domain, a 21 amino acid transmembrane domain and a 380 amino acid cytoplasmic domain containing a Ser/Thr protein kinase. TGF-beta RII contains 3 N-linked glycosylation sites. For a recent review on TGF-beta signaling please refer to Feng XH & Derynck R (2005) Ann. Rev Cell Dev Biol. 21: 659-93.