TGF-beta Receptor III Antibody

Transforming growth factor-beta (TGF-beta) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-4). TGF-beta elicits signaling through three cell surface receptors: type I (RI), type II (RII), and type III (RIII). Type I and type II receptors are serine/threonine kinases that form a heteromeric complex. In response to ligand binding, the type II receptors form a stable complex with the type I receptors allowing phosphorylation and activation of type I receptor kinases (5). The type III receptor, also known as betaglycan, is a transmembrane proteoglycan with a large extracellular domain that binds TGF-beta with high affinity but lacks a cytoplasmic signaling domain (6, 7). Expression of the type III receptor can regulate TGF-beta signaling through presentation of the ligand to the signaling complex. The only known direct TGF-beta signaling effectors are the Smad family proteins, which transduce signals from the cell surface directly to the nucleus to regulate target gene transcription (8, 9).

Q03167

A synthetic peptide of human TGFBR3

WB

93kDa