Transforming growth factor‐β (TGF‐β) type‐I and type‐II receptors form a ligand‐dependent heteromeric signalling complexes, in which transforming growth factor‐β receptor type II (TβRII) trends to act as the primary receptor. In the present study, we used a chimeric soluble type‐II receptor fused with the Fc regions of human immunoglobulin (TβRIIs‐Fc) in order to obtain a putative TGF‐β antagonist. Biochemical studies revealed that TβRIIs‐Fc shared the same properties as the wild‐type receptor. The TβRIIs‐Fc receptor displayed an affinity of 1370 ± 363 pM which was similar to those of the wild‐type TβRII when expressed alone in Cos‐1 cells (1122 ± 413 pM). Furthermore, the chimeric receptor showed the same selectivity for TGF‐β isoforms as the native receptor. Although both TGF‐β1 and TGF‐β3 were able to bind TβRIIs‐Fc, TGF‐β2 could not compete with the binding of TGF‐β1 to TβRIIs‐Fc. It was noted that this type of fused Fc receptor could be used in FlashPlate screening for potent agonism and antagonism of TGFβ. Moreover, biological activities of the chimeric receptor showed it to be a potent TGF‐β1‐antiproliferative and TGF‐β1‐extracellular matrix transcriptional inhibitor on responses in Mv1Lu cells. To conclude, our results clearly show that the TβRIIs‐Fc chimeric receptor could be used as a potent TGF‐β antagonist. These data raised the possibility that this TβRIIs‐Fc construct might act successfully as an antagonist of both TGF‐β1 and TGF‐β3 in vivo.