Chordin

Chordin is a bone morphogenetic protein antagonist composed of four small cysteine-rich domains, whose function is not known. Chordin was originally identified in Xenopus laevis in the laboratory of Edward M. De Robertis as a key developmental protein that dorsalizes early vertebrate embryonic tissues. The polypeptide is 941 amino acids long and 120 kDa large and it dorsalizes the developing embryo by binding ventralizing TGFβ proteins such as bone morphogenetic proteins. It may also play a role in organogenesis. There are five named isoforms of this protein that are produced by alternative splicing.