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A total of three members of the TGF beta family, TGFbeta1, TGFbeta2 and TGFbeta3, have been identified in mammals. Each is synthesized as a latent precursor that is subsequently cleaved forming the 112 amino acid growth factor which becomes active upon dimerization. TGFbetas mediate their activity by high affinity binding to the type II receptor 70kDa transmembrane protein with a cytoplasmic serine-threonine kinase domain.
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