TGFβ1/2/3 Anticuerpo(H-112): sc-7892

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Transforming growth factor betas (TGF∫s) were originally discovered due to their ability to promote anchorage-independent growth of rat NRK fibroblasts in the presence of TGFå. It is now realized that TGF∫s mediate many cell-cell interactions that occur during embryonic development. Three TGF∫s have been identified in mammals. TGF∫1, TGF∫2 and TGF∫3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecules. Biologically active TGF∫ requires dimerization of the monomers (usually homodimers) and release of the latent peptide portion. Overall, the mature region of the TGF∫3 protein has approximately 80% identity to the mature region of both TGF∫1 and TGF∫2. However, the NH2 terminals or precursor regions of their molecules share only 27% sequence identity.