A recombinant partial protein sequence (within amino acids 50-250) from the human protein was used as the immunogen for the TGF beta 3 antibody.
Transforming growth factor betas (TGF-betas) were originally discovered due to their ability to promote anchorage-independent growth of rat NRK fibroblasts in the presence of TGF-beta. TGF-beta 1, TGF-beta 2 and TGF-beta 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. TGF-beta 3 mediates many intercellular interactions that occur during embryonic development, cell differentiation and epithelial homeostasis. TGF-beta 3 overexpresses in extramammary Paget s disease (EPD) and downregulates in Bowen s disease, indicating that its expression is a useful indicator of tumor activity. TGF-beta 3 levels strongly correlate with IGF-1 and osteocalcin levels in serum. Significant amounts of TGF-beta 3 circulation appear to be representative of TGFbeta 3 expression in bone and may in part be derived from bone. Glucocorticoids may block TGF-beta production by modulating mRNA levels and c-Jun activity.
