The TGFB1 gene is mapped to human chromosome 19q13.2 and codes for a 25 kDa peptide. TGF-ß1 polypeptide is produced as a precursor with hydrophobic signal sequence, pro-region and mature peptide. Cleavage of the precursor at tetrabasic cleavage site results in monomers of carboxy-terminal 112 amino acids. The biologically active form of Tgfb1 exists as a disulphide-linked homodimer.
TGF-β1 is a multifunctional peptide capable of influencing cell proliferation, differentiation, and other functions in a wide range of cell types. Transformed as well as non-neoplastic tissues release transforming growth factors and essentially all cells possess a specific TGF-β1 receptor. In general, cells of mesenchymal origin appear to be stimulated by TGF-β1; whereas, hepatocytes, T and B lymphocytes, keratinocytes, and many epithelial cells are inhibited by the peptide. TGF-β1 interacts with Epidermal Growth Factor (EGF), Platelet Derived Growth Factor (PDGF), Fibroblast Growth Factor (FGF), and T Cell Growth Factor (T-CGF) either by enhancing or antagonizing their characteristic actions. TGF-β1 plays a fundamental role in tissue growth and differentiation by involvement in adipogenesis, myogenesis, chondrogenesis, osteogenesis, epithelial cell differentiation, and immune cell function. TGF-β1 is associated with the developmental and metastasis of colorectal cancer.
Transforming growth factor-β1 (TGF-β1) is produced by many cell types, but is reported to be most concentrated in mammalian platelets, where it is present at approximately four times the level of TGF-β2.
HumanKine TGF-β1 is expressed in human HEK 293 cells as a mature, disulfide linked, non- glycosylated, homodimer with a predicted molecular mass of 25 kDa.