TGFA Human

TGF-α was initially discovered in the media of retrovirally transformed fibroblasts, and its name comes from its ability to induce transformation in cultured fibroblasts . The transforming activity of TGF-α was later shown to require TGF-beta, which potentiates the activity of TGF-α through a separate receptor . Members of the EGF family, including TGF-α, share an EGF-like domain of 45-60 amino acids characterized by the conservation of six regularly spaced cysteines, forming three disulfide bonds that function as their receptor binding domain .

Soluble TGF-α is released from its membrane-bound precursor, pro-TGF-α, following proteolytic cleavage. However, the membrane-bound precursor is still able to bind and activate EGFR . Binding of soluble or membrane-bound TGF-α to EGFR leads to receptor dimerization, tyrosine autophosphorylation, and activation of downstream signaling components . This signaling pathway is crucial for cell proliferation, differentiation, and development .

TGF-α and related peptides play an important role in the progression of cancer as well as in neuropathological processes . It is produced by monocytes, keratinocytes, and various tumor cells, and it stimulates the proliferation of a wide range of epidermal and epithelial cells . The development of TGF-α human recombinant using yeast expression systems has provided a valuable biopharmaceutical tool for therapeutic applications .

Recombinant human TGF-α is used in various research and therapeutic applications. It is supplied as a lyophilized material that is very stable at -20°C and can be reconstituted with sterile water for use in cell proliferation assays . The bioactivity of recombinant TGF-α is determined in cell proliferation assays, and it is used to study cell signaling pathways, cancer progression, and tissue repair mechanisms .