Pro-TGF-alpha Antibody detects enogenous levels TGF-alpha precusor protein but not mature TGF-alpha. It does not cross-react with other family members at physiological levels.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the amino-terminal sequence of TGF-alpha . Antibodies are purified by protein A and peptide affinity chromatography.
Background
Transforming growth factor alpha (TGF-alpha) is a member of the epidermal growth factor (EGF) family, sharing the same receptor, EGFR, and regulating cell proliferation, survival, and differention (1). Members of the family 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. TGF-alpha was initially discovered in the media of retrovirally transformed fibroblasts, and it name comes from its ability to induce transformation in cultured fibroblasts (2). This transforming activity was later shown to require TGF-beta, which potentiates the activity of TGF-alpha through a separate receptor (3). Soluble TGF-alpha is released from its membrane-bound precusor, pro-TGF-alpha, following protolytic cleavage, but the membrane bound precursor is still able to bind and activate EGFR (4). Binding of soluble or membrane bound TGF-alpha to EGFR leads to receptor dimerization, tyrosine autophosphorylation, and activation of downstream signaling components. TGF-alpha and related peptides play an important role in the progression of cancer as well as in neuropathological processes (5,6).