TACE Antibody detects endogenous levels of TACE protein. Additional bands result from differential glycosylation.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to amino acids surrounding Val200 of human TACE. Antibodies are purified by Protein A and peptide affinity chromatography.
Background
TACE (TNF-α converting enzyme), also known as ADAM17, is a transmembrane metalloprotease that plays a key role in the cleavage of a number cell surface molecules in a process known as “shedding". TACE is abundantly expressed in many adult tissues, but in fetal development expression is differentially regulated (1). An important substrate of TACE is pro-TNF-α (1). Increased expression of TACE is associated with several pathological conditions including osteoarthritis and rheumatoid arthritis, where the pro-inflammatory effects of increased TNF-α contribute to disease pathogenesis (2,3). Regulation of other important molecules by TACE such as EGFR and Notch has recently been documented. TACE is responsible for the shedding of EGFR ligands such as amphiregulin and TNF-α. Some tumors have hyperactivated EGFR due to upregulated TNF-α production and upregulated TACE, making TACE a potential target for drug development (4). TACE activates Notch in a ligand-independent manner and has been shown to play a role in the development of the Drosophila nervous system (5). TACE has also been proposed to act as α-secretase for amyloid precursor protein (APP) (6), and to be involved in the renewal and proliferation of neural stem cells (7).