ADAM-17, also known as TNF-Convertase, or TACE, was first cloned from human epithelial cells. The ADAMs proteins are structurally similar, with a signal sequence, metalloprotease domain (inactive in some ADAMs), disintegrin domain, cystein-rich domain, EGF-like repeat, type-I transmembrane and Cytoplasmic domain. A member of the metalloproteinase family containing disintegrin-like domains (ADAMs), ADAM-17 is known to process the TNF- trimer from the membrane-attached precursor to the soluble form. ADAM-17 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active, cleaving TNF precursor as well as TNF p75 receptor, myeloid precursor protein, amyloid plaque protein, L-selectin and TGF-, making ADAM-17 a "sheddase." ADAM-17 contains a cleavage site for prohormone convertases (furin), and the majority of ADAM17 is secreted as activated enzyme, cleaved at the furin site. ADAM-17 is known to associate with MAD2 via the Cytoplasmic domain, implying cellular regulation pathways. ADAM-17 is expressed in a wide range of cells in culture. Three human ADAM-17 sequences encode proteins with different Cytoplasmic domains, as is the case for other ADAMs proteases. The 824 amino acid sequence encodes a 92,960 Dalton protein, the 807 AA sequence 91,003 Dalton, and the 694 AA sequence 78,543 Dalton predicted MW. Glycosylation and other post-translational modifications increase the apparent molecular weight on PAGE gels. Mouse and rat ADAM-17 sequences are both 827 AA, predicting 93,073 and 93,017 Dalton proteins, respectively. RP5-ADAM-17 recognizes a 120 kDa band in reduced Western blots of conditioned media or cell lysates, which is converted to a 55-60 kDa band. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species. EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen.

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