ADAMTS-3 was first described in human brain, and is 61% identical to human ADAMTS-2. ADAMTS-3 message was found in placenta, cartilage, skin, lung, brain and heart. ADAMTS-3 was found to be a member of a larger family of ADAMs metalloproteinases containing thrombospondin (TS) repeats. ADAMTS-3 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active, cleaving procollagen-II. In addition to the metalloprotease domain, ADAMTS-3 has a propeptide domain, a Prohormone Convertase (PC, furin) cleavage site, a cysteine-rich domain and three thrombospondin-1 like domains, followed by a C-terminal domain unique to ADAMTS-2 and 3. ADAMTS-3 does not have a transmembrane domain, unlike many of the ADAMs proteases, and is a secreted protein, much of which binds to the ECM. Other ADAMs family members (ADAM-10, ADAM-17) have been more thoroughly studied, and are known to play key roles in inflammation, growth factor maturation and release, and a wide range of other functions. The full length ADAMTS-3 sequence codes for a 1,201 amino acid protein, with a predicted mass is 135.114 kD, but glycosylation and the abundance of cysteine residues gives ADAMTS-3 a greater apparent molecular weight on reduced SDS PAGE gels. Purified ADAMTS-3 resolves at a lower molecular weight of 108 kD, due to cleavage at the furin site. RP1ADAMTS-3 recognizes the zymogen of ADAMTS-3 at 140-130 kD in reduced Western blots, activated forms at 105-94 kD (major bands), and breakdown products at 50 kD, 34 kD in cell culture media and lysates. A strong band at about 53 kD is seen in media of some cell types, perhaps an alternative form. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 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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