ADAMTS-2, also known as Procollagen N-Proteinase (PNP), was first described in calf skin as a proteinase that processes the amino end of Type-I collagen. PNP message was found in skin, aorta, liver, tendon, bladder, retina and skeletal muscle. Later, PNP was found to be a member of a larger family of ADAMs metalloproteinases containing thrombospondin (TS) repeats. ADAMTS-2 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active, cleaving procollagen. In addition to the metalloprotease domain, ADAMTS-2 has a propeptide domain, a Prohormone Convertase (PC, furin) cleavage site, a cysteine-rich domain and three thrombospondin-1 like domains, followed by a unique C-terminal domain. ADAMTS-2 does not have a transmembrane domain, unlike many of the ADAMs proteases, and is a secreted protein, much of which binds to the ECM. ADAMTS-2 knockout mice develop fragile skin (similar to dermatospaxis), and male infertility. 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-2 sequence codes for a 1,211 amino acid protein (1,205 bovine), with a predicted mass is 134.722 kD, but glycosylation and the abundance of cysteine residues gives ADAMTS-2 a greater apparent molecular weight on reduced SDS PAGE gels. Purified ADAMTS-2 resolves at a lower molecular weight of 107 kD, due to cleavage at the furin site. RP2ADAMTS-2 recognizes the zymogen of ADAMTS-2 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 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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