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ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) is a family of secreted proteinases related to, but distinct from ADAM (a disintegrin and metalloproteinase) [1]. Presently eighteen family members have been identified in the human genome [2]. Mouse ADAMTS1 was first described by Kuno et al. [3] and the human orthologue was cloned by Vázques et al. [4]. ADAMTS1 consists of a prodomain, a metalloprotease domain, a thrombospondin (TSP) homologous domain with TSP type I motif, a spacer region and C-terminal TSP submotifs. The prodomain is cleaved off by a furin-type protease. There occurs additional processing at the C-terminal end [5].

ADAMTS1 has been found in human articular cartilage [6] and in neurons. The protein is induced by IL-1 [4].

ADAMTS1 displays antiangiogenic properties and inhibits endothelial cell proliferation [4]. ADAMTS1-null mice exhibit growth retardation and defects in morphology [7]. The active protease cleaves aggrecan at several sites [8] and versican [9]. ADAMTS1 activity is inhibited by metalloproteinase inhibitors TIMP 3 and TIMP 4 at higher concentrations [8] and by catechin gallate esters [10].