ADAMTS-1, also known as METH-1, was first described as a protein elevated in invasive mouse tumors. Initial observations indicated a role for ADAMTS-1 in tumor progression, since the protein was preferentially expressed in more invasive tumor cell lines. Induction of ADAMTS-1 by LPS in mouse suggested the possibility that ADAMTS-1 could be involved in inflammation. ADAMTS-1 is also elevated in ovulation, where the expression seems to be under hormonal regulation. ADAMTS-1 has also been implicated in arthritis, possibly due to the turnover of aggrecan. ADAMTS-1 was also identified in mouse heart and kidney, and the human ortholog, METH-1, was found in heart, kidney, adrenal gland, thymus, liver, and skeletal muscle. A knockout mouse lacking ADAMTS-1 was found to have numerous developmental defects. A member of the metalloproteinase family containing disintegrin-like domains (ADAMs), the function of ADAMTS-1 is still poorly understood. ADAMTS-1 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active, cleaving aggrecan. In addition to the metalloprotease domain, ADAMTS-1 has a propeptide domain, two Prohormone Convertase (PC, furin) cleavage sites, a cysteine-rich domain and three thrombospondin-1 like domains. The ADAMTS proteins do not have a transmembrane domain, unlike the ADAMs proteases, and are secreted proteins. ADAMTS-1 is thought to be preferentially secreted into the ECM, where it binds via the thrombospondin motifs to the ECM. The full length ADAMTS-1 sequence codes for a 967 amino acid protein, with a predicted mass of 105.383 kD, but glycosylation and the abundance of cysteine residues gives ADAMTS-1 a greater apparent molecular weight on reduced SDS PAGE gels. ADAMTS-1 is cleaved by furin or other prohormone convertases at one or both of the furin consensus sites in the amino portion of the molecule, producing the proteolytically active form. A second cleavage by a metalloproteinase is thought to yield a shed form of ADAMTS-1, releasing it from the ECM by cleavage between the first and second thrombospondin motifs. RP1-ADAMTS-1 recognizes the zymogen of ADAMTS-1, and the furin cleaved ADAMTS-1, but not the shed form. 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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