Purified by antigen-specific affinity chromatography.
Immunogen
Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of mouse ADAMTS-1(A disintegrin and metalloproteinase with thrombospondin motifs 1)
c3-c5 antibody, meth1 antibody, xadamts1 antibody, C3-C5 antibody, METH1 antibody, ADAM-TS1 antibody, ADAMTS antibody, ADAMTS-1 antibody, METH-1 antibody, adamts1 antibody, ADAM metallopeptidase with thrombospondin type 1 motif 1 antibody, ADAM metallopeptidase with thrombospondin type 1 motif, 1 antibody, a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 1 antibody, ADAM metallopeptidase with thrombospondin type 1 motif 1 L homeolog antibody, ADAMTS1 antibody, adamts1 antibody, Adamts1 antibody, adamts1.L antibody
Background
ADAM-TS1 (A disintegrin and metalloproteinase with thrombospondin motifs 1) cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. ADAM-TS1 has angiogenic inhibitor activity. Active metalloprotease may be associated with various inflammatory processes as well as development of cancer cachexia. ADAM-TS1 may play a critical role in follicular rupture. ADAM-TS1 cleaves aggrecan at the 1691-Glu-|-Leu1692 site, within the chondroitin sulfate attachment domain. It binds 1 zinc ion per subunit. ADAM-TS1 is a secreted protein and is associated with the extracellular matrix.It is induced in vitro in colon adenocarcinoma cells by interleukin-1, or in vivo in kidney and heart by lipopolysaccharide and it is also induced by LH stimulation in granulose cells of preovulatory follicles. The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. The precursor is cleaved by a furin endopeptidase. ADAM-TS1 contains 1 disintegrin domain, 1 peptidase M12B domain, and 3 TSP type-1 domains.