Human MMP-16/MT3-MMP APC-conjugated Antibody

Matrix Metalloproteinase 16 (MMP-16), also known as MT3-MMP, is a 62-63 kDa member of the peptidase M10A family of enzymes (1,2). MMP-16 is found on capillary endothelial cells, cortical neurons cerebellar granule cells, granulosa lutein and theca lutein cells, and melanoma cells (3-6). MMP-16 has been shown to cleave proMMP-2 in a complex with chondroitin-4 sulfate (7). It also cleaves NgR1 and select matrix proteins (4). Notably, cleavage of MMP-14 inactivates this molecules, arresting cell migration (6). Structurally, proMMP-16 is 65-66 kDa in size and consists of the following domains: a pro domain containing the furin cleavage site, a catalytic domain containing the zinc-binding site, a hinge region, a hemopexin-like domain, a transmembrane domain, and a cytoplasmic tail (1). There is one soluble 47-48 kDa splice variant that retains proteolytic activity. Over amino acids (aa) 32-535, human and mouse MMP-16 share 98% amino acid sequence identity.