|Detection of MMP‑16/MT3‑MMP in PC‑3 Human Cell Line by Flow Cytometry. PC‑3 human prostate cancer cell line was stained with Mouse Anti-Human MMP‑16/MT3‑MMP APC‑conjugated Monoclonal Antibody (Catalog # FAB1785A, filled histogram) or isotype control antibody (Catalog # IC003A, open histogram). View our protocol for Staining Membrane-associated Proteins.|
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.
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