Human MMP-16/MT3-MMP Alexa Fluor® 488-conjugated Antibody Summary
Accession # P51512
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix (ECM). MMP-16 (MT3-MMP) is found in brain, lung, placenta, smooth muscle cells, and malignant tumor tissues including oral melanoma and renal carcinoma (1). MMP-16 has been shown to activate proMMP-2 and degrade various ECM components including native collagens (2, 3). MMP-16 has been proposed to possess the potential to directly enhance the growth and invasiveness of cells in vivo, two critical processes for development and carcinogenesis (4). Structurally, MMP-16 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 cytoplamasic tail (1). The structure of the catalytic domain in complex with a hydroxamate inhibitor has been solved (5).
- Takino, T. et al. (1995) J. Biol. Chem. 270:23013.
- Shofuda, K. et al. (1997) J. Biol. Chem. 272:9749.
- Shimada, T. et al. (1999) Eur. J. Biochem. 262:907.
- Kang, T. et al. (2000) FASEB J. 14:2559.
- Lang, R. et al. (2004) J. Mol. Biol. 336:213.
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