MMP‑16/MT3‑MMP was detected in immersion fixed paraffin-embedded sections of human breast using Goat Anti-Human MMP‑16/MT3‑MMP Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1785) at 15 µg/mL ...read more
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Reconstitute at 0.2 mg/mL in sterile PBS.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for MMP-16/MT3-MMP Antibody [Unconjugated]
chromosome 8 open reading frame 57
matrix metallopeptidase 16 (membrane-inserted)
matrix metalloproteinase 16 (membrane-inserted)
Membrane-type matrix metalloproteinase 3
Membrane-type-3 matrix metalloproteinase
Putative transmembrane protein C8orf57
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). The rhMMP-16PC consists of the pro and catalytic domains, which can be activated by treatment with furin.
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.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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