MMP-16/MT3-MMP Antibody (782005) [Alexa Fluor® 488] Summary
Chinese hamster ovary cell line CHO-derived recombinant human MMP-16/MT3-MMP
Accession # P51512
Detects human MMP-16/MT3-MMP in ELISAs. In direct ELISAs, no cross-reactivity
with recombinant human MMP-14, -15, or -24 is observed.
Test in a species/application not listed above to receive a full credit towards a future purchase.
- Flow Cytometry 0.25-1 ug/10^6 cells
Flow Cytometry: Please use 0.25-1 ug of conjugated antibody per 10e6 cells.
Packaging, Storage & Formulations
Store the unopened product at 2 - 8 °C. Do not use past expiration date.
Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.
0.09% Sodium Azide
Please see the vial label for concentration. If unlisted please contact technical services.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for MMP-16/MT3-MMP Antibody (782005) [Alexa Fluor® 488]
- chromosome 8 open reading frame 57
- EC 3.4.24
- EC 3.4.24.-
- EC 220.127.116.11
- matrix metallopeptidase 16 (membrane-inserted)
- matrix metalloproteinase 16 (membrane-inserted)
- matrix metalloproteinase-16
- Membrane-type matrix metalloproteinase 3
- Membrane-type-3 matrix metalloproteinase
- MT-MMP 3
- 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).
- 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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