Human MMP-16/MT3-MMP Alexa Fluor® 488-conjugated Antibody

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FAB1785G-100UG
R&D Systems Antibodies
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Human MMP-16/MT3-MMP Alexa Fluor® 488-conjugated Antibody Summary

Species Reactivity
Human
Specificity
Detects human MMP-16/MT3-MMP in ELISAs. In direct ELISAs, no cross-reactivity with recombinant human MMP-14, -15, or -24 is observed.
Source
Monoclonal Mouse IgG2a Clone # 782005
Immunogen
Chinese hamster ovary cell line CHO-derived recombinant human MMP-16/MT3-MMP
Ala32-Pro535
Accession # P51512
Formulation
Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.
Label
Alexa Fluor 488 (Excitation= 488 nm, Emission= 515-545 nm)

Applications

Recommended Concentration
Sample
Flow Cytometry
0.25-1 µg/106 cells
PC‑3 human prostate cancer cell line

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.

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Preparation and Storage

Shipping
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Store the unopened product at 2 - 8 °C. Do not use past expiration date.

Background: MMP-16/MT3-MMP

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).

References
  1. Takino, T. et al. (1995) J. Biol. Chem. 270:23013.
  2. Shofuda, K. et al. (1997) J. Biol. Chem. 272:9749.
  3. Shimada, T. et al. (1999) Eur. J. Biochem. 262:907.
  4. Kang, T. et al. (2000) FASEB J. 14:2559.
  5. Lang, R. et al. (2004) J. Mol. Biol. 336:213.
Long Name
Matrix Metalloproteinase 16/Membrane Type 3 MMP
Entrez Gene IDs
4325 (Human)
Alternate Names
chromosome 8 open reading frame 57; DKFZp761D112; EC 3.4.24; EC 3.4.24.-; EC 3.4.24.80; matrix metallopeptidase 16 (membrane-inserted); matrix metalloproteinase 16 (membrane-inserted); matrix metalloproteinase-16; Membrane-type matrix metalloproteinase 3; Membrane-type-3 matrix metalloproteinase; MMP16; MMP-16; MMPX2; MMP-X2; MT3MMP; MT3-MMP; MT3-MMPC8orf57; MT-MMP 3; MT-MMP2; MTMMP3; MT-MMP3; Putative transmembrane protein C8orf57

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