MMP-16/MT3-MMP Antibody (782005) [Alexa Fluor™ Plus 488]

• Reactivity: Hu
• Clone: 782005
• Clonality: Monoclonal
• Host: Mouse
• Conjugate: Alexa Fluor Plus 488

MMP-16/MT3-MMP Antibody (782005) [Alexa Fluor™ Plus 488] Summary

• 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.
• Isotype: IgG2a
• Clonality: Monoclonal
• Host: Mouse

Packaging, Storage & Formulations

• Storage: Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied
• Buffer: Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.

Notes

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™ Plus 488]

• 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

Background

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).

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.

Limitations

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.