• 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 IgG    _2A Clone # 782005

• Purification

  Protein A or G purified from hybridoma culture supernatant

• Immunogen

  Chinese hamster ovary cell line CHO-derived recombinant human MMP-16/MT3-MMP    
  Ala32-Pro535    
  Accession # P51512

• Formulation

  Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.

• Label

  Unconjugated

Applications

• Recommended    
  Concentration

  Sample

• Flow Cytometry

  2.5 µg/10    ⁶ cells

  See below

• 
  

• CyTOF-ready

  Ready to be labeled using established conjugation methods. No BSA or other carrier proteins that could interfere with conjugation.

• 
  

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Data Examples

Preparation and Storage

• Reconstitution

  Sterile PBS to a final concentration of 0.5 mg/mL.

• Shipping

  The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C

• Stability & Storage

  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.

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