MMP-16/MT3-MMP Antibody [Alexa Fluor® 488]

• Reactivity: Hu
• Applications: WB, IHC, IP
• Clonality: Polyclonal
• Host: Goat
• Conjugate: Alexa Fluor 488

MMP-16/MT3-MMP Antibody [Alexa Fluor® 488] Summary

• Immunogen: E. coli-derived recombinant human MMP‑16/MT3‑MMP
  Ala32-Gly291 (Ile152Asn)
  Accession # P51512
• Specificity: Detects human MMP‑16/MT3‑MMP in direct ELISAs and Western blots.
• Isotype: IgG
• Clonality: Polyclonal
• Host: Goat
• Purity Statement: Antigen Affinity-purified

Applications/Dilutions

• Dilutions:
  • Immunohistochemistry
  • Immunoprecipitation
  • Western Blot

Packaging, Storage & Formulations

• Storage: Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied
• Buffer: Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% 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 [Alexa Fluor® 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). The rhMMP-16PC consists of the pro and catalytic domains, which can be activated by treatment with furin.

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.