Anti-MMP3 Antibody Picoband® Fluoro647 Conjugated

Stromelysin-1, also known as matrix metalloproteinase-3 (MMP-3), is an enzyme that in humans is encoded by the MMP3 gene. It is mapped to 11q22.2. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix and during tissue remodeling in normal physiological processes, such as embryonic development and reproduction, as well as in disease processes, such as arthritis, and tumour metastasis. The MMP-3 enzyme degrades collagen types II, III, IV, IX, and X, proteoglycans, fibronectin, laminin, and elastin. In addition, MMP-3 can also activate other MMPs such as MMP-1, MMP-7, and MMP-9, rendering MMP-3 crucial in connective tissue remodeling. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation.

A synthetic peptide corresponding to a sequence at the C-terminal of human MMP3, different from the related mouse sequence by seven amino acids, and from the related rat sequence by ten amino acids.

Angiogenesis, Atherosclerosis, Cancer, Cardiovascular, Cell Biology, Cytoskeleton/ECM, ECM Enzymes, Extracellular Matrix, Invasion/Microenvironment, Metalloprotease, Proteolysis/Ubiquitin, Proteolytic Enzymes, Signal Transduction, Tumor Biomarkers

Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.

1. Entrez Gene: MMP3 matrix metallopeptidase 3 (stromelysin 1, progelatinase) 2. Lu, P. C.-S., Ye, H., Maeda, M., Azar, D. T. Immunolocalization and gene expression of matrilysin during corneal wound healing. Invest. Ophthal. Vis. Sci. 40: 20-27, 1999. 3. Ye S, Eriksson P, Hamsten A, Kurkinen M, Humphries SE, Henney AM (May 1996) . Progression of coronary atherosclerosis is associated with a common genetic variant of the human stromelysin-1 promoter which results in reduced gene expression. J. Biol. Chem. 271 (22) : 13055–60.