Anti-MMP2 Antibody Picoband®

Matrix metalloproteinase-2 (MMP2) is a Type IV collagenase, 72-kD, which is also known as gelatinase and is a member of a group of secreted zinc metalloproteases. The MMP2 gene is 17 kb long with 13 exons varying in size from 110 to 901 bp and 12 introns ranging from 175 to 4,350 bp, located within a region of human chromosome 16q13. In addition, the extra exons encode the amino acids of the fibronectin-like domain which has so far been found in only the 72- and 92-kDa type IV collagenase. MMP2, which has a critical role in the binding of progelatinase A and TIMP4 via the C-terminal hemopexin-like domain (C domain), is functionally associated on the surface of angiogenic blood vessels. Not only is a likely effector of endometrial menstrual breakdown, MMP2 is also effector and regulator of the inflammatory response. Moreover, MMP2 could be helpful in diagnosing Takayasu arteritis.

E. coli-derived human MMP2 recombinant protein (Position: K429-C660) . Human MMP2 shares 95.7% and 95.3% amino acid (aa) sequence identity with mouse and rat MMP2, respectively.

Angiogenesis, Cancer, Cancer Metabolism, Cardiovascular, Cell Biology, Extracellular Matrix, Invasion/Microenvironment, Metabolism, Metabolism Processes, Metalloprotease, Pathways and Processes, Proteolysis/Ubiquitin, Proteolytic Enzymes, Response To Hypoxia, Tumor Biomarkers

Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.

1. Collier, I. E.; Bruns, G. A. P.; Goldberg, G. I.; Gerhard, D. S. : On the structure and chromosome location of the 72- and 92-kDa human type IV collagenase genes. Genomics 9: 429-434, 1991. 2. Huhtala, P.; Chow, L. T.; Tryggvason, K. : Structure of the human type IV collagenase gene. J. Biol. Chem. 265: 11077-11082, 1990. 3. Irwin, J. C.; Kirk, D.; Gwatkin, R. B. L.; Navre, M.; Cannon, P.; Giudice, L. C. : Human endometrial matrix metalloproteinase-2, a putative menstrual proteinase: hormonal regulation in cultured stromal cells and messenger RNA expression during the menstrual cycle. J. Clin. Invest. 97: 438-447, 1996. 4. Nagase, H.; Barrett, A. J.; Woessner, J. F., Jr. : Nomenclature and glossary of the matrix metalloproteinases. Matrix Suppl. 1: 421-424, 1992.

Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.

Isoform 1: Secreted, extracellular space, extracellular matrix. Membrane. Nucleus. Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes.