Anti-MMP2

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.

Lyophilized

2-8C. For long term -20C after reconstitution.

• 1. Nagase, H., Barrett, A. J., Woessner, J. F., Jr. : Nomenclature and glossary of the matrix metalloproteinases. Matrix Suppl. 1: 421-424, 1992.
• 2. 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.
• 3. Huhtala, P., Chow, L. T., Tryggvason, K. : Structure of the human type IV collagenase gene. J. Biol. Chem. 265: 11077-11082, 1990.
• 4. 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.

Immunogen affinity purified.