Description
Product Characteristics: Matrix metalloproteinases (MMPs) are a family of at least 20 structurally related, zinc-containing enzymes that have the ability to brea kDaown connective tissue. MMP-3, also known as stomelysin-1 and transin, belongs to the stromelysin group of MMP's which also includes MMP-10. MMP-3 has shown direct and indirect substrate specificity to collagens III, IV, V and IX, gelatins, fibronectin, fibrinogen, plasminogen, proteoglycans, elastin, casein, entactin, myelin basic protein, IL-1b, serum amyloid A, TIMP-2, MMP-1, MMP-7, MMP-8, MMP-9, and MMP-13.
Target Information: Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]