Application:IF
Reactivity: Human,Mouse,Rat
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, metastasis, and atherosclerosis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases.
MMP12 was first described in murine macrophages, later in human macrophages, and more recently in other cell types. Also known as metalloelastase, MMP12 is able to degrade elastin, entactin, laminin 1, fibronectin, type IV collagen as well as insulin B-chain and casein. MMP12 is often confused with the Serine proteinase, Leukocyte elastase (EC 3.4.21.37) because of similar nomenclature. MMP12 is structurally similar to the classical MMPs (MMP1, MMP3); it contains a propeptide with autoinhibitory cysteine switch site, a well-conserved zinc site, hinge region and hemopexin domain. MMP12 lacks a transmembrane domain and furin cleavage site. The zymogen for MMP-12 is about 54 kD, and is quickly activated to the 45 kD form; and this breaks down to cascade of active forms, ending with the common 22 kD form. Stimulated macrophages produce MMP12; it has also been found in osteosarcoma cells, synovial fibroblasts and lung fibroblasts.