|
|
MMP-7 |
Also Known As: MMP-7; MMP7; MPSL1; PUMP-1; matrin; matrix metalloproteinase 7;
matrix metalloproteinase 7 (matrilysin, uterine); uterine matrilysin;
matrix metallopeptidase 7 (matrilysin, uterine); matrix metalloproteinase 7;
mpsl1; matrix metallopeptidase 7 matrilysin uterine; and pump1
|
|
|
|
MMP-7 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. The enzyme encoded by this gene degrades proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. Predicted molecular weight of 28kDa. [provided by RefSeq]
Antibodies to MMP-7:
2D3 |
|
|
|
 |
|
|
|
|
|
