MMP-1 Products

Description

The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis. MMP1, also known as interstitial collagenase, is the only enzyme that is able to initiate the breakdown of the interstitial collagens, types I, II, and III.

Bioinformatics

Entrez	4312 Human
Product By Gene ID	4312
Alternate Names	CLGmatrix metalloprotease 1 CLGN EC 3.4.24 EC 3.4.24.7 Fibroblast collagenase interstitial collagenase matrix metallopeptidase 1 (interstitial collagenase) matrix metalloproteinase 1 (interstitial collagenase) Matrix metalloproteinase-1 MMP1 MMP-1

Research Areas for MMP-1

Find related products by research area and learn more about each of the different research areas below.

Angiogenesis
Cancer
Cell Biology
Cellular Markers
Extracellular Matrix