Enzymes
Product List
MMP23B Human
Matrix Metallopeptidase 23B Human Recombinant
MMP28 Human
Matrix Metalloproteinase-28 Human Recombinant
MMP9 Rat
Matrix Metalloproteinase-9 Rat Recombinant
ProMatrilysin
ProMatrix Metalloproteinase-7 Recombinant
MMP1 Human, sf9
Matrix Metalloproteinase-1 Human Recombinant, sf9
MMP10 Human
Matrix Metallopeptidase 10 Human Recombinant
MMP14 Human
Matrix Metalloproteinase-14 Recombinant Human
This product consists of the human version of the enzyme MMP14, produced in a laboratory setting using E. coli bacteria. It is a single chain of 264 amino acids, without any sugar molecules attached (non-glycosylated), and has a molecular weight of 29.6 kDa. The purity of the MMP14 is ensured through specific chromatography techniques.
Escherichia Coli.
A clear, colorless solution that has been sterilized by filtration.
MMP14 Human, His
Matrix Metalloproteinase-14 Human Recombinant, His Tag
MMP2 Human
Matrix Metalloproteinase-2 Human Recombinant
Introduction
Matrix metalloproteinases (MMPs), also known as matrix metallopeptidases or matrixins, are a family of calcium-dependent zinc-containing endopeptidases. They belong to the larger metzincin superfamily of proteases . MMPs are classified based on their substrate specificity and domain structure into several groups: collagenases, gelatinases, stromelysins, matrilysins, and membrane-type MMPs (MT-MMPs) .
MMPs are known for their ability to degrade various components of the extracellular matrix (ECM), but they also play roles in regulating extracellular tissue signaling networks . They are expressed in various tissues and have distinct expression patterns. For instance, MMP-1 is found in fibroblasts, MMP-2 in endothelial cells, and MMP-9 in neutrophils . Their tissue distribution is broad, encompassing skin, lungs, heart, and other organs .
MMPs contribute to the homeostasis of many tissues and participate in several physiological processes, such as bone remodeling, angiogenesis, immunity, and wound healing . They play a crucial role in immune responses by regulating the release or activation of chemokines, cytokines, and growth factors . MMPs are also involved in pathogen recognition and host defense mechanisms .
MMPs interact with other molecules and cells through various mechanisms. They can be activated by chaotropic agents or by cleavage of the pro-peptide by other proteases . MMPs bind to specific substrates and degrade them, influencing cell behaviors such as migration, proliferation, and apoptosis . They also participate in downstream signaling cascades by modulating the availability of growth factors and cytokines .
The activity of MMPs is tightly regulated at multiple levels:
- Gene Expression: Transcription and mRNA stability are key regulatory points .
- Compartmentalization: This regulates the efficiency of proteolysis through cell surface recruitment and substrate availability .
- Pro-enzyme Activation: MMPs are synthesized as inactive zymogens and require activation .
- Inhibition: Tissue inhibitors of metalloproteinases (TIMPs) are endogenous inhibitors that regulate MMP activity .
MMPs have significant applications in biomedical research, serving as diagnostic tools and therapeutic targets. They are involved in the diagnosis and treatment of various diseases, including cancer, arthritis, and cardiovascular diseases . MMP inhibitors are being explored as potential therapeutic agents to modulate MMP activity in pathological conditions .
MMPs play essential roles throughout the life cycle, from development to aging and disease. During embryogenesis, they are involved in tissue remodeling and morphogenesis . In adulthood, MMPs contribute to tissue repair and maintenance . Dysregulation of MMP activity is associated with aging and various diseases, including cancer and fibrosis .
