Enzymes
Product List
MMP-2 Human, HEK
Matrix Metalloproteinase-2 Human Recombinant, HEK
MMP-2 is purified by proprietary chromatographic techniques.
MMP2 Mouse
Matrix Metalloproteinase-2 Mouse Recombinant
MMP2 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 644 amino acids (30-662 aa) and having a molecular mass of 72.4kDa.
MMP2 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
MMP23B Human
Matrix Metallopeptidase 23B Human Recombinant
MMP23B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
MMP28 Human
Matrix Metalloproteinase-28 Human Recombinant
MMP9 Human, HEK
Matrix Metalloproteinase-9 Human Recombinant, HEK
MMP9 Human Recombinant is a single, glycosylated polypeptide chain containing 694 amino acids (20-707a.a) and having a molecular mass of 77.2kDa (calculated). MMP9 is fused to a 6 a.a His tag at C-terminal.
HEK293 Cells.
MMP9 Mouse
Matrix Metalloproteinase-9 Mouse Recombinant
MMP9 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (20-730 a.a) containing a total of 717 amino acids, having a molecular mass of 79.3kDa.
MMP9 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
MMP9 Rat
Matrix Metalloproteinase-9 Rat Recombinant
MMP9 Rat produced in HEK293 cells is a single, glycosylated polypeptide chain containing 695 amino acids (20-708 a.a.) and having a molecular mass of 77.2kDa. MMP9 is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
ProMatrilysin
ProMatrix Metalloproteinase-7 Recombinant
ProMMP 9 Human
Pro-Matrix Metalloproteinase-9 Human Recombinant
The Pro-MMP-9 is purified by proprietary chromatographic techniques.
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 .
