Matrix Metalloproteinase-9 Mouse Recombinant
Recombinant mouse MMP9, expressed in Sf9 insect cells, is a single, glycosylated polypeptide chain. It comprises 717 amino acids (20-730 a.a.) and has a molecular weight of 79.3 kDa. The protein is engineered with a 6-amino acid Histidine tag at the C-terminus to facilitate purification, which is achieved using proprietary chromatographic methods.
Sf9, Baculovirus cells.
Matrix Metalloproteinase-1 Human Recombinant
Matrix Metalloproteinase-1 Human Recombinant, HEK
Matrix Metalloproteinase-13 Human Recombinant
Matrix Metalloproteinase-7 Human Recombinant
Matrix Metalloproteinase-7 Human Recombinant, Active
Recombinant Matrix Metalloproteinase-7, expressed in E. coli, is produced as a single, non-glycosylated polypeptide chain with a molecular weight of 19.13 kDa. The purification of MMP-7 is achieved through proprietary chromatographic methods.
Matrix Metalloproteinase-9 Human Recombinant, HEK
HEK293 Cells.
Matrix Metalloproteinase-9 Mouse Recombinant
Matrix Metalloproteinase-2 Human Recombinant, HEK
Matrix Metalloproteinase-2 Mouse Recombinant
MMP2 Mouse, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 644 amino acids (residues 30-662). It has a molecular weight of 72.4 kDa. The protein features a 6-amino acid Histidine tag fused to its C-terminus. Purification is achieved using proprietary chromatographic techniques.
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:
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 .