MMP14 Human
Escherichia Coli.
Matrix Metallopeptidase 14, Matrix Metallopeptidase 14 (Membrane-Inserted), Membrane-Type-1 Matrix Metalloproteinase, Membrane Type 1 Metalloprotease, EC 3.4.24.80, MT-MMP 1, MT1-MMP, MMP-14, MMP-X1, MT1MMP, MTMMP1, Matrix Metalloproteinase 14 (Membrane-Inserted), Membrane-Type Matrix Metalloproteinase 1, Matrix Metalloproteinase-14, EC 3.4.24, MT-MMP, WNCHRS, Matrix metalloproteinase-14, Membrane-type matrix metalloproteinase 1.
Sterile filtered colorless solution.
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
Matrix Metalloproteinase-14 Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 264 amino acids and having a molecular mass of 29.6kDa.
MMP14 is purified by proprietary chromatographic techniques.
Product Specs
Matrix metalloproteinase-14 (MMP14), also known as membrane-type 1 matrix metalloproteinase (MT1-MMP), is a protein found on the surface of cells. It plays a crucial role in breaking down the structural components surrounding cells, known as the extracellular matrix (ECM). This breakdown is essential for various physiological processes, including tissue remodeling and wound healing. MMP14 is particularly active at the leading edge of invading cancer cells, where it contributes to tumor spread by degrading the ECM and facilitating tumor cell movement. Additionally, MMP14 activates other enzymes like MMP-2, further enhancing ECM degradation. It also modifies cell adhesion molecules like CD44 and integrin alpha V, influencing cell-cell and cell-ECM interactions. Due to its involvement in these processes, MMP14 is recognized as a key player in both normal physiological functions and disease states like cancer.
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.
A clear, colorless solution that has been sterilized by filtration.
The MMP14 solution is provided in a solution containing 20mM Tris-HCl at a pH of 7.4, 30% glycerol, 300mM NaCl, 3mM CaCl2, and 10µM ZnCl2. It is filtered through a 0.2 µm filter for sterilization.
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended periods, it should be stored frozen at -20°C. To ensure stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is recommended. Repeated freezing and thawing of the product should be avoided.
The purity of this product is greater than 95%, determined by two methods: RP-HPLC analysis and SDS-PAGE analysis.
Matrix Metallopeptidase 14, Matrix Metallopeptidase 14 (Membrane-Inserted), Membrane-Type-1 Matrix Metalloproteinase, Membrane Type 1 Metalloprotease, EC 3.4.24.80, MT-MMP 1, MT1-MMP, MMP-14, MMP-X1, MT1MMP, MTMMP1, Matrix Metalloproteinase 14 (Membrane-Inserted), Membrane-Type Matrix Metalloproteinase 1, Matrix Metalloproteinase-14, EC 3.4.24, MT-MMP, WNCHRS, Matrix metalloproteinase-14, Membrane-type matrix metalloproteinase 1.
Escherichia Coli.
ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYG.
Product Science Overview
MMP-14 is a transmembrane protein that contains a potential transmembrane domain, suggesting its expression at the cell surface rather than being secreted . The enzyme is synthesized as an inactive proenzyme and is activated when cleaved by extracellular proteinases . MMP-14 is known for its ability to degrade various ECM components, including collagen, and is essential for pericellular collagenolysis and the modeling of skeletal and extraskeletal connective tissues during development .
One of the key functions of MMP-14 is the activation of progelatinase A (MMP-2), which plays a significant role in cell growth and migration . MMP-14 is also involved in the formation of fibrovascular tissues in association with pro-MMP-2 . Additionally, MMP-14 has been implicated in the reorganization of the actin cytoskeleton by cleaving PTK7 and regulating Notch signaling by mediating the cleavage and inhibition of DLL1 .
Recombinant human MMP-14 is produced using recombinant DNA technology, where the MMP-14 gene is cloned into an expression vector and expressed in a suitable host system, such as E. coli . The recombinant protein is then purified using chromatographic techniques to obtain a high-purity product . This recombinant form of MMP-14 is used in various research applications to study its structure, function, and role in different biological processes.
MMP-14 has been associated with several diseases, including Winchester syndrome and multicentric osteolysis-nodulosis-arthropathy spectrum . Its role in activating MMP-2 and its involvement in tumor invasion make it a potential target for therapeutic interventions in cancer research . Understanding the function and regulation of MMP-14 is crucial for developing strategies to modulate its activity in various pathological conditions.
