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Human Polyclonal MMP14 Primary Antibody for IHC (p), WB - ABIN3044302
Jin, Jiang, Yang, Zhang, Yang, Zhang, Li, Yang, Ma: Acipimox attenuates atherosclerosis and enhances plaque stability in ApoE-deficient mice fed a palmitate-rich diet. in Biochemical and biophysical research communications 2012
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Human Polyclonal MMP14 Primary Antibody for IHC (fro), IHC (p) - ABIN4886668
Jiang, Jin, Li, Zhang, Yang, Yang, Li, Yang, Ma: Intermittent hypobaric hypoxia promotes atherosclerotic plaque instability in ApoE-deficient mice. in High altitude medicine & biology 2013
Show all 6 Pubmed References
Human Polyclonal MMP14 Primary Antibody for WB - ABIN3043408
Xiao, Li, Yu, Xiao, Hu, Tang, Zeng, He, Zeng, Ye, Xu: MicroRNA-10b promotes migration and invasion through KLF4 and HOXD10 in human bladder cancer. in Oncology reports 2014
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Human Monoclonal MMP14 Primary Antibody for CyTOF, FACS - ABIN4899219
Mierke, Bretz, Altevogt: Contractile forces contribute to increased glycosylphosphatidylinositol-anchored receptor CD24-facilitated cancer cell invasion. in The Journal of biological chemistry 2011
Show all 4 Pubmed References
Human Polyclonal MMP14 Primary Antibody for CyTOF, FACS - ABIN4900817
Gkantidis, Blumer, Katsaros, Graf, Chiquet: Site-specific expression of gelatinolytic activity during morphogenesis of the secondary palate in the mouse embryo. in PLoS ONE 2012
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Human Polyclonal MMP14 Primary Antibody for FACS, IHC (p) - ABIN390138
Will, Hinzmann: cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment. in European journal of biochemistry / FEBS 1995
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Human Polyclonal MMP14 Primary Antibody for WB - ABIN1881546
Sakr, Takino, Domoto, Nakano, Wong, Sasaki, Nakanuma, Sato: GI24 enhances tumor invasiveness by regulating cell surface membrane-type 1 matrix metalloproteinase. in Cancer science 2010
Human Monoclonal MMP14 Primary Antibody for FACS - ABIN4895758
Sathyamoorthy, Tezera, Walker, Brilha, Saraiva, Mauri, Wilkinson, Friedland, Elkington: Membrane Type 1 Matrix Metalloproteinase Regulates Monocyte Migration and Collagen Destruction in Tuberculosis. in Journal of immunology (Baltimore, Md. : 1950) 2015
Human Monoclonal MMP14 Primary Antibody for FACS - ABIN4895756
Loskutov, Kozyulina, Kozyreva, Ice, Jones, Roston, Smolkin, Ivanov, Wysolmerski, Pugacheva: NEDD9/Arf6-dependent endocytic trafficking of matrix metalloproteinase 14: a novel mechanism for blocking mesenchymal cell invasion and metastasis of breast cancer. in Oncogene 2015
MMP14 rs1042703 was associated with nominally shorter time to progression in malignant mesothelioma patients.
analysis of MT1-MMP structure and proteolytic activity
In squamous cell carcinoma of the cervix (SCCC), higher levels of MMP-14 expression were established in tumor cells, as evidenced by IHC (+3) and RT-PCR.Furin activity in the tumor was much higher than that in normal tissues. The expression of TIMP-2 (show TIMP2 Antibodies) mRNA was sufficiently obvious in both the tumor and normal tissues to the bottom of the uterine cavity.
MMP-14 is regulated by a cascade of IL-6 (show IL6 Antibodies) and p53 (show TP53 Antibodies), demonstrating that the tumor microenvironment directly stimulates molecular changes in cancer cells to drive an invasive phenotype
cytomembrane MMP14 was induced by IL-6 (show IL6 Antibodies) secreted from astrocytes, thereby enhancing the migration and invasion of glioma cells through activation of MMP2 (show MMP2 Antibodies)
MMP-14 levels decrease in lungs from endotoxemic mice and serum from septic patients. * Mmp14 (-/-) mice show increased lung injury and mortality following endotoxemia. * Absence of Mmp14 decreases activated MMP-2 (show MMP2 Antibodies) and increases S100A9 (show S100A9 Antibodies) levels in lung tissue. * MMP-14 ameliorates inflammation by promoting S100A9 (show S100A9 Antibodies) cleavage by activated MMP-2 (show MMP2 Antibodies).
In turn, LIMK1 (show LIMK1 Antibodies) and LIMK2 (show LIMK2 Antibodies) are required for MT1-MMP-dependent matrix degradation and cell invasion in a three-dimensional type I collagen environment.
miR (show MLXIP Antibodies)-337-3p directly binds to the MMP-14 promoter to repress MZF1 (show ZFP42 Antibodies)-facilitatd MMP-14 expression, thus suppressing the progression of gastric cancer
CCN3 (Nov (show NOV Antibodies)) and CCN5 (WISP2 (show WISP2 Antibodies)) are novel substrates of MMP14.
The current data support MT1-MMP as an additional ILK (show ILK Antibodies) substrate and show that modulation of ILK (show ILK Antibodies) expression and activity inhibit MT1-MMP-related pro-metastatic behaviors of ovarian cancer cells.
MT1-MMP expressed by vascular smooth muscle cells plays a key role in limiting the progression of atherosclerosis in APOE (show APOE Antibodies)-null mice by regulating proliferative responses and inhibiting the deterioration of VSMC function in atherogenic vascular walls.
Study documents that MT1-MMP is widely expressed in the tooth and surrounding connective tissues during development and postnatal growth. Consistent with this expression, loss of MT1-MMP in mice impairs tooth root formation and eruption in association with multiple defects in dentoalveolar tissues.
Authors demonstrate that CAIX (show CA9 Antibodies) associates with MMP14 through potential phosphorylation residues within its intracellular domain, and that CAIX (show CA9 Antibodies) enhances MMP14-mediated collagen degradation by directly contributing hydrogen ions required for MMP14 catalytic activity.
High mmp14 expression is associated with Lung Metastasis of Breast Cancer.
Although neither proteinase is required for branching morphogenesis, transcriptome profiling reveals a key role for MMP14 and MMP15 (show MMP15 Antibodies) in regulating mammary gland adipocyte differentiation. Whereas MMP14 promotes the generation of white fat depots crucial for energy storage, MMP15 (show MMP15 Antibodies) differentially controls the formation of thermogenic brown fat.
The authors identified the membrane-tethered matrix metalloprotease (show ADAMTS7 Antibodies) MT1-MMP as a prominent host-extracellular matrix-remodeling collagenase in influenza infection.
MMP-14 expression in fibroblasts plays a crucial role in collagen remodeling in adult skin and largely contributes to dermal homeostasis underlying its pathogenic role in fibrotic skin disease in a mouse model
MT1-MMP directly cleaves LYVE-1 (show LYVE1 Antibodies) on lymphatic endothelial cells to inhibit LYVE-1 (show LYVE1 Antibodies)-mediated lymphangiogenic responses and restrains the production of VEGF-C (show VEGFC Antibodies).
The authors propose a model for cell-regulated collagen fibril assembly during tendon development in which MMP14 cleaves a molecular bridge tethering collagen fibrils to the plasma membrane of fibripositors.
results suggest that ET-1 (show EDN1 Antibodies)-induced activation of proMMP-2 is mediated via cross-talk between NADPH oxidase (show NOX1 Antibodies)-PKCalpha (show PKCa Antibodies)-p(38)MAPK (show MAPK1 Antibodies) and NFkappaB-MT1MMP signaling pathways along with a marked decrease in TIMP-2 (show TIMP2 Antibodies) expression in the cells
Data indicate the involvement of PKC-alpha (show PKCa Antibodies) in proMMP-2 activation and inhibition of TIMP-2 (show TIMP2 Antibodies) expression by NF-kappaB (show NFKB1 Antibodies)-MT1-MMP-dependent and -independent pathway.
Data suggest that EMMPRIN derived from endometrial epithelial cells regulates expression of matrix metalloproteinases (MMP-2 (show MMP2 Antibodies); MMP-14) in endometrial stromal cells; expression of stromal MMPs is significantly higher in coculture with epithelial cells.
MMP-14, MMP-2 (show MMP2 Antibodies) and TIMP-2 (show TIMP2 Antibodies) are co-localized in the fetal compartment and therefore could influence the timely release of fetal membranes in cattle.
Results describe distinct changes in expression of MMP2 (show MMP2 Antibodies), MMP14, and the metallopeptidase (show ECEL1 Antibodies) inhibitor TIMP2 (show TIMP2 Antibodies) between different phases of the estrous cycle indicating an endocrine regulation.
EMMPRIN from the luminal epithelium may regulate the expression of stromal MMP-2 (show MMP2 Antibodies) and MMP-14 suggesting a role in adhesion and fusion of embryo to luminal epithelium.
MT1-MMP seems to act by inducing tissue remodeling in cartilage
sphingosine 1-phosphate is the predominant serum factor essential for MT1-MMP-dependent migration and morphogenic differentiation of vascular endothelial cells
MT1-MMP plays a crucial role in RAGE (show AGER Antibodies)-activated NADPH oxidase (show NOX1 Antibodies)-dependent signaling pathways.
MMP-1 (show MMP1 Antibodies) was involved in osteoarthritis development in rabbit ACLT model and the amount of its expression was related with the degree of cartilage degradation.
Modulation of MT1-MMP activity and microRNA-133a exportation into the myocardial interstitium occurred in the setting of acute myocardial ischemia-reperfusion.
A heterogeneous response in MT1-MMP activity likely contributes to regional dysfunction with ischemia-reperfusion. Subsequent I/R activates a proteolytic cascade within the MI region, contributing to continued adverse remodeling.
PI3K-dependent regulation of MT1-MMP protein synthesis and subsequent activation of latent MMP-2 (show MMP2 Antibodies) as critical events in neointimal hyperplasia after vascular injury.
Induction of endogenous MMP-14 gene and coexpression of SAF-1 (show MAZ Antibodies) & MMP-14 in the macrophages present in the atherosclerotic plaque implicate SAF-1 (show MAZ Antibodies) as a key regulator of MMP-14 gene induction in macrophage cells.
In an isolated left ventricular myocyte ischemia/reperfusion model, hypoxia induced a >70% increase in MT1-MMP abundance in myocytes. Confocal microscopy revealed MT1-MMP internalization during this time & reemergence to the membrane with reperfusion.
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily\; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. This protein activates MMP2 protein, and this activity may be involved in tumor invasion.
matric metalloproteinase 14
, matrix metalloproteinase-14
, membrane type 1 metalloprotease
, membrane-type-1 matrix metalloproteinase
, MT-MMP 1
, Membrane type 1-MMP
, matrix metalloproteinase 14 (membrane-inserted)
, membrane-type matrix metalloproteinase 1
, type 1 matrix metalloprotease 14
, matrix metalloproteinase 14 membrane-inserted
, matrix metalloproteinase 14, membrane-inserted
, membrane type 1-matrix metalloproteinase
, matrix metalloproteinase 14 preproprotein
, matrix metallopeptidase 1 (interstitial collagenase)
, matrix metalloproteinase 14
, membrane type 1 metalloproteinase
, membrane-type 1 matrix metalloproteinase
, membrane type-1 metalloproteinase