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anti-Human MMP14 Anticorps:
anti-Mouse (Murine) MMP14 Anticorps:
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Human Polyclonal MMP14 Primary Antibody pour WB - ABIN3043408
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. dans Biochemical and biophysical research communications 2012
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Human Polyclonal MMP14 Primary Antibody pour 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. dans High altitude medicine & biology 2013
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Human Polyclonal MMP14 Primary Antibody pour IHC (p), WB - ABIN3044302
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. dans Oncology reports 2014
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Human Monoclonal MMP14 Primary Antibody pour CyTOF, FACS - ABIN4899220
Mierke, Bretz, Altevogt: Contractile forces contribute to increased glycosylphosphatidylinositol-anchored receptor CD24-facilitated cancer cell invasion. dans The Journal of biological chemistry 2011
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Human Monoclonal MMP14 Primary Antibody pour CyTOF, FACS - ABIN4899219
Mierke, Frey, Fellner, Herrmann, Fabry: Integrin α5β1 facilitates cancer cell invasion through enhanced contractile forces. dans Journal of cell science 2011
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Human Polyclonal MMP14 Primary Antibody pour CyTOF, FACS - ABIN4900817
Gkantidis, Blumer, Katsaros, Graf, Chiquet: Site-specific expression of gelatinolytic activity during morphogenesis of the secondary palate in the mouse embryo. dans PLoS ONE 2012
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Human Monoclonal MMP14 Primary Antibody pour 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. dans Oncogene 2015
Human Monoclonal MMP14 Primary Antibody pour FACS - ABIN4895758
Sathyamoorthy, Tezera, Walker, Brilha, Saraiva, Mauri, Wilkinson, Friedland, Elkington: Membrane Type 1 Matrix Metalloproteinase Regulates Monocyte Migration and Collagen Destruction in Tuberculosis. dans Journal of immunology (Baltimore, Md. : 1950) 2015
Human Polyclonal MMP14 Primary Antibody pour WB - ABIN1881546
Sakr, Takino, Domoto, Nakano, Wong, Sasaki, Nakanuma, Sato: GI24 enhances tumor invasiveness by regulating cell surface membrane-type 1 matrix metalloproteinase. dans Cancer science 2010
Human Polyclonal MMP14 Primary Antibody pour FACS, IHC (p) - ABIN390138
Will, Hinzmann: cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment. dans European journal of biochemistry / FEBS 1995
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In turn, LIMK1 (Montrer LIMK1 Anticorps) and LIMK2 (Montrer LIMK2 Anticorps) are required for MT1-MMP-dependent matrix degradation and cell invasion in a three-dimensional type I collagen environment.
miR (Montrer MLXIP Anticorps)-337-3p directly binds to the MMP-14 promoter to repress MZF1 (Montrer ZFP42 Anticorps)-facilitatd MMP-14 expression, thus suppressing the progression of gastric cancer
CCN3 (Nov (Montrer NOV Anticorps)) and CCN5 (WISP2 (Montrer WISP2 Anticorps)) are novel substrates of MMP14.
The current data support MT1-MMP as an additional ILK (Montrer ILK Anticorps) substrate and show that modulation of ILK (Montrer ILK Anticorps) expression and activity inhibit MT1-MMP-related pro-metastatic behaviors of ovarian cancer cells.
Kinase activation led to increased MMP-2 (Montrer MMP2 Anticorps) and MT1-MMP expression and melanoma cell migration induced by hHK-1 (Montrer HOOK1 Anticorps). Thus, hHK-1 (Montrer HOOK1 Anticorps) and the NK1 receptor (Montrer TACR1 Anticorps) are critical to melanoma cell migration and each may be a promising chemotherapeutic target
Endoplasmic reticulum (ER) glycosylation of MMP14 is required for ECM (Montrer MMRN1 Anticorps) degradation and tumor growth.
Authors demonstrate that CAIX (Montrer CA9 Anticorps) associates with MMP14 through potential phosphorylation residues within its intracellular domain, and that CAIX (Montrer CA9 Anticorps) enhances MMP14-mediated collagen degradation by directly contributing hydrogen ions required for MMP14 catalytic activity.
developed a GNP-based, near-infrared fluorescent contrast agent that is highly specific for MMP-14 detection in breast tumor cell lines.
ERO1alpha plays a crucial role in HSC (Montrer FUT1 Anticorps) proliferation via posttranslational modification of collagen and MT1-MMP
MT1-MMP-expressing cells induced co-cultured non-MT1-MMP-expressing cells.
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.
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 (Montrer MMP15 Anticorps) in regulating mammary gland adipocyte differentiation. Whereas MMP14 promotes the generation of white fat depots crucial for energy storage, MMP15 (Montrer MMP15 Anticorps) differentially controls the formation of thermogenic brown fat.
The authors identified the membrane-tethered matrix metalloprotease (Montrer ADAMTS7 Anticorps) 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 (Montrer LYVE1 Anticorps) on lymphatic endothelial cells to inhibit LYVE-1 (Montrer LYVE1 Anticorps)-mediated lymphangiogenic responses and restrains the production of VEGF-C (Montrer VEGFC Anticorps).
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.
We demonstrate that MMP-14-mediated signaling in fetal hepatic progenitor cells promotes biliary luminal formation around the portal vein and negatively controls the maturation of hepatocytes.
Results show a reciprocal association between levels of heparanase (Montrer HPSE Anticorps) and MMP14, a membrane-bound MMP, shedding light on how branching occurs within developing mammary glands.
results suggest that ET-1 (Montrer EDN1 Anticorps)-induced activation of proMMP-2 is mediated via cross-talk between NADPH oxidase (Montrer NOX1 Anticorps)-PKCalpha (Montrer PKCa Anticorps)-p(38)MAPK (Montrer MAPK1 Anticorps) and NFkappaB-MT1MMP signaling pathways along with a marked decrease in TIMP-2 (Montrer TIMP2 Anticorps) expression in the cells
Data indicate the involvement of PKC-alpha (Montrer PKCa Anticorps) in proMMP-2 activation and inhibition of TIMP-2 (Montrer TIMP2 Anticorps) expression by NF-kappaB (Montrer NFKB1 Anticorps)-MT1-MMP-dependent and -independent pathway.
Data suggest that EMMPRIN derived from endometrial epithelial cells regulates expression of matrix metalloproteinases (MMP-2 (Montrer MMP2 Anticorps); MMP-14) in endometrial stromal cells; expression of stromal MMPs is significantly higher in coculture with epithelial cells.
MMP-14, MMP-2 (Montrer MMP2 Anticorps) and TIMP-2 (Montrer TIMP2 Anticorps) 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 (Montrer MMP2 Anticorps), MMP14, and the metallopeptidase (Montrer ECEL1 Anticorps) inhibitor TIMP2 (Montrer TIMP2 Anticorps) between different phases of the estrous cycle indicating an endocrine regulation.
EMMPRIN from the luminal epithelium may regulate the expression of stromal MMP-2 (Montrer MMP2 Anticorps) 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 (Montrer AGER Anticorps)-activated NADPH oxidase (Montrer NOX1 Anticorps)-dependent signaling pathways.
MMP-1 (Montrer MMP1 Anticorps) 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 (Montrer MMP2 Anticorps) as critical events in neointimal hyperplasia after vascular injury.
Induction of endogenous MMP-14 gene and coexpression of SAF-1 (Montrer MAZ Anticorps) & MMP-14 in the macrophages present in the atherosclerotic plaque implicate SAF-1 (Montrer MAZ Anticorps) 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