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anti-Human MMP14 Antikörper:
anti-Mouse (Murine) MMP14 Antikörper:
anti-Rat (Rattus) MMP14 Antikörper:
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Human Polyclonal MMP14 Primary Antibody für 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. in Biochemical and biophysical research communications 2012
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Human Polyclonal MMP14 Primary Antibody für IHC (p), WB - ABIN3044302
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
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Human Polyclonal MMP14 Primary Antibody für IHC (fro), IHC (p) - ABIN4886668
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 für CyTOF, FACS - ABIN4899220
Mierke, Bretz, Altevogt: Contractile forces contribute to increased glycosylphosphatidylinositol-anchored receptor CD24-facilitated cancer cell invasion. in The Journal of biological chemistry 2011
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Human Monoclonal MMP14 Primary Antibody für CyTOF, FACS - ABIN4899219
Mierke, Frey, Fellner, Herrmann, Fabry: Integrin α5β1 facilitates cancer cell invasion through enhanced contractile forces. in Journal of cell science 2011
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Human Polyclonal MMP14 Primary Antibody für 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 Monoclonal MMP14 Primary Antibody für 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
Human Monoclonal MMP14 Primary Antibody für 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 Polyclonal MMP14 Primary Antibody für 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 für 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
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 (zeige MMP2 Antikörper) and increases S100A9 (zeige S100A9 Antikörper) levels in lung tissue. * MMP-14 ameliorates inflammation by promoting S100A9 (zeige S100A9 Antikörper) cleavage by activated MMP-2 (zeige MMP2 Antikörper).
In turn, LIMK1 (zeige LIMK1 Antikörper) and LIMK2 (zeige LIMK2 Antikörper) are required for MT1-MMP-dependent matrix degradation and cell invasion in a three-dimensional type I collagen environment.
miR (zeige MLXIP Antikörper)-337-3p directly binds to the MMP-14 promoter to repress MZF1 (zeige ZFP42 Antikörper)-facilitatd MMP-14 expression, thus suppressing the progression of gastric cancer
CCN3 (Nov (zeige NOV Antikörper)) and CCN5 (WISP2 (zeige WISP2 Antikörper)) are novel substrates of MMP14.
The current data support MT1-MMP as an additional ILK (zeige ILK Antikörper) substrate and show that modulation of ILK (zeige ILK Antikörper) expression and activity inhibit MT1-MMP-related pro-metastatic behaviors of ovarian cancer cells.
Kinase activation led to increased MMP-2 (zeige MMP2 Antikörper) and MT1-MMP expression and melanoma cell migration induced by hHK-1 (zeige HOOK1 Antikörper). Thus, hHK-1 (zeige HOOK1 Antikörper) and the NK1 receptor (zeige TACR1 Antikörper) are critical to melanoma cell migration and each may be a promising chemotherapeutic target
Endoplasmic reticulum (ER) glycosylation of MMP14 is required for ECM (zeige MMRN1 Antikörper) degradation and tumor growth.
Authors demonstrate that CAIX (zeige CA9 Antikörper) associates with MMP14 through potential phosphorylation residues within its intracellular domain, and that CAIX (zeige CA9 Antikörper) 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 (zeige FUT1 Antikörper) proliferation via posttranslational modification of collagen and MT1-MMP
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 (zeige MMP15 Antikörper) in regulating mammary gland adipocyte differentiation. Whereas MMP14 promotes the generation of white fat depots crucial for energy storage, MMP15 (zeige MMP15 Antikörper) differentially controls the formation of thermogenic brown fat.
The authors identified the membrane-tethered matrix metalloprotease (zeige ADAMTS7 Antikörper) 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 (zeige LYVE1 Antikörper) on lymphatic endothelial cells to inhibit LYVE-1 (zeige LYVE1 Antikörper)-mediated lymphangiogenic responses and restrains the production of VEGF-C (zeige VEGFC Antikörper).
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 suggest that ET-1 (zeige EDN1 Antikörper)-induced activation of proMMP-2 is mediated via cross-talk between NADPH oxidase (zeige NOX1 Antikörper)-PKCalpha (zeige PKCa Antikörper)-p(38)MAPK (zeige MAPK1 Antikörper) and NFkappaB-MT1MMP signaling pathways along with a marked decrease in TIMP-2 (zeige TIMP2 Antikörper) expression in the cells
Data indicate the involvement of PKC-alpha (zeige PKCa Antikörper) in proMMP-2 activation and inhibition of TIMP-2 (zeige TIMP2 Antikörper) expression by NF-kappaB (zeige NFKB1 Antikörper)-MT1-MMP-dependent and -independent pathway.
Data suggest that EMMPRIN derived from endometrial epithelial cells regulates expression of matrix metalloproteinases (MMP-2 (zeige MMP2 Antikörper); MMP-14) in endometrial stromal cells; expression of stromal MMPs is significantly higher in coculture with epithelial cells.
MMP-14, MMP-2 (zeige MMP2 Antikörper) and TIMP-2 (zeige TIMP2 Antikörper) 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 (zeige MMP2 Antikörper), MMP14, and the metallopeptidase (zeige ECEL1 Antikörper) inhibitor TIMP2 (zeige TIMP2 Antikörper) between different phases of the estrous cycle indicating an endocrine regulation.
EMMPRIN from the luminal epithelium may regulate the expression of stromal MMP-2 (zeige MMP2 Antikörper) 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 (zeige AGER Antikörper)-activated NADPH oxidase (zeige NOX1 Antikörper)-dependent signaling pathways.
MMP-1 (zeige MMP1 Antikörper) 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 (zeige MMP2 Antikörper) as critical events in neointimal hyperplasia after vascular injury.
Induction of endogenous MMP-14 gene and coexpression of SAF-1 (zeige MAZ Antikörper) & MMP-14 in the macrophages present in the atherosclerotic plaque implicate SAF-1 (zeige MAZ Antikörper) 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