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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 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 für WB - ABIN3043408
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 Monoclonal MMP14 Primary Antibody für 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
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Human Monoclonal MMP14 Primary Antibody für CyTOF, FACS - ABIN4899220
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 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
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 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
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
MT1-MMP-expressing cells induced co-cultured non-MT1-MMP-expressing cells.
The mechanism of transition from nondifferentiated to differentiated states in HepaRG cells was studied by proteomics. Two key factors (MMP-14 and OCLN (zeige OCLN Antikörper)) were validated by qRT-PCR and Western blot. Blockade of MMP-14 further demonstrated its important function during tumor cell migration.
Data suggest that phosphorylation of Thr567 in cytoplasmic tail of MT1-MMP (MMP14) influences behavior of both individual ovarian cancer cells and multicellular aggregates; tumor cells expressing MT1-MMP-T567E phosphomimetic mutant exhibit enhanced cell migration and enhanced cell adhesion to peritoneum and other biological surfaces.
MMP-14 Is a novel substrate for matriptase (zeige ST14 Antikörper), which regulates the levels of MMP-14 on the cell surface. High levels of matriptase (zeige ST14 Antikörper) in alpha-1 antitrypsin (zeige SERPINA1 Antikörper) deficiency may contribute to increased extracellular matrix degradation by alveolar macrophages both directly and through MMP-14 activation.
High expression of MMP14 and CDK7 (zeige CDK7 Antikörper) was independent prognostic factors for overall survival in patients with gastric cancer.
only collagen-IV (zeige COL4 Antikörper) elicits the formation of proteolytically active podosomes through a mechanism involving increased Src (zeige SRC Antikörper) phosphorylation, p190RhoGAP (zeige GRLF1 Antikörper)-B (also known as ARHGAP5 (zeige ARHGAP5 Antikörper)) relocalisation and MT1-MMP (also known as MMP14) cell surface exposure at podosome sites.
This study demonstrates that excessive ECM (zeige MMRN1 Antikörper) degradation mediated by high levels of MT1-MMP is not associated with cell migration and tumourigenesis, while low levels of MT1-MMP promote invasion and vascularization in vivo.
DDR2 (zeige DDR2 Antikörper) mediates collagen-induced activation of MT1-MMP in human fibroblasts
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 show a reciprocal association between levels of heparanase (zeige HPSE Antikörper) and MMP14, a membrane-bound MMP, shedding light on how branching occurs within developing mammary glands.
MT1-MMP proteolytic activity is required for maintaining cell integrity, loss of MT1-MMP causes cell senescence and nuclear defects.
of the transcripts of tissue inhibitors of matrix metalloproteinases (TIMPs) showed that expression of both TIMP1 (zeige TIMP1 Antikörper) and TIMP2 (zeige TIMP2 Antikörper) correlates negatively with the invasive potential of cells.
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