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Human MMP14 ELISA Kit for Sandwich ELISA - ABIN415141
Kaimal, Aljumaily, Tressel, Pradhan, Covic, Kuliopulos, Zarwan, Kim, Sharifi, Agarwal: Selective blockade of matrix metalloprotease-14 with a monoclonal antibody abrogates invasion, angiogenesis, and tumor growth in ovarian cancer. in Cancer research 2013
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Sugimoto, Ishibashi, Sawamura, Inoue, Kamioka, Uekita, Ohkawara, Sakamoto, Sakamoto, Okamoto, Takuwa, Kakino, Fujita, Tanaka, Teramoto, Maruyama, Takeishi: LOX-1-MT1-MMP axis is crucial for RhoA and Rac1 activation induced by oxidized low-density lipoprotein in endothelial cells. in Cardiovascular research 2009
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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 (show FUT1 ELISA Kits) 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 (show OCLN ELISA Kits)) 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 (show ST14 ELISA Kits), which regulates the levels of MMP-14 on the cell surface. High levels of matriptase (show ST14 ELISA Kits) in alpha-1 antitrypsin (show SERPINA1 ELISA Kits) deficiency may contribute to increased extracellular matrix degradation by alveolar macrophages both directly and through MMP-14 activation.
High expression of MMP14 and CDK7 (show CDK7 ELISA Kits) was independent prognostic factors for overall survival in patients with gastric cancer.
only collagen-IV (show COL4 ELISA Kits) elicits the formation of proteolytically active podosomes through a mechanism involving increased Src (show SRC ELISA Kits) phosphorylation, p190RhoGAP (show GRLF1 ELISA Kits)-B (also known as ARHGAP5 (show ARHGAP5 ELISA Kits)) relocalisation and MT1-MMP (also known as MMP14) cell surface exposure at podosome sites.
This study demonstrates that excessive ECM (show MMRN1 ELISA Kits) 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 (show DDR2 ELISA Kits) 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 (show MMP15 ELISA Kits) in regulating mammary gland adipocyte differentiation. Whereas MMP14 promotes the generation of white fat depots crucial for energy storage, MMP15 (show MMP15 ELISA Kits) differentially controls the formation of thermogenic brown fat.
The authors identified the membrane-tethered matrix metalloprotease (show ADAMTS7 ELISA Kits) 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 ELISA Kits) on lymphatic endothelial cells to inhibit LYVE-1 (show LYVE1 ELISA Kits)-mediated lymphangiogenic responses and restrains the production of VEGF-C (show VEGFC ELISA Kits).
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 (show HPSE ELISA Kits) 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 (show TIMP1 ELISA Kits) and TIMP2 (show TIMP2 ELISA Kits) correlates negatively with the invasive potential of cells.
results suggest that ET-1 (show EDN1 ELISA Kits)-induced activation of proMMP-2 is mediated via cross-talk between NADPH oxidase (show NOX1 ELISA Kits)-PKCalpha (show PKCa ELISA Kits)-p(38)MAPK (show MAPK1 ELISA Kits) and NFkappaB-MT1MMP signaling pathways along with a marked decrease in TIMP-2 (show TIMP2 ELISA Kits) expression in the cells
Data indicate the involvement of PKC-alpha (show PKCa ELISA Kits) in proMMP-2 activation and inhibition of TIMP-2 (show TIMP2 ELISA Kits) expression by NF-kappaB (show NFKB1 ELISA Kits)-MT1-MMP-dependent and -independent pathway.
Data suggest that EMMPRIN derived from endometrial epithelial cells regulates expression of matrix metalloproteinases (MMP-2 (show MMP2 ELISA Kits); MMP-14) in endometrial stromal cells; expression of stromal MMPs is significantly higher in coculture with epithelial cells.
MMP-14, MMP-2 (show MMP2 ELISA Kits) and TIMP-2 (show TIMP2 ELISA Kits) 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 ELISA Kits), MMP14, and the metallopeptidase (show ECEL1 ELISA Kits) inhibitor TIMP2 (show TIMP2 ELISA Kits) 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 ELISA Kits) 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 ELISA Kits)-activated NADPH oxidase (show NOX1 ELISA Kits)-dependent signaling pathways.
MMP-1 (show MMP1 ELISA Kits) 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 ELISA Kits) as critical events in neointimal hyperplasia after vascular injury.
Induction of endogenous MMP-14 gene and coexpression of SAF-1 & MMP-14 in the macrophages present in the atherosclerotic plaque implicate SAF-1 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