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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 art. Additionally we are shipping MMP14 Kits (24) and MMP14 Proteins (23) and many more products for this protein.
Showing 10 out of 236 products:
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
Show all 4 references for ABIN390138
Human Polyclonal MMP14 Primary Antibody for ELISA, WB - ABIN1536142
Sato, Takino, Okada, Cao, Shinagawa, Yamamoto, Seiki: A matrix metalloproteinase expressed on the surface of invasive tumour cells. in Nature 1994
Show all 2 references for ABIN1536142
Human Polyclonal MMP14 Primary Antibody for EIA, IHC (p) - ABIN358687
Takino, Sato, Yamamoto, Seiki: Cloning of a human gene potentially encoding a novel matrix metalloproteinase having a C-terminal transmembrane domain. in Gene 1995
Show all 2 references for ABIN358687
Human Monoclonal MMP14 Primary Antibody for IHC (fro), IHC (p) - ABIN567585
Cupler, Danon, Jay, Hench, Ropka, Dalakas: Early features of zidovudine-associated myopathy: histopathological findings and clinical correlations. in Acta neuropathologica 1995
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
Silencing KIF1B (show KIF1B Antibodies) inhibited expression of membranal MT1-MMP in glioma cells; however, the amount of MT1-MMP in the whole cell lysate was not affected.
Independent prognostic value of MMP-14 expression in ovarian cancer is limited to a role in PFS for stromal MMP-14.
Data indicate that miR (show MLXIP Antibodies)-337-3p directly binds the MMP-14 promoter to repress its transcription, thus suppressing the progression of NB.
Results identify the tumor suppressor SPRY4 (show SPRY4 Antibodies) as a novel molecular effector of MT1-MMP affecting melanoma cell motility.
Pressure and Temperature Effects on the Activity and Structure of the Catalytic Domain of Human MT1-MMP
MiR (show MLXIP Antibodies)-22 downregulation promotes GC invasion and metastasis by upregulating MMP14 and Snail (show SNAI1 Antibodies), and then inducing ECM (show MMRN1 Antibodies) remodeling and EMT (show ITK Antibodies).
MT1-MMP islets thus act as cellular memory devices.
Overexpression of MT1-MMP in HT-1080 (show CDC123 Antibodies) cells does not significantly alter the invasive ability of these cells.
positive MT1-MMP immunostaining could be found in synoviocytes, vascular endothelial cells, infiltrating macrophages and monocytes in rheumatoid arthritis synovium tissues
TIMP2 (show TIMP2 Antibodies)-based and enediyne-integrated fusion protein targets MMP-14 in colorectal and esophageal neoplasms to suppress growth.
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.
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 Antibodies) 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 Antibodies) and TIMP2 (show TIMP2 Antibodies) correlates negatively with the invasive potential of cells.
Angiotensin II suppresses RECK (show RECK Antibodies), but induces matrix metalloproteinases both in vivo and in vitro.
Active MT1-MMP promotes Notch1 (show NOTCH1 Antibodies) cleavage independently of ADAM10 (show ADAM10 Antibodies) or -17.
LV mass was similar among WT, MT1-MMP overexpression, and MT1-MMP reduced expression after PO, significant differences in LV function.
In the kidneys of Sirt1 (show SIRT1 Antibodies)(endo-/-) mice, impaired angiogenesis, reduced matrilytic activity, and retention of the profibrotic cleavage substrates tissue transglutaminase (show TGM2 Antibodies) and endoglin (show ENG Antibodies) accompanied MMP-14 suppression.
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