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anti-Rat (Rattus) MMP2 Anticorps:
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Chicken Polyclonal MMP2 Primary Antibody pour ICC, IF - ABIN152329
Krekoski, Neubauer, Graham, Muir: Metalloproteinase-dependent predegeneration in vitro enhances axonal regeneration within acellular peripheral nerve grafts. dans The Journal of neuroscience : the official journal of the Society for Neuroscience 2002
Show all 38 Pubmed References
Human Monoclonal MMP2 Primary Antibody pour ICC, IHC (fro) - ABIN152258
Locke, Royce, Wainewright, Samuel, Tang: Comparison of airway remodeling in acute, subacute, and chronic models of allergic airways disease. dans American journal of respiratory cell and molecular biology 2007
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Human Polyclonal MMP2 Primary Antibody pour IF (p), IHC (p) - ABIN668286
Wu, Fan, Zhang, Ning, Zeng, Zhou, Li, Chen, Zhang, Wang, Hsieh, He: PI3K/Akt to GSK3?/?-catenin signaling cascade coordinates cell colonization for bladder cancer bone metastasis through regulating ZEB1 transcription. dans Cellular signalling 2012
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Human Polyclonal MMP2 Primary Antibody pour IF (p), IHC (p) - ABIN707426
Cavdar, Ozbal, Celik, Ergur, Guneli, Ural, Camsari, Guner: The effects of alpha-lipoic acid on MMP-2 and MMP-9 activities in a rat renal ischemia and re-perfusion model. dans Biotechnic & histochemistry : official publication of the Biological Stain Commission 2014
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Cow (Bovine) Polyclonal MMP2 Primary Antibody pour IHC, ELISA - ABIN1582259
Seet, Su, Barathi, Lee, Poh, Heng, Manser, Vithana, Aung, Weaver, Sage, Wong: SPARC deficiency results in improved surgical survival in a novel mouse model of glaucoma filtration surgery. dans PLoS ONE 2010
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Guinea Pig Monoclonal MMP2 Primary Antibody pour ELISA, ICC - ABIN152257
Rork, Hadzimichalis, Kappil, Merrill: Acetaminophen attenuates peroxynitrite-activated matrix metalloproteinase-2-mediated troponin I cleavage in the isolated guinea pig myocardium. dans Journal of molecular and cellular cardiology 2006
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Human Polyclonal MMP2 Primary Antibody pour WB - ABIN657616
Shi, Shang, Pan, Wang, Jiang, Hao, Zhang, Cai, Xu, Zhan, Wang: Calreticulin promotes migration and invasion of esophageal cancer cells by upregulating neuropilin-1 expression via STAT5A. dans Clinical cancer research : an official journal of the American Association for Cancer Research 2014
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Human Monoclonal MMP2 Primary Antibody pour ELISA, WB - ABIN1098146
Langers, Verspaget, Hawinkels, Kubben, van Duijn, van der Reijden, Hardwick, Hommes, Sier: MMP-2 and MMP-9 in normal mucosa are independently associated with outcome of colorectal cancer patients. dans British journal of cancer 2012
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Human Monoclonal MMP2 Primary Antibody pour ELISA, ICC - ABIN451535
Siddesha, Valente, Yoshida, Sakamuri, Delafontaine, Iba, Noda, Chandrasekar: Docosahexaenoic acid reverses angiotensin II-induced RECK suppression and cardiac fibroblast migration. dans Cellular signalling 2014
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Human Monoclonal MMP2 Primary Antibody pour ELISA, IHC (fro) - ABIN314177
Muir: Differences in proliferation and invasion by normal, transformed and NF1 Schwann cell cultures are influenced by matrix metalloproteinase expression. dans Clinical & experimental metastasis 1995
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study demonstrated that matrix metalloproteinase 1 (Montrer MMP1 Anticorps) and 2 might be fundamental for events related to equine tissue remodeling, which occurs during follicular development
Data indicate that matrix metalloproteinases mmp1 (Montrer MMP1 Anticorps) and mmp2 mutants have distinct heart phenotypes.
We also show that follicular OA-Oamb signaling induces Mmp2 enzymatic activation but not Mmp2 protein expression, likely via intracellular Ca2 (Montrer CA2 Anticorps)+ as the second messenger.
Finally, matrix metalloproteinase 2 (Mmp2), a type of protease thought to facilitate mammalian ovulation, is expressed in mature follicle and corpus luteum cells.
As a Wnt (Montrer WNT4 Anticorps) signaling antagonist, MMP2 cleaves the glypican (Montrer GPC1 Anticorps), reducing the ability of Dlp (Montrer DMD Anticorps) to interact with the Wnt (Montrer WNT4 Anticorps) ligand and promote its distribution.
Matrix metalloproteinase 2 is required for fat-body remodeling in Drosophila
Drosophila MMP2 regulates the matrix molecule faulty attraction (Frac) to promote motor axon targeting in Drosophila.
Dendrite reshaping of adult Drosophila sensory neurons requires matrix metalloproteinase MMP2-mediated modification of the basement membranes
Mmp2 expression in the developing air sac (Montrer ADCY10 Anticorps) is controlled by the Drosophila FGF homolog Branchless and then participates in a negative feedback and lateral inhibition mechanism that defines the precise pattern of FGF signaling.
findings demonstrate a critical role for Mmp2 in tubulogenesis post-induction, and implicate Mmp2 in regulating dynamic and essential changes to the extracellular matrix
Dexamethasone and hydrocortisone alter expression and activity of MMP-2 and MMP-9 (Montrer MMP9 Anticorps) in the embryonic zebrafish.
MMP-2 and -9 expression were suppressed significantly by treatment with SB-3CT. The data demonstrated, for the first time, that SB-3CT strongly reduced corneal lymphangiogenesis and macrophage infiltration during inflammation.
animals were submitted to the evaluation of Blood-Brain Barrier permeability and MMP-2 and MMP-9 (Montrer MMP9 Anticorps) in striatum, hippocampus and cerebral cortex
High MMP2 expression is associated with abdominal aortic aneurysm.
Low MMP2 expression is associated with liver fibrosis.
Cleavage of beta-DG still occurred when both MMP-2 and MMP-9 (Montrer MMP9 Anticorps) were knocked out in gamma - sarcoglycan (Montrer SGCG Anticorps)-deficient mice. The study found that up-regulation of MMP-14 (Montrer MMP14 Anticorps) is capable of cleaving beta-DG, and it may be involved in the pathogenesis of sarcoglycanopathy.
NH2-terminal truncated MMP-2 "primes" the kidney to enhanced susceptibility to I-R injury via induction of mitochondrial dysfunction.
Study demonstrated evidence of beta-dystroglycan cleavage by matrix metalloproteinase-2/-9 in permanent middle cerebral artery occlusion mouse brains; this cleavage was implicated in aquaporin-4 (Montrer AQP4 Anticorps) redistribution and brain edema in cerebral ischemia.
These results indicate that increased MMP2 and MMP9 (Montrer MMP9 Anticorps) activity in the brains of mouse adenovirus type 1-infected susceptible mice may be due to MMP activity produced by endothelial cells, astrocytes, and microglia, which in turn may contribute to blood-brain barrier disruption and encephalitis in susceptible mice.
Studies define a novel HMGA1 (Montrer HMGA1 Anticorps)-MMP-2 pathway involved in a subset of human carcinosarcomas and tumor progression in murine models.
activation of astrocyte MMP2/JNK1 (Montrer MAPK8 Anticorps)/2 contributes to the pathogenesis of pain hypersensitivity in the complex regional pain syndrome model
Concentrations of MMP-2 and MMP-9 (Montrer MMP9 Anticorps) in serum in humans measured after acute stroke are potentially influenced by extraneous covariates rather than being directly associated with characteristics of the underlying stroke.
There were no differences in activities of MMP-2, proMMP-9, and MMP-9 (Montrer MMP9 Anticorps)/NGAL (neutrophil gelatinase associated lipocalin (Montrer LCN2 Anticorps)) complex (gelatin substrate) in men with detected prostate cancer, although the latter two were somewhat diminished.
Data indicate that the matrix metallopeptidases MMP-2/MMP-9 (Montrer MMP9 Anticorps) ratio provided better compromise between specificity and sensitivity in distinguishing PE from normal pregnancies, than either of the two MMPs alone.
The A/A genotype (OR=0.120) and A allele (OR=0.442) reduce the risk of recurrent depressive disorder occurrence in the examined polymorphisms for MMP-2, MMP-7 (Montrer MMP7 Anticorps) and MMP-9 (Montrer MMP9 Anticorps).
Data suggest that MMP2 expression in lung neoplasms can be regulated by dietary factors; here, metabolites of quercetin (an antioxidant, anticarcinogenic dietary supplement) quercetin-3-glucuronide and quercetin 3'-sulfate down-regulates expression of MMP2 in A549 cells; the mechanism for this enzyme repression appears to involve up-regulation of PPARgamma (Montrer PPARG Anticorps).
MiRNA199a-3p suppresses tumor growth, migration, invasion and angiogenesis in hepatocellular carcinoma by targeting VEGFA (Montrer VEGFA Anticorps), VEGFR1 (Montrer FLT1 Anticorps), VEGFR2 (Montrer KDR Anticorps), HGF (Montrer HGF Anticorps) and MMP2
Expression of MMP2 is suppressed by Rubus idaeus extract by down-regulating ERK1/2 (Montrer MAPK1/3 Anticorps) signaling pathway.
The rates of CD44st and MMP2 expression were higher in squamous cell carcinomas than in adenocarcinomas, were closely associated with lymph node metastasis and TNM (Montrer ODZ1 Anticorps) stage, and affected patients' prognoses.
characteristics involving MMP-2 and MMP-9 (Montrer MMP9 Anticorps) in Chagas' disease to clarify their participation on the inflammation/regulation and fibrosis, and the synergistic or antagonistic role between them [Review]
This study showed a significantly greater prevalence of the C/C and C/T genotypes in the patients with age-related macular degeneration (AMD (Montrer AMD1 Anticorps)) younger than 65 years and those aged >/=65 years, respectively.
this study shows that differential FFAR1 (Montrer FFAR1 Anticorps) signaling is associated with gene expression or gelatinase granule release in bovine neutrophils
NADPH oxidase (Montrer NOX1 Anticorps) plays an important role in proMMP-2 expression and activation and MMP-2 mediated SMC (Montrer DYM Anticorps) proliferation occurs through the involvement of Spm (Montrer NPC1 Anticorps)-Cer (Montrer CBLN1 Anticorps)-S1P (Montrer MBTPS1 Anticorps) signaling axis under ANG II (Montrer AGT Anticorps) stimulation of PASMCs
The expression patterns of MMP1 (Montrer MMP1 Anticorps), MMP2, and MMP8 (Montrer MMP8 Anticorps) were explored during fetal and postnatal development of longissimus dorsi muscle in cattle, and the relationships of MMP1 (Montrer MMP1 Anticorps), MMP2, and MMP8 (Montrer MMP8 Anticorps) expression levels with meat quality traits were analyzed in cattle. The expression of MMP1 (Montrer MMP1 Anticorps), MMP2, and MMP8 (Montrer MMP8 Anticorps) were also tested in four kinds of fat tissues and three kinds of skeletal muscle tissues.
The results showed that a decrease in MMP-1 (Montrer MMP1 Anticorps) and MMP-2 gene expression is accompanied with a decrease in NO concentrations in infertile cows affected with ovarian cysts.
Activation of cytosolic MMP-9 (Montrer MMP9 Anticorps) and MMP-2 was investigated in the retinal endothelial cells incubated in high glucose for 6-96 h, and correlated with their mitochondrial accumulation and mitochondrial damage.
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 (Montrer MMP14 Anticorps)-dependent and -independent pathway.
Data suggest that EMMPRIN derived from endometrial epithelial cells regulates expression of matrix metalloproteinases (MMP-2; MMP-14 (Montrer MMP14 Anticorps)) in endometrial stromal cells; expression of stromal MMPs is significantly higher in coculture with epithelial cells.
Adding pure bovine MMP-2 to the smooth muscle membrane suspension causes an increase in Ca(2+)-ATPase (Montrer CA-P60A Anticorps) activity, but the pretreatment with TIMP-2 (Montrer TIMP2 Anticorps) inhibits the increase in the enzyme activity
A differential pattern of matrix metalloproteinase-2 and Tissue inhibitor metalloproteinase-2 was observed in cow uteri with adenomyosis.
MMP-14 (Montrer MMP14 Anticorps), MMP-2 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.
we demonstrated the presence of high molecular weight (HMW) complexes (130, 170, and 220 kDa) containing MMP9 (Montrer MMP9 Anticorps), TIMP1 (Montrer TIMP1 Anticorps), and NGAL (Montrer LCN2 Anticorps) (also MMP2 in 220 kDa complex) without proteolytic activity.
Data demonstrate for the first time that MMP2 and MMP9 (Montrer MMP9 Anticorps) are expressed in swine ovarian follicle both in theca and granulosa layers.
FiO2 used for resuscitation affects matrix metalloproteinases MMP-9 (Montrer MMP9 Anticorps) and MMP-2, caspase-3 (Montrer CASP3 Anticorps) and BDNF (Montrer BDNF Anticorps)
MMP-2 may play an important role in regulating MLC1 turnover in the heart under normal physiological conditions
Oxygen for newborn resuscitation increases MMP-2/-9 activity resulting in tissue damage and influencing remodeling processes.
PI3K-dependent regulation of MT1-MMP (Montrer MMP14 Anticorps) protein synthesis and subsequent activation of latent MMP-2 as critical events in neointimal hyperplasia after vascular injury.
MMP-2 processes dental sialophosphoprotein into smaller subunits in the dentin matrix during odontogenesis
contribution of MMPs to the inflammatory breakdown of the blood-CSF (Montrer CSF2 Anticorps) barrier in vitro
The levels of matrix metalloproteinase-2 and matrix metalloproteinase-9 (Montrer MMP9 Anticorps) in the corpus luteum of swine during luteolysis are reported.
Hemodialysis graft placement leads to early increases in wall shear stress, VEGF-A (Montrer VEGFA Anticorps), pro-MMP-9 (Montrer MMP9 Anticorps), MMP-2, VEGFR-1 (Montrer FLT1 Anticorps), VEGFR-2 (Montrer KDR Anticorps), and TIMP-1 (Montrer TIMP1 Anticorps), which may contribute to the development of venous stenosis.
Inflammatory factors such as TNF-alpha (Montrer TNF Anticorps) can stimulate MMP-2/9 activity in corneal epithelium cells. This may be a potential manipulating mechanism of MMP expression in the pathogenesis of corneal diseases
Results provide evidence that MMP-2 bears the potentiality to cleave alpha-DG enriched from rabbit skeletal muscle indicating that this degradation indeed might also occur in vivo.
In conclusion, MMP-2 could be responsible for the proteolysis of dystrophin (Montrer DMD Anticorps).
Castor (Montrer CASZ1 Anticorps) oil polymer induces bone formation with high matrix metalloproteinase-2 expression.
MMP2 spinal cord expression is increased in cervical spondylotic myelopathy.
Ulinastatin (Montrer AMBP Anticorps) effectively inhibited the increased expression of MMP-2, MMP-3 (Montrer MMP3 Anticorps), and iNOS (Montrer NOS2 Anticorps) in degenerated NP cells induced by IL-1beta (Montrer IL1B Anticorps) in vitro.
Hemoperfusion could obviously reduce oxidative stress and the expression levels of MMP-2, MMP-9 (Montrer MMP9 Anticorps) and TIMP-1 (Montrer TIMP1 Anticorps) in rabbits with acute paraquat poisoning.
The RNA interference targeting COX-2 (Montrer COX2 Anticorps) can effectively inhibit the expression of COX-2 (Montrer COX2 Anticorps) and MMP-2 in IL-1alpha stimulated rabbit corneal stromal cells in vitro.
Our results strongly suggest that ischaemic postconditioning may exert part of its cardioprotective effects through the inhibition of MMP-2 activity.
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. This gene encodes an enzyme which degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. Mutations in this gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms have been found for this gene.
, matrix metalloprotease 2
, matrix metalloproteinase
, matrix metalloproteinase 2
, 72 kDa type IV collagenase
, Gelatinase A
, matrix metalloproteinase-2
, 72 kDa gelatinase
, gelatinase A
, 72kD gelatinase
, 72kD type IV collagenase
, 72kDa gelatinase
, 72kDa type IV collagenase
, collagenase type IV-A
, matrix metalloproteinase-II
, neutrophil gelatinase
, matrix metalloproteinase 2 (72 KDa type IV collagenase)
, matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)