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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 44 Pubmed References
Human Polyclonal MMP2 Primary Antibody pour ELISA, WB - ABIN5518776
Wuttke, Schmitt, Buchner, Doletschek: [Typical cases of an inflammatory aortic aneurysm demonstrated by computed tomography]. dans Röntgenpraxis; Zeitschrift für radiologische Technik 1989
Show all 28 Pubmed References
Human Polyclonal MMP2 Primary Antibody pour IF, IHC - ABIN6711840
Tang, Zhu, Gao, Fu, Liu, Liu, Song, Zhu, Leng, Wang, Chen, Du, Huang, Zhou, Kang, Cui: MicroRNA-29a promotes colorectal cancer metastasis by regulating matrix metalloproteinase 2 and E-cadherin via KLF4. dans British journal of cancer 2014
Show all 19 Pubmed References
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
Show all 14 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
Show all 13 Pubmed References
Human Polyclonal MMP2 Primary Antibody pour ELISA, ICC - ABIN6263299
Li, Zhang, Sun, Sun, Shi, Liu, Liu: MicroRNA-181a regulates epithelial-mesenchymal transition by targeting PTEN in drug-resistant lung adenocarcinoma cells. dans International journal of oncology 2016
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Polyclonal MMP2 Primary Antibody pour IHC (fro), IHC (p) - ABIN540673
Mikami, Katsube, Oya, Ishida, Kosaka, Mizuno, Mukai, Okada: Expression of Snail and Slug in renal cell carcinoma: E-cadherin repressor Snail is associated with cancer invasion and prognosis. dans Laboratory investigation; a journal of technical methods and pathology 2011
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Human Polyclonal MMP2 Primary Antibody pour WB - ABIN6683509
Fu, Wang, Wu, Feng, Wang, Zhou, Ma, Wang: HMGA1 exacerbates tumor growth through regulating the cell cycle and accelerates migration/invasion via targeting miR-221/222 in cervical cancer. dans Cell death & disease 2018
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Human Polyclonal MMP2 Primary Antibody pour WB - ABIN6143911
Huang, Song, Sun, Zhang, Huang: IRX5 promotes NF-κB signalling to increase proliferation, migration and invasion via OPN in tongue squamous cell carcinoma. dans Journal of cellular and molecular medicine 2018
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Human Monoclonal MMP2 Primary Antibody pour IHC (p), WB - ABIN659015
Wang, Cao, Huang, Ke, Luo, Lin, Wang, Zhang, Wang: EFEMP1 promotes the migration and invasion of osteosarcoma via MMP-2 with induction by AEG-1 via NF-κB signaling pathway. dans Oncotarget 2016
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potential activity 1.4 times higher in control placentas than in placentas of mares retaining fetal membranes
study demonstrated that matrix metalloproteinase 1 and 2 might be fundamental for events related to equine tissue remodeling, which occurs during follicular development
there are only two MMP genes in Drosophila, DmMmp1 and DmMmp2, which makes Drosophila an attractive system to analyze the basis of MMP specificity. Previously, Drosophila MMPs have been categorized by their pericellular localization, as Mmp1 appeared to be secreted and Mmp2 appeared to be membrane-anchored, suggesting that protein localization was the critical distinction in this small MMP family
inhibition of ECM degradation by inhibition of matrix metalloproteinase 2 (Mmp2) to preserve the extracellular environment characteristics of young adults led to increased dendrite regeneration
Data indicate that matrix metalloproteinases mmp1 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+ 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 signaling antagonist, MMP2 cleaves the glypican, reducing the ability of Dlp to interact with the Wnt 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 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.
complete base sequence given for a 758 residue polypeptide
Drosophila matrix metalloproteinases are required for tissue remodeling, but not embryonic development.
MMP activity is essential for embryonic motor axon fasciculation
findings demonstrate a critical role for Mmp2 in tubulogenesis post-induction, and implicate Mmp2 in regulating dynamic and essential changes to the extracellular matrix
Mmp2 facilitates endothelial-to-hematopoietic transition via ECM remodeling.
membrane-type 1 metalloproteinase, zmmp-2, and tissue inhibitor 2 of metalloproteinases mRNA transcripts were expressed in the blastema
Dexamethasone and hydrocortisone alter expression and activity of MMP-2 and MMP-9 in the embryonic zebrafish.
the aim of this study was to determine whether Acanthamoeba spp. may affect the levels of matrix metalloproteinases (MMP-2,-9), their tissue inhibitors (TIMP-1,-3) and MMP-9/TIMP-1, MMP-2/TIMP-3 ratios in the cerebral cortex and hippocampus, in relation to the host's immunological status.
results suggest that in response to stretch, MMP-2 responds rapidly by inhibiting conversion of a MMP-2 to the active form, while a slower up-regulation of MMP-9 may play a role in the long-term remodeling of extracellular matrix in response to continuous mechanical loading
Downstream molecular target of protein tyrosine phosphatase sigma (PTPsigma) modulation in oligodendrocyte progenitor cells (OPCs) involving upregulation of the protease matrix metallopeptidase 2 (MMP-2) that allows OPCs to enzymatically digest their way through chondroitin sulfate proteoglycans (CSPGs
In obese mice, periodontitis caused the downregulation of MMP2, and upregulation of TIMP1 and TGF-beta1 at transcriptional and translational levels.
In the initial periods of AP progression, an increased expression of MMP9 in the TLR2 KO and MyD88 KO mice was observed. In the final periods of AP progression, a reduction of MMP2 expression and an increase of MMP9 expression in the TLR2 KO mice were observed. MMP2 and MMP9 production was modulated for TLR2 and MyD88 during apical periodontitis progression
MMP-2 promoted and MMP-13 disrupted vasculogenic mimicry formation in large cell lung cancer by cleaving laminin-5 to influence EGFR signal activation.
Diet and exercise affect atheromatous MMP2/9 activity by modulating the systemic inflammatory milieu, with sVCAM-1, resistin, and adiponectin closely interacting with each other and with visceral fat.
calpains inhibition plays crucial roles in vascular restenosis by preventing neointimal hyperplasia at the early stage via suppression of the MMP2/TGF-beta1 pathway.
Aneurysmal-prone factors induced HIF-1alpha can cause overexpression of MMP-2 and MMP-9 and promote aneurysmal progression.
These studies illustrated an important role of MMP2 in cognitive and motor behaviors and confirm its importance in NPC activities crucial to brain development, growth and response to and recovery from injury.
Secretagogin-dependent MMP2 release from neurons regulates neuroblast migration.
This novel mouse model will be a very useful tool for evaluating the mechanistic pathways and for development of novel therapies in cigarette smoke-associated lung emphysema.
matrix metalloproteinase 2 (Mmp2) transcript is a target of miR-195a-3p, and that silencing Mmp2 phenocopied the reduced proliferation and migration of MSCs. The therapeutic potential of miR-195a-3p as an angiogenesis inhibitor was also demonstrated in a laser-induced choroidal neovascularization mouse model.
developed a novel selective radiolabeled MMP2/9 inhibitor, suitable for single photon emission computed tomography (SPECT) imaging that effectively targets atherosclerotic lesions in mice
MMP-2 and MMP-9 have roles in early stages of experimental autoimmune encephalomyelitis induction; MMP-9 from an immune cell source is required in EAE for initial infiltration of leukocytes into the central nervous system
This study illustrated that tumour-derived MMP2 has at least two roles in tumour malignancy; to enhance tumour invasiveness by degrading the extracellular matrix and to enhance tumour growth by promoting vessel maturation and function.
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 in striatum, hippocampus and cerebral cortex
High MMP2 expression is associated with abdominal aortic aneurysm.
Low MMP2 expression is associated with liver fibrosis.
Treatment with PFOA did not affect cell migration, but enhanced cell invasion, adhesion and activity of MMP-2 in FTC133 cells. PFOA selectively enhanced the phosphorylation of nuclear factor kappa B (NF-kappaB) p65, as well as induced NF-kappaB nuclear translocation.
The authors' findings suggest that changes in DNA methylation at the promoter region of MMP2 could underlie the changes in its expression in the ectopic endometria from patients with endometriosis.
Elevated levels of MMP-2 protein levels were observed in all regions of PT-PE placenta possibly influencing the degradation of placental ECM. Lower mRNA expression of MMP-9 both in PT-PE and T-PE may contribute to a disturbed placental vascularization.
IGFBP2 acts as a stimulator of Vasculogenic mimicry formation in glioma cells via enhancing CD144 and MMP2 expression.
In both diffuse adenomyosis and adenomyomas, the basal layer of the eutopic and ectopic endometrium differed many (3-8.5) times, showing the higher expression of the enzymes in the epithelial and stromal cells, which affected their invasive activity (moesin, PAK 4, MMP 2 and MMP 9), and the increased number of CD34 cells in its stroma.
The expression of the gelatinases MMP 2, MMP 9 and regulators of their activity is aimed at increasing the tumor destructive (invasive) potential and can occur (be induced) in the intact corpus uteri tissue that is morphologically different from cervix uteri tissue with apparent participation of signaling through an epithelial-mesenchymal interaction.
Matrix metalloproteinase-2 alleles and genotypes, along with four-locus haplotypes, are related to reduced susceptibility to breast cancer in Tunisian women, suggesting a protective effect.
The serum level of MMP2 was significantly increased after spinal cord stimulation and remained elevated up to three months after implantation.
MMP-2 and OPG may be involved in the pathogenesis of atherosclerosis in patients with chronic kidney disease and could potentially be of use as biomarkers of subclinical atherosclerosis in these patients.
Overexpression of TRIM55 was associated with lower cell migration and invasion ability, and it led to high expression of E-cadherin and low expression of Vimentin and MMP2.
Report higher MMP-2 expression in epithelial ovarian cancers sensitive to platinum-taxane based chemotherapy.
the findings of this study suggested that d2HG induced angiogenic activity via VEGFR2 signaling and increased MMP2 activity.
In periodontitis, EMMPRIN regulates MMP-2, 9 expressions, the activation of Wnt/beta-catenin signaling pathway downregulates the EMMPRIN/MMP-2, 9 routes and the blockade of EMMPRIN attenuates Wnt/beta-catenin signaling pathway.
The polymorphisms in MMP2, MMP9 and MMP20 genes were not statistically associated with human dental fluorosis.
Our results provide evidence showing that the variant CT and TT genotypes at MMP-2 promoter -1306 or -735 may play a minor role in determining the susceptibility to childhood acute lymphocytic leukemia in Taiwan.
High MMP2 expression is associated with Renal Cell Carcinoma.
Migfilin promotes migration and invasion in glioma by driving EGFR and MMP-2 signalings
PAX6 overexpression increasing MMP2 and MMP9 expression.
findings demonstrate that MMP-2 rs243865 polymorphism and MMP-9 rs3918242 polymorphism can increase the risk of HPS occurrence in cirrhotic patients, which provides a potential target for prevention of HPS in cirrhotic patients.
Results demonstrated that MMP-2 is highly expressed in the ligamentum flavum (LF) tissue of patients with lumbar spinal canal stenosis, and that MMP-2, induced by IL-6 in LF fibroblasts, promotes the loss of elastic fibers during LF tissue degeneration.
this study shows that differential FFAR1 signaling is associated with gene expression or gelatinase granule release in bovine neutrophils
NADPH oxidase plays an important role in proMMP-2 expression and activation and MMP-2 mediated SMC proliferation occurs through the involvement of Spm-Cer-S1P signaling axis under ANG II stimulation of PASMCs
The expression patterns of MMP1, MMP2, and MMP8 were explored during fetal and postnatal development of longissimus dorsi muscle in cattle, and the relationships of MMP1, MMP2, and MMP8 expression levels with meat quality traits were analyzed in cattle. The expression of MMP1, MMP2, and MMP8 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 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 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 in proMMP-2 activation and inhibition of TIMP-2 expression by NF-kappaB-MT1-MMP-dependent and -independent pathway.
Data suggest that EMMPRIN derived from endometrial epithelial cells regulates expression of matrix metalloproteinases (MMP-2; MMP-14) 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 activity, but the pretreatment with TIMP-2 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, MMP-2 and TIMP-2 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, MMP14, and the metallopeptidase inhibitor TIMP2 between different phases of the estrous cycle indicating an endocrine regulation.
EMMPRIN from the luminal epithelium may regulate the expression of stromal MMP-2 and MMP-14 suggesting a role in adhesion and fusion of embryo to luminal epithelium.
High shear stress up-regulates type IV collagen synthesis and down-regulates MMP-2 secretion in endothelial cells.
increased MMP-2 activity subsequently played a pivotal role in stimulating Ca2+ ATPase activity in bovine pulmonary vascular smooth muscle plasma membrane
MMP2 has a role in the oxidant activation of Ca2+Atpase
results suggest a significant role of matrix metalloproteinase-2 and-9 in growth and development of bovine follicle
Cells constitutively produced proMMP-9 and proMMP-2, and treatment with TNFalpha, hepatocyte growth factor, and 12-O-tetradecanoylphorbol 13-acetate resulted in significant increase in level of proMMP-9 but not in level of proMMP-2.
MMP-2 and MMP-9 production in blastocysts attached to the endometrial cells is regulated by TNF-alpha and TNF-beta
study suggests that MMP-2 plays an important role in regulating Ca2+ATPase activity, and ATP-dependent and Na+-dependent Ca2+ uptake in microsomes of bovine pulmonary artery smooth muscle during treatment with peroxynitrite
reveal a potentially novel role for strain-induced endothelial matrix metalloproteinase-2 in regulating vascular smooth muscle cell migration
we demonstrated the presence of high molecular weight (HMW) complexes (130, 170, and 220 kDa) containing MMP9, TIMP1, and NGAL (also MMP2 in 220 kDa complex) without proteolytic activity.
Data demonstrate for the first time that MMP2 and MMP9 are expressed in swine ovarian follicle both in theca and granulosa layers.
FiO2 used for resuscitation affects matrix metalloproteinases MMP-9 and MMP-2, caspase-3 and BDNF
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 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 barrier in vitro
The levels of matrix metalloproteinase-2 and matrix metalloproteinase-9 in the corpus luteum of swine during luteolysis are reported.
Hemodialysis graft placement leads to early increases in wall shear stress, VEGF-A, pro-MMP-9, MMP-2, VEGFR-1, VEGFR-2, and TIMP-1, which may contribute to the development of venous stenosis.
In conclusion, thrombin activates pro-MMP-2 in the absence of elevated pro-MMP-2 expression and secretion in CSMCs, and thrombin induces CSMC mitogenesis involving its action on MMP-2.
MMP-2 has a novel function in the degradation of the nuclear matrix in cigarette smoke-induced endothelial apoptosis.
we cloned the 5'-upstream sequence, 3'-downstream sequence as well as other missed genomic sequences of porcine MMP-2, the genomic structure and the promotor sequence were analyzed and found to share high similarity with those of human MMP-2.
The expression of MMP2 and MMP9 in lung injury induced by mechanical stress, hypoxic injury, and septic shock in anesthetized swine are reported.
The association results showed that the animals with the C allele of MMP2 have a significantly larger loin muscle area than that of the animals with the G allele (P < 0.05)
These results show that MMP-2 activates the EGFR and triggers downstream signaling pathways increasing Reactive Oxygen Species formation and promoting vasoconstriction.
The present study demonstrated the ability of 30 and 100 ng/ml TIMP3 to attenuate migration and proliferation, and to inhibit the activity of MMP2, MMP9 and TNFalpha secretion of NA SMCs. In conclusion, TIMP3 may be considered a potential therapeutic drug for use in a novel drugeluting stent, to attenuate the progressive dilation of the aortic NA.
Selenium suppressed high-fat diet-induced MMP2 over-expression in vivo by improving lipid metabolism.
Repetitive mechanical stimulation of tendon cells results in a small increase in matrix metalloproteinase2 levels, but it appears unlikely that serum matrix metalloproteinase2 will be a useful indicator of tendon overuse injury.
Inflammatory factors such as TNF-alpha 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.
These data suggest that OxyHb suppresses K V currents through both reactive oxygen species-dependent and independent pathways involving MMP activation.
In conclusion, MMP-2 could be responsible for the proteolysis of dystrophin.
Castor oil polymer induces bone formation with high matrix metalloproteinase-2 expression.
MMP2 spinal cord expression is increased in cervical spondylotic myelopathy.
Ulinastatin effectively inhibited the increased expression of MMP-2, MMP-3, and iNOS in degenerated NP cells induced by IL-1beta in vitro.
Hemoperfusion could obviously reduce oxidative stress and the expression levels of MMP-2, MMP-9 and TIMP-1 in rabbits with acute paraquat poisoning.
Exposure to long periods of light irrespective of its characteristics leads to the increased expression of some matrix metalloprpteases.
The RNA interference targeting COX-2 can effectively inhibit the expression of COX-2 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)