Use your antibodies-online credentials, if available.
Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
Afficher toutes les espèces
Afficher tous les synonymes
Sélectionnez vos espèces et l'application
anti-Rat (Rattus) MMP2 Anticorps:
anti-Mouse (Murine) MMP2 Anticorps:
anti-Human MMP2 Anticorps:
Vous arrivez à notre recherche pré-filtrée.
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 39 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
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
Show all 5 Pubmed References
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
Show all 4 Pubmed References
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
Show all 3 Pubmed References
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
Show all 2 Pubmed References
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
Show all 2 Pubmed References
Human Monoclonal MMP2 Primary Antibody pour CyTOF, FACS - ABIN4900818
Zhao, McCloud, Fleming, Klempner: Borrelia burgdorferi-induced monocyte chemoattractant protein-1 production in vivo and in vitro. dans Biochemical and biophysical research communications 2007
Show all 2 Pubmed References
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
Show all 2 Pubmed References
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
inhibition of ECM (Montrer MMRN1 Anticorps) 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 (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
Mmp2 facilitates endothelial-to-hematopoietic transition via ECM (Montrer MMRN1 Anticorps) remodeling.
Dexamethasone and hydrocortisone alter expression and activity of MMP-2 and MMP-9 (Montrer MMP9 Anticorps) in the embryonic zebrafish.
In obese mice, periodontitis caused the downregulation of MMP2, and upregulation of TIMP1 (Montrer TIMP1 Anticorps) and TGF-beta1 (Montrer TGFB1 Anticorps) at transcriptional and translational levels.
In the initial periods of AP progression, an increased expression of MMP9 (Montrer MMP9 Anticorps) in the TLR2 KO and MyD88 (Montrer MYD88 Anticorps) KO mice was observed. In the final periods of AP progression, a reduction of MMP2 expression and an increase of MMP9 (Montrer MMP9 Anticorps) expression in the TLR2 KO mice were observed. MMP2 and MMP9 (Montrer MMP9 Anticorps) production was modulated for TLR2 and MyD88 (Montrer MYD88 Anticorps) during apical periodontitis progression
MMP-2 promoted and MMP-13 (Montrer MMP13 Anticorps) disrupted vasculogenic mimicry formation in large cell lung cancer by cleaving laminin-5 to influence EGFR (Montrer EGFR Anticorps) 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 (Montrer TGFB1 Anticorps) pathway.
Aneurysmal-prone factors induced HIF-1alpha (Montrer HIF1A Anticorps) can cause overexpression of MMP-2 and MMP-9 (Montrer MMP9 Anticorps) and promote aneurysmal progression.
These studies illustrated an important role of MMP2 in cognitive and motor behaviors and confirm its importance in NPC (Montrer NPC1 Anticorps) activities crucial to brain development, growth and response to and recovery from injury.
Secretagogin (Montrer SCGN Anticorps)-dependent MMP2 release from neurons regulates neuroblast migration.
matrix metalloproteinase 2 (Mmp2) transcript is a target of miR (Montrer MLXIP Anticorps)-195a-3p, and that silencing Mmp2 phenocopied the reduced proliferation and migration of MSCs. The therapeutic potential of miR (Montrer MLXIP Anticorps)-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
We conclude that S1P (Montrer MBTPS1 Anticorps) attenuates the invasion of C643 cells by activating S1P2 (Montrer S1PR2 Anticorps) and the Rho-ROCK pathway, by decreasing calpain activity, and by decreasing the expression, secretion and activity of MMP2 and, to a lesser extent, MMP9 (Montrer MMP9 Anticorps). Our results thus unveil a novel function for the S1P2 (Montrer S1PR2 Anticorps) receptor in attenuating thyroid cancer cell invasion.
High mmp2 expression is associated with ovarian cancer cell migration and invasion.
MMP-2 was expressed in high percentage of endometrial cancer and its expression may be associated closely with clinical stage, and tumor invasion and metastasis, indicating that MMP-2 overexpression may serve as a predictive factor for poor prognosis of endometrial cancer.
MMP2 single nucleotide polymorphisms association with lymphedema caused by Wuchereria bancrofti.
High MMP2 expression is associated with esophageal squamous cell carcinoma.
Data suggest that environmental carcinogen PFOA (perfluorooctanoic acid) stimulates ovarian cancer cell migration, invasion, and MMP2/MMP9 expression by up-regulating ERK/NFkappaB signaling pathway. (MMP = matrix metallopeptidase; NFkappaB = nuclear factor kappa B)
Matrix-metalloproteinase-2 is implicated in the pathophysiological mechanism of stenosis development and has a predictive value for arteriovenous fistula failure in hemodialysis patients
Fli1 (Montrer FLI1 Anticorps) functioned as an oncogene (Montrer RAB1A Anticorps) in HCC (Montrer FAM126A Anticorps) carcinogenesis and it exerted its promoting metastatic effect primarily by modulating the matrix metalloproteinase (MMP)2 signaling pathway.
Rictor (Montrer RICTOR Anticorps) regulates the vasculogenic mimicry of melanoma and determines the patients' survival via the AKT (Montrer AKT1 Anticorps)-MMP2-MMP9 (Montrer MMP9 Anticorps) pathway.
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.
Selenium suppressed high-fat diet-induced MMP2 over-expression in vivo by improving lipid metabolism.
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)