Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Human MMP2 Protein expressed in Human Cells - ABIN2002031
Brooks, Silletti, von Schalscha, Friedlander, Cheresh: Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity. in Cell 1998
Show all 7 Pubmed References
Human MMP2 Protein expressed in Escherichia coli (E. coli) - ABIN1080273
Zheng, Hu, Huang, Xu, Yang, Li: In vivo bioengineered ovarian tumors based on collagen, matrigel, alginate and agarose hydrogels: a comparative study. in Biomedical materials (Bristol, England) 2015
Human MMP2 Protein expressed in HEK-293 Cells - ABIN2181511
Fernandez-Patron, Radomski, Davidge: Vascular matrix metalloproteinase-2 cleaves big endothelin-1 yielding a novel vasoconstrictor. in Circulation research 1999
Show all 6 Pubmed References
study demonstrated that matrix metalloproteinase 1 (show MMP1 Proteins) and 2 might be fundamental for events related to equine tissue remodeling, which occurs during follicular development
inhibition of ECM (show MMRN1 Proteins) 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 (show MMP1 Proteins) 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 (show CA2 Proteins)+ 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 (show WNT4 Proteins) signaling antagonist, MMP2 cleaves the glypican (show GPC1 Proteins), reducing the ability of Dlp (show DMD Proteins) to interact with the Wnt (show WNT4 Proteins) 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 (show ADCY10 Proteins) 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 (show MMRN1 Proteins) remodeling.
Dexamethasone and hydrocortisone alter expression and activity of MMP-2 and MMP-9 (show MMP9 Proteins) in the embryonic zebrafish.
In obese mice, periodontitis caused the downregulation of MMP2, and upregulation of TIMP1 (show TIMP1 Proteins) and TGF-beta1 (show TGFB1 Proteins) at transcriptional and translational levels.
In the initial periods of AP progression, an increased expression of MMP9 (show MMP9 Proteins) in the TLR2 KO and MyD88 (show MYD88 Proteins) KO mice was observed. In the final periods of AP progression, a reduction of MMP2 expression and an increase of MMP9 (show MMP9 Proteins) expression in the TLR2 KO mice were observed. MMP2 and MMP9 (show MMP9 Proteins) production was modulated for TLR2 and MyD88 (show MYD88 Proteins) during apical periodontitis progression
MMP-2 promoted and MMP-13 (show MMP13 Proteins) disrupted vasculogenic mimicry formation in large cell lung cancer by cleaving laminin-5 to influence EGFR (show EGFR Proteins) 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 (show TGFB1 Proteins) pathway.
Aneurysmal-prone factors induced HIF-1alpha (show HIF1A Proteins) can cause overexpression of MMP-2 and MMP-9 (show MMP9 Proteins) and promote aneurysmal progression.
These studies illustrated an important role of MMP2 in cognitive and motor behaviors and confirm its importance in NPC (show NPC1 Proteins) activities crucial to brain development, growth and response to and recovery from injury.
Secretagogin (show SCGN Proteins)-dependent MMP2 release from neurons regulates neuroblast migration.
matrix metalloproteinase 2 (Mmp2) transcript is a target of miR (show MLXIP Proteins)-195a-3p, and that silencing Mmp2 phenocopied the reduced proliferation and migration of MSCs. The therapeutic potential of miR (show MLXIP Proteins)-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 propose that serum levels of MMP-2 and MMP-9 (show MMP9 Proteins) are not predictive on treatment response and survival in LARC (show CCL20 Proteins) patients.
that miR (show MLXIP Proteins)-338-5p has a function in promoting glioma cell invasion by targeting TSHZ3 (show ZNF537 Proteins) suppression on MMP2
In dilation cardiomyopathy, expression of MMP-2, MMP-9 (show MMP9 Proteins), and TIMP-1 (show TIMP1 Proteins) and their ratios in autopsy material and in cultures was elevated by 1.5-9 times.
OSM (show OSM Proteins) [oncostatin M (show OSM Proteins)]might be involved in the invasiveness of extravillous trophoblasts under hypoxia conditions via increasing MMP-2 and MMP-9 (show MMP9 Proteins) enzymatic activities through STAT3 (show STAT3 Proteins) signaling. Increased MMP-9 (show MMP9 Proteins) activity by OSM (show OSM Proteins) seems to be more important in primary trophoblasts.
TIMP2 (show TIMP2 Proteins) promotes tumor progression and miR2055p directly regulates TIMP2 (show TIMP2 Proteins), thereby suppressing proMMP2 activation and inhibiting oral squamous cell carcinoma cell invasiveness.
Elevated MMP-2 levels were observed in blood of pancreatic cancer patients which correlated with its tissue expression. However, these levels did not associate with survival or any clinicopathological parameters of patients.
2G allele of MMP-1 (show MMP1 Proteins), C allele of MMP-2 and 5A/6A genotype of MMP-3 (show MMP3 Proteins) are associated with susceptibility and disease progression of type 2 diabetic nephropathy
Increased urinary concentration of matrix metallopeptidase 2 (MMP-2) at 12 and 16 weeks of gestation predicted an increased risk of developing preeclampsia in the study population.
There was no difference found in MMP-2, MMP-9 (show MMP9 Proteins) or TLR-4 (show TLR4 Proteins) levels between non-thrombocytopenic and thrombocytopenic septic donors. PLA formation was increased in thrombocytopenic patients.
MMP2 rs243865 was the only single nucleotide polymorphism significantly associated with Floppy Mitral Valve/Mitral Valve Prolapse (FMV/MVP (show MVP Proteins)) as compared to the control.The frequency of certain MMP2 polymorphisms is higher in patients with the FMV/MVP (show MVP Proteins) syndrome and patients with FMV/MVP (show MVP Proteins) without the syndrome.
this study shows that differential FFAR1 (show FFAR1 Proteins) signaling is associated with gene expression or gelatinase granule release in bovine neutrophils
NADPH oxidase (show NOX1 Proteins) plays an important role in proMMP-2 expression and activation and MMP-2 mediated SMC (show DYM Proteins) proliferation occurs through the involvement of Spm (show NPC1 Proteins)-Cer (show CBLN1 Proteins)-S1P (show MBTPS1 Proteins) signaling axis under ANG II (show AGT Proteins) stimulation of PASMCs
The expression patterns of MMP1 (show MMP1 Proteins), MMP2, and MMP8 (show MMP8 Proteins) were explored during fetal and postnatal development of longissimus dorsi muscle in cattle, and the relationships of MMP1 (show MMP1 Proteins), MMP2, and MMP8 (show MMP8 Proteins) expression levels with meat quality traits were analyzed in cattle. The expression of MMP1 (show MMP1 Proteins), MMP2, and MMP8 (show MMP8 Proteins) 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 (show MMP1 Proteins) 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 (show MMP9 Proteins) 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 (show PKCa Proteins) in proMMP-2 activation and inhibition of TIMP-2 (show TIMP2 Proteins) expression by NF-kappaB (show NFKB1 Proteins)-MT1-MMP (show MMP14 Proteins)-dependent and -independent pathway.
Data suggest that EMMPRIN derived from endometrial epithelial cells regulates expression of matrix metalloproteinases (MMP-2; MMP-14 (show MMP14 Proteins)) 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 (show TIMP2 Proteins) 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 (show MMP14 Proteins), MMP-2 and TIMP-2 (show TIMP2 Proteins) 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 (show MMP9 Proteins), TIMP1 (show TIMP1 Proteins), and NGAL (show LCN2 Proteins) (also MMP2 in 220 kDa complex) without proteolytic activity.
Data demonstrate for the first time that MMP2 and MMP9 (show MMP9 Proteins) are expressed in swine ovarian follicle both in theca and granulosa layers.
FiO2 used for resuscitation affects matrix metalloproteinases MMP-9 (show MMP9 Proteins) and MMP-2, caspase-3 (show CASP3 Proteins) and BDNF (show BDNF Proteins)
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 (show MMP14 Proteins) 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 (show CSF2 Proteins) barrier in vitro
The levels of matrix metalloproteinase-2 and matrix metalloproteinase-9 (show MMP9 Proteins) in the corpus luteum of swine during luteolysis are reported.
Hemodialysis graft placement leads to early increases in wall shear stress, VEGF-A (show VEGFA Proteins), pro-MMP-9 (show MMP9 Proteins), MMP-2, VEGFR-1 (show FLT1 Proteins), VEGFR-2 (show KDR Proteins), and TIMP-1 (show TIMP1 Proteins), 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 (show TNF Proteins) 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 (show DMD Proteins).
Castor oil polymer induces bone formation with high matrix metalloproteinase-2 expression.
MMP2 spinal cord expression is increased in cervical spondylotic myelopathy.
Ulinastatin (show AMBP Proteins) effectively inhibited the increased expression of MMP-2, MMP-3 (show MMP3 Proteins), and iNOS (show NOS2 Proteins) in degenerated NP cells induced by IL-1beta (show IL1B Proteins) in vitro.
Hemoperfusion could obviously reduce oxidative stress and the expression levels of MMP-2, MMP-9 (show MMP9 Proteins) and TIMP-1 (show TIMP1 Proteins) in rabbits with acute paraquat poisoning.
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)