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Human MMP 9 Protein expressed in Human Cells - ABIN2002581
Opdenakker, Van den Steen, Dubois, Nelissen, Van Coillie, Masure, Proost, Van Damme: Gelatinase B functions as regulator and effector in leukocyte biology. in Journal of leukocyte biology 2001
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Rat (Rattus) MMP 9 Protein expressed in Human Cells - ABIN3218785
Belotti, Paganoni, Manenti, Garofalo, Marchini, Taraboletti, Giavazzi: Matrix metalloproteinases (MMP9 and MMP2) induce the release of vascular endothelial growth factor (VEGF) by ovarian carcinoma cells: implications for ascites formation. in Cancer research 2003
Show all 5 Pubmed References
Our findings indicate that overexpression of MMP-9 rescued insulin (show INS Proteins) survival signaling in vitro and in early stages in the 5XFAD model of AD.
Review/Meta-analysis: Matrix metalloproteinase-9 has high predictive value for hemorrhagic transformation after acute ischemic stroke.
In dilation cardiomyopathy, expression of MMP-2 (show MMP2 Proteins), MMP-9, and TIMP-1 (show TIMP1 Proteins) and their ratios in autopsy material and in cultures was elevated by 1.5-9 times.
The expression of MMP-9 is associated with clinical outcome in chondrosarcoma.
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 (show MMP2 Proteins) and MMP-9 enzymatic activities through STAT3 (show STAT3 Proteins) signaling. Increased MMP-9 activity by OSM (show OSM Proteins) seems to be more important in primary trophoblasts.
MMP-9 levels in the tumor tissue extracts had also increased significantly
MMP-9 -1562 C/T polymorphism might be related to the digestive cancer susceptibility [meta-analysis]
MMP-9 protein overexpression was found in prostate cancers, low expression in any of the normal tissues or in benign prostatic tissue
Hypoxia promotes retinoblastoma cell line HXO-RB44 invasion by activating HIF-1alpha (show HIF1A Proteins)/MMP9 signaling pathway.
There was no difference found in MMP-2 (show MMP2 Proteins), MMP-9 or TLR-4 (show TLR4 Proteins) levels between non-thrombocytopenic and thrombocytopenic septic donors. PLA formation was increased in thrombocytopenic patients.
In the initial periods of AP progression, an increased expression of MMP9 in the TLR2 KO and MyD88 (show MYD88 Proteins) KO mice was observed. In the final periods of AP progression, a reduction of MMP2 (show MMP2 Proteins) expression and an increase of MMP9 expression in the TLR2 KO mice were observed. MMP2 (show MMP2 Proteins) and MMP9 production was modulated for TLR2 and MyD88 (show MYD88 Proteins) during apical periodontitis progression
Our data suggest that MMP-9 deficiency does not result in major abnormalities in the development of any conventionally selected or agonist selected subsets and does not interfere with thymocyte apoptosis and clearance, and that MMP-9 expression is not induced in immature T cells at any stage of their thymic development.
analysis of Foxn1 (show FOXN2 Proteins) and Mmp-9 expression in the intact and postinjured skin of young, adult, and old C57BL/6J and transgenic Foxn1 (show FOXN2 Proteins)::Egfp mice
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.
Myocardial MMP-9 inhibition prevents ventricular arrhythmia through pleiotropic effects, including the modulation of calcium homeostasis and reduced calcium leakage.
results first identified the role of SNX10 (show SNX10 Proteins) in MMP9 trafficking and secretion, and provided an evidence for SNX10 (show SNX10 Proteins) as a possible therapeutic target for bone destructing disease.
Thus, the light reintroduction-induced increase in MMP-9 removes constraints on structural and functional plasticity in the mature cortex.
the ZnT3 (show Slc30a3 Proteins) null state removed synaptic zinc, it rather increased free zinc in the cytosol of brain cells, which appeared to increase MMP-9 activity and BDNF (show BDNF Proteins) levels. The present results suggest that zinc dyshomeostasis during the critical period of brain development may be a possible contributing mechanism for ASD (show GUSB Proteins).
MMP-9 activation by hypoxia requires LRP1 (show LRP1 Proteins) and Pyk2 (show PTK2B Proteins) phosphorylation in fibroblasts.
Aneurysmal-prone factors induced HIF-1alpha (show HIF1A Proteins) can cause overexpression of MMP-2 (show MMP2 Proteins) and MMP-9 and promote aneurysmal progression.
Results provide evidence for the utility of MMP9 and TIMP1 (show TIMP1 Proteins) as markers of age- and lactocrine-sensitive porcine female reproductive tract development.
Increased MMP-9 expression is associated with carotid atherosclerotic plaque.
Increased expression of MMP-9 is associated with intraplaque hemorrhage in a swine model of vulnerable carotid atherosclerosis
we demonstrated the presence of high molecular weight (HMW) complexes (130, 170, and 220 kDa) containing MMP9, TIMP1 (show TIMP1 Proteins), and NGAL (show LCN2 Proteins) (also MMP2 (show MMP2 Proteins) in 220 kDa complex) without proteolytic activity.
Data demonstrate for the first time that MMP2 (show MMP2 Proteins) 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 (show MMP2 Proteins), caspase-3 (show CASP3 Proteins) and BDNF (show BDNF Proteins)
Oxygen for newborn resuscitation increases MMP-2 (show MMP2 Proteins)/-9 activity resulting in tissue damage and influencing remodeling processes.
contribution of MMPs to the inflammatory breakdown of the blood-CSF (show CSF2 Proteins) barrier in vitro
The levels of matrix metalloproteinase-2 (show MMP2 Proteins) and matrix metalloproteinase-9 (MMP-9)in the corpus luteum of swine during luteolysis are reported.
Our data define pericyte interactions as a main inducer of endothelial MMP secretion and propose a new role for pericyte-endothelial cell crosstalk at the BBB in vitro
In diabetic retinopathy transcription of MMP-9 is regulated by AP-1 binding at both, proximal and distal sites of its promoter, and acetylation of c-Jun and c-Fos subunits is important in its regulation.
These data demonstrate that serum neutrophil haptoglobin (show HP Proteins)-MMP 9 complexes appear sooner and decline more rapidly than other acute phase proteins.
Activation of cytosolic MMP-9 and MMP-2 (show MMP2 Proteins) was investigated in the retinal endothelial cells incubated in high glucose for 6-96 h, and correlated with their mitochondrial accumulation and mitochondrial damage.
Role of TGF-beta1 (show TGFB1 Proteins) and TNF-alpha (show TNF Proteins) in IL-1beta (show IL1B Proteins) mediated activation of proMMP-9 in pulmonary artery smooth muscle cells: involvement of an aprotinin sensitive protease.
Decreased MMP-9 and increased TIMP-1 (show TIMP1 Proteins) expression were found in peripheral blood cells from Mycobacterium avium subsp. paratuberculosis (Map)-infected cattle after stimulation with Map lysate and Map purified protein derivative than in control cattle.
We used a trophoblast cell line (F3) derived from bovine placentomes to examine the influence of EGF (show EGF Proteins) on MMP-9 and TIMP-1 (show TIMP1 Proteins) expression by semiquantitative RT-PCR and MMP activity by zymography.
results suggest a significant role of matrix metalloproteinase-2 (show MMP2 Proteins) and-9 in growth and development of bovine follicle
Cells constitutively produced proMMP-9 and proMMP-2, and treatment with TNFalpha (show TNF Proteins), hepatocyte growth factor (show HGF Proteins), 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
Results suggest that MMP-2 (show MMP2 Proteins), MMP-9, and TIMP-2 (show TIMP2 Proteins) mRNAs are expressed in bovine placentomes during the gestational and postpartum periods and that these enzymes, in conjunction with steroidogenic enzymes, mediate fetal membrane detachment after parturition.
Mmp9 is dispensable for Hematopoietic stem cells budding, and is required for proper colonization of secondary niches.
The findings of this study suggest that Mmp-9 is a protective molecule against infection by Listeria monocytogenes by engaging in migration of zebrafish macrophages to the site of infection via a non-proteolytic role.
elevated beta-oxidation-fuelled mitochondria-derived reactive oxygen species within epidermal cells helps guide matrix metalloproteinase-driven leukocyte recruitment.
Mmp9 regulates both acute and chronic tissue damage and plays an essential role in collagen reorganization during wound repair.
MeHg impairs tail development at least partially by activation of the tissue remodeling proteases Mmp9 and Mmp13 (show MMP13 Proteins).
study identified mechanism by which mycobacteria induce granulomas: ESAT-6 induced MMP9 in epithelial cells neighboring infected macrophages; MMP9 enhanced recruitment of macrophages, which contributed to nascent granuloma maturation & bacterial growth
From 24h post fertilization, mmp9 expression was detected in a population of circulating white blood cells.
expression and activity of MMP-2 (show MMP2 Proteins) and MMP-9 in the embryonic zebrafish.
The MMP-9 gene was duplicated and differentiated into two genes, one was specialized in a common ancestor of X. laevis and X. tropicalis expressed in degenerating and remodeling organs in response to thyroid hormone (show PTH Proteins) during metamorphosis.
MMP-9TH is responsible in the larval epithelial apoptosis through degrading ECM (show MMRN1 Proteins) components in the basal lamina, whereas MMP-9 is involved in the removal of dying epithelial cells during amphibian intestinal remodeling
metamorphic tail and intestine RNA levels of TIMP-2 (show TIMP2 Proteins), MT1-MMP (show MMP14 Proteins) and Gel-A, but not MT3-MMP (show MMP24 Proteins) or TIMP-3 (show TIMP3 Proteins), are elevated during periods of cell death and proliferation
Expression of MMP-9 increased after cerebral aneurysm induction, peaking at week 3, leading to reduced smooth muscle cell number, damaged endothelial cells, and damage to the aneurysm wall elastic layer.
Inflammatory factors such as TNF-alpha (show TNF Proteins) can stimulate MMP-2 (show MMP2 Proteins)/9 activity in corneal epithelium cells. This may be a potential manipulating mechanism of MMP expression in the pathogenesis of corneal diseases
Therefore, it was reasonable to speculate that the increased expression of VEGF (show VEGFA Proteins) and MMP-9 in residual hepatic tumor cells and tumor angiogenesis post-embolization would be responsible for the increased metastatic potentiality and invasiveness.
Performing minimally invasive surgical procedures in the early stages of intracerebral hemorrhage significantly decreases MMP-9.
Increased expression of MMP-9 in spinal cord follows cervical spondylotic myelopathy.
Hemoperfusion could obviously reduce oxidative stress and the expression levels of MMP-2 (show MMP2 Proteins), MMP-9 and TIMP-1 (show TIMP1 Proteins) in rabbits with acute paraquat poisoning.
In experimental syringomyelia, MMP-9 plays an important role in causing edema in the presyrinx state.
Tongxinluo can inhibit the expression of MMP-3 (show MMP3 Proteins) and 9 and increase the expression of PPARgamma (show PPARG Proteins) in atherosclerotic rabbits.
TGF-beta (show TGFB1 Proteins) mediated MMP-9 induction may be regulated by the NF-kappaB (show NFKB1 Proteins), Smad3 (show SMAD3 Proteins), and JNK (show MAPK8 Proteins) pathways, whereas the IL-1beta (show IL1B Proteins) mediated induction may be regulated by the NF-kappaB (show NFKB1 Proteins) and p38 (show MAPK14 Proteins) pathways.
The results showed that MMP-2 (show MMP2 Proteins), MMP-9, and StAR were significantly expressed in the granulosa and thecal cells of the ovarian atretic follicles during proestrus, and were strongly expressed in the corpus luteum during metestrus.
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. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling.
92 kDa gelatinase
, 92 kDa type IV collagenase
, macrophage gelatinase
, matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
, matrix metalloproteinase-9
, type V collagenase
, 92kD gelatinase
, 92kD type IV collagenase
, 92kDa gelatinase
, 92kDa type IV collagenase
, Gel B
, collagenase type IVB
, gelatinase B
, matrix metalloproteinase 9
, 92-kDa type IV collagenase
, matrix metalloproteinase 9 (gelatinase B 92-kDa type IV collagenase)
, matrix metalloproteinase 9 (gelatinase B, 92-kDa type IV collagenase)
, type IV collagenase MMP-9
, Matrix metalloproteinase-9
, matrix metalloproteinase 9 (gelatinase B, 92kDa matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
, 75 kDa gelatinase