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TIMP2 is a member of the TIMP gene family. Additionally we are shipping Metalloproteinase Inhibitor 2 Kits (82) and Metalloproteinase Inhibitor 2 Proteins (42) and many more products for this protein.
Showing 10 out of 265 products:
Human Monoclonal TIMP2 Primary Antibody for IF - ABIN396528
Alakus, Afriani, Warnecke-Eberz, Bollschweiler, Fetzner, Drebber, Metzger, Hölscher, Mönig: Clinical impact of MMP and TIMP gene polymorphisms in gastric cancer. in World journal of surgery 2010
Show all 5 references for ABIN396528
Human Polyclonal TIMP2 Primary Antibody for IF, ELISA - ABIN1533420
Hu, Cai, Hu, Patel, Bard, Jamison, Coling: Metalloproteinases and their associated genes contribute to the functional integrity and noise-induced damage in the cochlear sensory epithelium. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2012
Show all 2 references for ABIN1533420
Human Polyclonal TIMP2 Primary Antibody for ICC, IF - ABIN407863
Silva, Nascimento, Pereira, Siqueira, Brum, Jaeger, Miyabara: β2-Adrenoceptor is involved in connective tissue remodeling in regenerating muscles by decreasing the activity of MMP-9. in Cell and tissue research 2016
Show all 2 references for ABIN407863
Human Polyclonal TIMP2 Primary Antibody for IF (p), IHC (p) - ABIN668346
Fang, Wu, Huang: Raloxifene upregulated mesangial cell MMP-2 activity via ER-? through transcriptional regulation. in Cell biochemistry and biophysics 2013
Show all 2 references for ABIN668346
Pathogenesis and progression of nasal polyps is closely related with elevated MMP-9 (show MMP9 Antibodies) and suppressed TIMP-2 expression
our results demonstrate that TIMP-2 stimulates lung adenocarcinoma cell proliferation
new evidence that promoter polymorphisms in TIMP2 are functional and may affect gene transcription with possible effects on craniofacial development leading to NSCL (show NHLH1 Antibodies)/P.
This study shows that urinary [TIMP-2]*[IGFBP7 (show IGFBP7 Antibodies)] has a good diagnostic performance in predicting adverse outcomes in neonatal and pediatric AKI of heterogeneous etiology.
TIMP1 (show TIMP1 Antibodies), TIMP2, and TIMP4 (show TIMP4 Antibodies) are increased in aqueous humor from primary open angle glaucoma patients.
showed a significant association between the variants of MMP-2 (show MMP2 Antibodies) and TIMP-2 promoters and spontaneous intracerebral hemorrhage
TIMP2 is elevated in patients with non-alcoholic fatty liver disease.
TIMP-2 interaction with MT1-MMP (show MMP14 Antibodies) provides tumor cells with either pro- or anti-apoptotic signaling depending on the extracellular environment and apoptotic stimulus.
MiR (show MLXIP Antibodies)-761 directly targeted ING4 (show ING4 Antibodies) and TIMP2.
The invasive potential of CSCC (show CYP11A1 Antibodies) has been established to be substantially influenced by the increased expression of MMP-9 (show MMP9 Antibodies) and uPA (show PRAP1 Antibodies) and by the decreased expression of TIMP-2, as well as to a lesser extent by a change in MMP-2 (show MMP2 Antibodies) expression
Data indicate the involvement of PKC-alpha (show PKCa Antibodies) in proMMP-2 activation and inhibition of TIMP-2 expression by NF-kappaB (show NFKB1 Antibodies)-MT1-MMP (show MMP14 Antibodies)-dependent and -independent pathway.
A differential pattern of matrix metalloproteinase-2 (show MMP2 Antibodies) and Tissue inhibitor metalloproteinase-2 was observed in cow uteri with adenomyosis.
MMP-14 (show MMP14 Antibodies), MMP-2 (show MMP2 Antibodies) 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 (show MMP2 Antibodies), MMP14 (show MMP14 Antibodies), and the metallopeptidase (show ECEL1 Antibodies) inhibitor TIMP2 between different phases of the estrous cycle indicating an endocrine regulation.
Production of TIMP-1 (show TIMP1 Antibodies) was augmented by IL-1alpha, TNFalpha (show TNF Antibodies), and hepatocyte growth factor (show HGF Antibodies) at level of translation and was transcriptionally increased by 12-O-tetradecanoylphorbol 13-acetate. Level of TIMP-2 mRNA was not affected by any treatments.
the different temporal expression patterns of TIMP-1 (show TIMP1 Antibodies) and TIMP-2 suggest that TIMP-1 (show TIMP1 Antibodies) may be important for luteal formation and development, while TIMP-2 may play significant roles during luteal development and maintenance
Identification, purification and partial characterization of timp-2 in bovine pulmonary artery smooth muscle
Results describe the isolation of matrix metalloproteinase 2 (MMP-2 (show MMP2 Antibodies)) from the MMP-2 (show MMP2 Antibodies)/tissue inhibitor of metalloproteinase 2 (TIMP-2) complex, and the characterization of both isolated MMP-2 (show MMP2 Antibodies) and the complex itself.
oxidants inactivate TIMP-2, and the resulting activation of MMP-2 (show MMP2 Antibodies) subsequently inhibits Na+ dependent Ca2 (show CA2 Antibodies)+ uptake in the microsomes
TIMP-2 has a role in the pericyte-induced stabilization of newly formed vascular networks that are predisposed to undergo regression and reveal specific molecular targets of the inhibitors regulating these events.
The pathology of laminitis is associated with increased and lowered transcription of MMP-14 (show MMP14 Antibodies) and TIMP-2, respectively.
Further investigation of MMP2 (show MMP2 Antibodies) inhibitors of TIMP2/TIMP4 (show TIMP4 Antibodies) showed an upregulated TIMP2 expression, but not TIMP4 (show TIMP4 Antibodies). low-dose pre-radiation attenuates the skin inflammation and ROS (show ROS1 Antibodies) production induced by medium-dose UV radiation
TIMP2 and TIMP3 (show TIMP3 Antibodies) play fundamental and differential roles in mediating pathological remodelling, independent from their MMP-inhibitory function
Reduced beta(2)GP I plays a role in diabetic mice related to vascular protection, inhibiting vascular lipid deposition, and plaque formation by reducing MMPs/TIMPs expression through down-regulation of the p38MAPK (show MAPK14 Antibodies) signaling pathway.
High TIMP2 expression is associated with liver fibrosis.
TIMP2 promotes kidney injury through metalloproteinase (MMP)2 (show MMP2 Antibodies) activation
Gene expression of Mmp-12 (show MMP12 Antibodies) and Mmp-13 (show MMP13 Antibodies), and Timp-1 (show TIMP1 Antibodies) was strongly upregulated at all time points in RD compared with controls. Timp-2, Mmp-2 (show MMP2 Antibodies), and Mmp-9 (show MMP9 Antibodies) expression was modest.
Data indicate a significantly increased expression of type I collagen, TIMP-2, TGF-beta (show TGFB1 Antibodies), PAI-1 (show SERPINE1 Antibodies) and RAGE (show AGER Antibodies) in diabetic db/db (show LEPR Antibodies) cells.
This study suggests that miR-17 participates in the regulation of cardiac matrix remodeling and provides a novel therapeutic approach using miR-17 inhibitors to prevent remodeling and heart failure after MI.
In neural stem cells, TIMP-2 acts as key effector of the proneurogenic response to inducing stimuli such as Marimastat.
Spread of Lewis lung carcinoma cells from serum to lungs was associated with increased serum content of TIMP-1 (show TIMP1 Antibodies) and TIMP-2.
To further study the function of TIMP-2 in development, we utilized zebrafish as an experimental model system
membrane-type 1 metalloproteinase, gelatinase A (show MMP2 Antibodies) , and tissue inhibitor 2 of metalloproteinases mRNA transcripts were expressed in the blastema
This gene is a member of the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix. In addition to an inhibitory role against metalloproteinases, the encoded protein has a unique role among TIMP family members in its ability to directly suppress the proliferation of endothelial cells. As a result, the encoded protein may be critical to the maintenance of tissue homeostasis by suppressing the proliferation of quiescent tissues in response to angiogenic factors, and by inhibiting protease activity in tissues undergoing remodelling of the extracellular matrix.
, metalloproteinase inhibitor 2
, tissue inhibitor of metalloproteinase 2
, tissue inhibitor of metalloproteinases 2
, collagenase inhibitor
, tissue inhibitor of mettaloproteinase 2
, tissue inhibitor of metalloproteinase-2
, tissue inhibitor of matrix metalloproteinase-2
, metalloproteinase inhibitor TIMP-2