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TIMP2 is a member of the TIMP gene family. Additionally we are shipping Metalloproteinase Inhibitor 2 Antibodies (264) and Metalloproteinase Inhibitor 2 Kits (77) and many more products for this protein.
Showing 10 out of 43 products:
Human TIMP2 Protein expressed in HEK-293 - ABIN2666719
Bourboulia, Stetler-Stevenson: Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs): Positive and negative regulators in tumor cell adhesion. in Seminars in cancer biology 2010
Show all 5 references for ABIN2666719
Human TIMP2 Protein expressed in Human Cells - ABIN2002769
Seo, Li, Guedez, Wingfield, Diaz, Salloum, Wei, Stetler-Stevenson: TIMP-2 mediated inhibition of angiogenesis: an MMP-independent mechanism. in Cell 2003
Show all 3 references for ABIN2002769
Human TIMP2 Protein expressed in HEK-293 Cells - ABIN2181824
Stetler-Stevenson, Krutzsch, Liotta: Tissue inhibitor of metalloproteinase (TIMP-2). A new member of the metalloproteinase inhibitor family. in The Journal of biological chemistry 1989
Show all 3 references for ABIN2181824
Human TIMP2 Protein expressed in Escherichia coli (E. coli) - ABIN1098377
Bahudhanapati, Zhang, Sidhu, Brew: Phage display of tissue inhibitor of metalloproteinases-2 (TIMP-2): identification of selective inhibitors of collagenase-1 (metalloproteinase 1 (MMP-1)). in The Journal of biological chemistry 2011
Show all 2 references for ABIN1098377
Human TIMP2 Protein expressed in Escherichia coli (E. coli) - ABIN1047368
Stetler-Stevenson, Brown, Onisto, Levy, Liotta: Tissue inhibitor of metalloproteinases-2 (TIMP-2) mRNA expression in tumor cell lines and human tumor tissues. in The Journal of biological chemistry 1990
Show all 2 references for ABIN1047368
significant differences were detected concerning the activity of TIMPs resulting in a negative correlation of TIMP1 (show TIMP1 Proteins) activity with MMP2 (show MMP2 Proteins) activity (p = 0.044) and negative correlations of TIMP2 and TIMP3 (show TIMP3 Proteins) with MMP9 (show MMP9 Proteins) activity
quantitative urine test is available to assess the risk of developing AKI by measuring the concentrations of two protein biomarkers, TIMP-2 and IGFBP-7 (show IGFBP7 Proteins)
Here we report isothermal titration calorimetric studies of the effects of selectivity-modifying mutations in NTIMP1 and NTIMP2 on the thermodynamics of their interactions with MMP1 (show MMP1 Proteins), MMP3 (show MMP3 Proteins), and MMP14 (show MMP14 Proteins).
miR (show MLXIP Proteins)-22 significantly upregulated the invasion capacity of 1321N1 cells. In silico analysis predicted that TIMP2 is a target gene of miR (show MLXIP Proteins)-22 which was confirmed by qPCR and Western blotting. Luciferase reporter assays demonstrated that miR (show MLXIP Proteins)-22 directly bound the 3'-untranslated regions of TIMP2. These data suggest that miR (show MLXIP Proteins)-22 acts to regulate invasion of 1321N1 astrocytoma cells by targeting TIMP2 expression.
The expression levels MMP-9 (show MMP9 Proteins), TIMP-1 (show TIMP1 Proteins), and TIMP-2 in both marrow plasma and culture supernatants were significantly higher in MM patients than controls.
Pathogenesis and progression of nasal polyps is closely related with elevated MMP-9 (show MMP9 Proteins) 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 Proteins)/P.
This study shows that urinary [TIMP-2]*[IGFBP7 (show IGFBP7 Proteins)] has a good diagnostic performance in predicting adverse outcomes in neonatal and pediatric AKI of heterogeneous etiology.
TIMP1 (show TIMP1 Proteins), TIMP2, and TIMP4 (show TIMP4 Proteins) are increased in aqueous humor from primary open angle glaucoma patients.
Data indicate the involvement of PKC-alpha (show PKCa Proteins) in proMMP-2 activation and inhibition of TIMP-2 expression by NF-kappaB (show NFKB1 Proteins)-MT1-MMP (show MMP14 Proteins)-dependent and -independent pathway.
A differential pattern of matrix metalloproteinase-2 (show MMP2 Proteins) and Tissue inhibitor metalloproteinase-2 was observed in cow uteri with adenomyosis.
MMP-14 (show MMP14 Proteins), MMP-2 (show MMP2 Proteins) 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 Proteins), MMP14 (show MMP14 Proteins), and the metallopeptidase (show ECEL1 Proteins) inhibitor TIMP2 between different phases of the estrous cycle indicating an endocrine regulation.
Production of TIMP-1 (show TIMP1 Proteins) was augmented by IL-1alpha, TNFalpha (show TNF Proteins), and hepatocyte growth factor (show HGF Proteins) 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 Proteins) and TIMP-2 suggest that TIMP-1 (show TIMP1 Proteins) 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 Proteins)) from the MMP-2 (show MMP2 Proteins)/tissue inhibitor of metalloproteinase 2 (TIMP-2) complex, and the characterization of both isolated MMP-2 (show MMP2 Proteins) and the complex itself.
oxidants inactivate TIMP-2, and the resulting activation of MMP-2 (show MMP2 Proteins) subsequently inhibits Na+ dependent Ca2 (show CA2 Proteins)+ 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 Proteins) and TIMP-2, respectively.
demonstrate that TIMP-2 plays a greater protective role than TIMP-1 (show TIMP1 Proteins) during the pathogenesis of atherosclerosis
Further investigation of MMP2 (show MMP2 Proteins) inhibitors of TIMP2/TIMP4 (show TIMP4 Proteins) showed an upregulated TIMP2 expression, but not TIMP4 (show TIMP4 Proteins). low-dose pre-radiation attenuates the skin inflammation and ROS (show ROS1 Proteins) production induced by medium-dose UV radiation
TIMP2 and TIMP3 (show TIMP3 Proteins) 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 Proteins) signaling pathway.
High TIMP2 expression is associated with liver fibrosis.
TIMP2 promotes kidney injury through metalloproteinase (MMP)2 (show MMP2 Proteins) activation
Gene expression of Mmp-12 (show MMP12 Proteins) and Mmp-13 (show MMP13 Proteins), and Timp-1 (show TIMP1 Proteins) was strongly upregulated at all time points in RD compared with controls. Timp-2, Mmp-2 (show MMP2 Proteins), and Mmp-9 (show MMP9 Proteins) expression was modest.
Data indicate a significantly increased expression of type I collagen, TIMP-2, TGF-beta (show TGFB1 Proteins), PAI-1 (show SERPINE1 Proteins) and RAGE (show AGER Proteins) in diabetic db/db (show LEPR Proteins) 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.
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 Proteins) , 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