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TIMP3 belongs to the TIMP gene family. Additionally we are shipping TIMP3 Antibodies (191) and TIMP3 Kits (106) and many more products for this protein.
Showing 10 out of 20 products:
native glycosaminoglycans interact with TIMP-3.
The expression level of LIPC (show LIPC Proteins), SLC16A8, and TIMP-3 was significantly associated with age-related macular degeneration pathology.
Levels of miR (show MLXIP Proteins)-221/222 are associated negatively with estrogen receptor (show ESR1 Proteins) in in situ tumors and positively with tissue inhibitor of metalloproteinase 3 TIMP3 messenger RNA expression levels in pure invasive breast cancers.
Electrostatic potential calculations suggested a competition between negatively charged GAGs and highly negatively charged complement-like domains of LRP-1 (show LRP1 Proteins) for the binding to a positively charged area of TIMP-3 as an underlying mechanism.
TIMP3 overexpression after myocardial infarction improves myocardial structural remodeling and function by promoting angiogenesis and inhibiting early proteolysis.
Single Nucleotide Variants of Candidate Genes in Aggrecan (show ACAN Proteins) Metabolic Pathway Are Associated with Lumbar Disc Degeneration and Modic Changes
Our data suggest that miR (show MLXIP Proteins)-206 may function as an inflammatory regulator and drive the expression of MMP9 (show MMP9 Proteins) in M.tb-infected THP-1 cells by targeting TIMP3, indicating that miR (show MLXIP Proteins)-206 is a potential therapeutic target for patients with TB.
Plasma TIMP3 is a biomarker for predicting the tumor stage in patients with oral squamous cell carcinoma .
TIMP-3 K26A/K45A retained higher affinity for sulfated (show SULF1 Proteins) glycosaminoglycans than K42A/K110A and exhibited increased affinity for ADAMTS-5 (show ADAMTS5 Proteins) in the presence of heparin.
Of the 225 genetic tests performed, 150 were for recessive IRD, and 75 were for dominant IRD. A positive molecular diagnosis was made in 70 (59%) of probands with recessive IRD and 19 (26%) probands with dominant IRD. Thirty-two novel variants were identified; among these, 17 sequence changes in four genes were predicted to be possibly or probably damaging including: ABCA4 (show ABCA4 Proteins) (14), BEST1 (show BEST1 Proteins) (2), PRPH2 (show PRPH2 Proteins) (1), and TIMP3
Circulating smoke components, including acrolein, contribute to vascular diseases through enhanced MMP-1 (show MMP1 Proteins) and decreased TIMP-3 secretion.
TIMP-3 is downregulated in a distinct subpopulation of atherosclerotic foam cells which have increased MMP-14 (show MMP14 Proteins).
Reactive oxygen species mediate TGF-beta1 (show TGFB1 Proteins)-induced TIMP-3 gene expression
TIMP3 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.
TIMP3 mRNA expression level was upregulated by multidirectional articular motion.
only the N-terminal, but not the C-terminal domain of TIMP-3, results in developmental defects.
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, are elevated during periods of cell death and proliferation
In a clinically relevant CADASIL (show NOTCH3 Proteins) mouse model, we show that exogenous ADAM17 (show ADAM17 Proteins) or HB-EGF (show HBEGF Proteins) restores cerebral arterial tone and blood flow responses, and identify upregulated voltage-dependent potassium channel (show KCNAB2 Proteins) (KV) number in cerebral arterial myocytes as a heretofore-unrecognized downstream effector of TIMP3-induced deficits.
TIMP3 promotes normal microvascular endothelial cell barrier function, at least partially, through inhibition of metalloproteinase-dependent disruption of adherens junctions, and septic downregulation of TIMP3 may contribute to septic MVEC barrier dysfunction.
data strongly suggest that TIMP3 has direct neuroprotective effects that can mitigate the deleterious effects associated with TBI, an area with few if any therapeutic options.
Elevated levels of TIMP3 and vitronectin, acting downstream of Notch3(ECD) deposition, play a role in CADASIL, producing divergent influences on early CBF deficits and later white matter lesions.
4-Hydroxyisoleucine improved insulin (show INS Proteins) resistant-like state in 3T3-L1 adipocytes by targeting TACE (show ADAM17 Proteins)/TIMP3 and the insulin (show INS Proteins) signaling pathway.
In a mouse model of prostate cancer, increased tumor growth, proliferation index, increased microvascular density, and invasion was observed in Pten(-/-), Timp3(-/-) prostate tumors compared to Pten(-/-), Timp3(+/+) tumors.
Timp3 status determines p53 (show TP53 Proteins), p38 (show CRK Proteins) and Notch (show NOTCH1 Proteins) coactivation to instruct hepatic cell fate and transformation.
TIMP2 (show TIMP2 Proteins) and TIMP3 play fundamental and differential roles in mediating pathological remodelling, independent from their MMP-inhibitory function
Expansion of stem cells counteracts age-related mammary regression in compound Timp1 (show TIMP1 Proteins)/Timp3-deficient mice.
lack of TIMP3 increases inflammation and polarizes macrophages towards a more inflammatory phenotype resulting in increased atherosclerosis.
These results suggest the crucial role of TIMP-3 in successful implantation and embryo survival and indicate the endometrial stromal decidualization-like in pigs.
This gene belongs to the TIMP gene family. The proteins encoded by this gene family are inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix (ECM). Expression of this gene is induced in response to mitogenic stimulation and this netrin domain-containing protein is localized to the ECM. Mutations in this gene have been associated with the autosomal dominant disorder Sorsby's fundus dystrophy.
metalloproteinase inhibitor 3
, TIMP metallopeptidase inhibitor 3 (Sorsby fundus dystrophy, pseudoinflammatory)
, tissue inhibitor metalloproteinase-3
, TIMP metallopeptidase inhibitor 3
, Metalloproteinase inhibitor 3
, MIG-5 protein
, protein MIG-5
, tissue inhibitor of metalloproteinases 3
, tissue inhibitor of metalloproteinase-3
, tissue inhibitor of metalloproteinase 3 (Sorsby fundus dystrophy, pseudoinflammatory)
, tissue inhibitor of metalloproteinase 3
, 21 kDa protein of extracellular matrix
, tissue inhibitor of metalloproteinases-3