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TIMP1 belongs to the TIMP gene family. Additionally we are shipping TIMP1 Kits (139) and TIMP1 Proteins (61) and many more products for this protein.
Showing 10 out of 306 products:
Human Monoclonal TIMP1 Primary Antibody for ELISA (Capture), FACS - ABIN4899800
Li, Hou, Shao, Tang, Li: The DSCs-expressed CD82 controls the invasiveness of trophoblast cells via integrinbeta1/MAPK/MAPK3/1 signaling pathway in human first-trimester pregnancy. in Biology of reproduction 2010
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Human Polyclonal TIMP1 Primary Antibody for IHC (p), WB - ABIN3044394
Jiang, Han, Li, Yang, Liu: Carboxymethyl chitosan represses tumor angiogenesis in vitro and in vivo. in Carbohydrate polymers 2015
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Human Polyclonal TIMP1 Primary Antibody for IF (cc), IF (p) - ABIN668331
Sassoli, Nosi, Tani, Chellini, Mazzanti, Quercioli, Zecchi-Orlandini, Formigli: Defining the role of mesenchymal stromal cells on the regulation of matrix metalloproteinases in skeletal muscle cells. in Experimental cell research 2014
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Cow (Bovine) Polyclonal TIMP1 Primary Antibody for IHC, ELISA - ABIN1582210
Pitteri, Kelly-Spratt, Gurley, Kennedy, Buson, Chin, Wang, Zhang, Wong, Chodosh, Nelson, Hanash, Kemp: Tumor microenvironment-derived proteins dominate the plasma proteome response during breast cancer induction and progression. in Cancer research 2011
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Human Polyclonal TIMP1 Primary Antibody for EIA, WB - ABIN453420
Safranek, Pesta, Holubec, Kulda, Dreslerova, Vrzalova, Topolcan, Pesek, Finek, Treska: Expression of MMP-7, MMP-9, TIMP-1 and TIMP-2 mRNA in lung tissue of patients with non-small cell lung cancer (NSCLC) and benign pulmonary disease. in Anticancer research 2009
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Human Polyclonal TIMP1 Primary Antibody for FACS, IF - ABIN390664
Wu, Wang, Guo, Ye, Wang, Yuan, Yao, Shang: A lipoxin A4 analog ameliorates blood-brain barrier dysfunction and reduces MMP-9 expression in a rat model of focal cerebral ischemia-reperfusion injury. in Journal of molecular neuroscience : MN 2012
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Human Monoclonal TIMP1 Primary Antibody for ICC, IF - ABIN261639
Jurga, Piotrowska, Makuch, Przewlocka, Mika: Blockade of P2X4 Receptors Inhibits Neuropathic Pain-Related Behavior by Preventing MMP-9 Activation and, Consequently, Pronociceptive Interleukin Release in a Rat Model. in Frontiers in pharmacology 2017
Human Monoclonal TIMP1 Primary Antibody for FACS - ABIN4896673
Domeij, Modéer, Quezada, Yucel-Lindberg: Cell expression of MMP-1 and TIMP-1 in co-cultures of human gingival fibroblasts and monocytes: the involvement of ICAM-1. in Biochemical and biophysical research communications 2005
Human Polyclonal TIMP1 Primary Antibody for EIA, IF - ABIN955221
Lin, Yang, Chung, Lee: Functional polymorphisms in matrix metalloproteinases-1, -3, -9 are associated with arteriovenous fistula patency in hemodialysis patients. in Clinical journal of the American Society of Nephrology : CJASN 2010
This study indicates that in our population, the COL4A3 (show COL4a3 Antibodies) rs55703767 polymorphism decreased the risk of KC. However, the TIMP-1 rs6609533 polymorphism was associated with an increased risk of KC.
Low MMP-8 (show MMP8 Antibodies)/TIMP-1 reflects left ventricle impairment in takotsubo cardiomyopathy and high TIMP-1 may help to differentiate it from acute coronary syndrome
Data show that the mean values for TIMP1, TIMP2 (show TIMP2 Antibodies) and MMP2 (show MMP2 Antibodies) were lower in survivors, MMP9 (show MMP9 Antibodies) was higher in survivors.
We conclude that in the resected esophageal cancer an increased mRNA expression of MMP-7 (show MMP7 Antibodies), MMP-10 (show MMP10 Antibodies) and TIMP-1 correlated with clinicopathologic features. We suggest that these genes may play a role during progression of the diseaseMMP-10, MMP-7 (show MMP7 Antibodies), TIMP-1, TIMP-2 (show TIMP2 Antibodies) were overexpressed in 73%, 85%, 55% and 42% of esophageal cancer samples, respectively.
plasma concentrations of MMP-7 (show MMP7 Antibodies), MMP-8 (show MMP8 Antibodies), -9 and TIMP-1 within 96 h from the onset of acute pancreatitis symptoms are elevated in acute pancreatitis patients compared with healthy controls
High TIMP1 expression is associated with hepatic fibrosis.
TIMP-1 was highly expressed in TNBC patients and was associated with a poor prognosis.
Results suggest a crucial role of MMP9 (show MMP9 Antibodies) at the early stage of carcinogenesis in the large intestine. The increase in MMP9 (show MMP9 Antibodies) and TIMP1 mRNA concentration and the decrease in MMP28 (show MMP28 Antibodies) in the large intestinal tissue may be a confirmation of cancer.
Expression of TIMP1 is i (show CD63 Antibodies)ncreased in chronic pancreatitis, pancreatic intra-epithelial neoplasia, and pancreatic ductal adenocarcinoma tissues from patients. TIMP1 signaling via CD63 leads to activation of hepatic stellate cells, which create an environment in the liver that increases its susceptibility to pancreatic tumor cells.
Our study provides information on the dynamic changes of MMP-9 (show MMP9 Antibodies)-TIMP-1 system and S100B (show S100B Antibodies) in the perioperative period. Preoperative reduction of TIMP-1 might be predictive for shunt requirement but future studies are required for verification.
Decreased MMP-9 (show MMP9 Antibodies) and increased TIMP-1 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 Antibodies) on MMP-9 (show MMP9 Antibodies) and TIMP-1 expression by semiquantitative RT-PCR and MMP activity by zymography.
Production of TIMP-1 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 (show TIMP2 Antibodies) mRNA was not affected by any treatments.
the different temporal expression patterns of TIMP-1 and TIMP-2 (show TIMP2 Antibodies) suggest that TIMP-1 may be important for luteal formation and development, while TIMP-2 (show TIMP2 Antibodies) may play significant roles during luteal development and maintenance
analysis of species specificity of human and bovine TIMP-1 binding to mouse TIMP-1 receptor
we demonstrated the presence of high molecular weight (HMW) complexes (130, 170, and 220 kDa) containing MMP9 (show MMP9 Antibodies), TIMP1, and NGAL (show LCN2 Antibodies) (also MMP2 (show MMP2 Antibodies) in 220 kDa complex) without proteolytic activity.
Hemodialysis graft placement leads to early increases in wall shear stress, VEGF-A (show VEGFA Antibodies), pro-MMP-9 (show MMP9 Antibodies), MMP-2 (show MMP2 Antibodies), VEGFR-1 (show FLT1 Antibodies), VEGFR-2 (show KDR Antibodies), and TIMP-1, which may contribute to the development of venous stenosis.
Results indicate that leukemia inhibitory factor (LIF (show LIF Antibodies)) and Oncostatin M (show OSM Antibodies) increase the expression of MMP-1 (show MMP1 Antibodies), MMP-3 (show MMP3 Antibodies), and TIMP-1 several fold, and that their expression is reduced to basal levels in the presence of the LIF (show LIF Antibodies) antagonist MH35-BD.
Hemoperfusion could obviously reduce oxidative stress and the expression levels of MMP-2 (show MMP2 Antibodies), MMP-9 (show MMP9 Antibodies) and TIMP-1 in rabbits with acute paraquat poisoning.
proteomic analysis of the mesenchymal stem cells secretome identified the TIMP-1 as a potential effector molecule responsible for the anti-angiogenic properties of MSC (show MSC Antibodies)
TIMP1 signaling via CD63 (show CD63 Antibodies) leads to activation of hepatic stellate cells, which create an environment in the liver that increases its susceptibility to pancreatic tumor cells.
This study highlights a previously undescribed integral role for TIMP1 in both vascular network maturation and adaptations to ischemia or alterations in flow.
TIMP-1 was identified as a selectively upregulated component secreted from immature astrocytes from human pluripotent stem cells.
demonstrate that TIMP-2 (show TIMP2 Antibodies) plays a greater protective role than TIMP-1 during the pathogenesis of atherosclerosis
Our findings reveal that elevated levels of TIMP-1 impact on neutrophil homeostasis via signaling through CD63 (show CD63 Antibodies).
TIMP-1 is a ligand of LRP-1 (show LRP1 Antibodies) and we highlight a new example of its MMP-independent, cytokine-like functions.
RAB37 (show RAB37 Antibodies) regulates the exocytosis of TIMP1 in a nucleotide-dependent manner to inactivate MMP9 (show MMP9 Antibodies) migration axis in vitro and in vivo and to suppress tumor metastasis.
PDGF-D (show PDGFD Antibodies) intensifies fibrogenesis by interfering with the fibrolytic activity of the TIMP-1/MMP-2 (show MMP2 Antibodies)/MMP (show MMP2 Antibodies)-9 (show MMP9 Antibodies) system, and PDGF-D (show PDGFD Antibodies) signaling is mediated through both PDGF (show PDGFA Antibodies)-alpha and -beta receptors.
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.
This gene belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases (MMPs), a group of peptidases involved in degradation of the extracellular matrix. In addition to its inhibitory role against most of the known MMPs, the encoded protein is able to promote cell proliferation in a wide range of cell types, and may also have an anti-apoptotic function. Transcription of this gene is highly inducible in response to many cytokines and hormones. In addition, the expression from some but not all inactive X chromosomes suggests that this gene inactivation is polymorphic in human females. This gene is located within intron 6 of the synapsin I gene and is transcribed in the opposite direction.
tissue inhibitor of matrix metalloproteinase-1
, TIMP metallopeptidase inhibitor 1
, Metalloproteinase inhibitor 1
, collagenase inhibitor
, erythroid potentiating activity
, erythroid-potentiating activity
, fibroblast collagenase inhibitor
, metalloproteinase inhibitor 1
, tissue inhibitor of metalloproteinases 1
, tissue inhibitor of metalloproteinase 1 (erythroid potentiating activity, collagenase inhibitor)
, tissue inhibitor of metallopeptidase 1
, tissue inhibitor of metalloproteinase 1
, metalloproteinase tissue inhibitor
, metalloproteinase tissue inhibitor 1
, TPA-induced protein
, collagenase inhibitor 16C8 fibroblast
, tissue inhibitor of metalloproteinase-1