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TIMP1 belongs to the TIMP gene family. Additionally we are shipping TIMP1 Kits (121) and TIMP1 Proteins (56) and many more products for this protein.
Showing 10 out of 269 products:
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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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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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 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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Cow (Bovine) Monoclonal TIMP1 Primary Antibody for EIA, IHC (p) - ABIN567563
Kodama, Kishi, Obata, Iwata, Hayakawa: Monoclonal antibodies to bovine collagenase inhibitor. in Collagen and related research 1988
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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
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
suggest better clinical usefulness of MMP-9 (show MMP9 Antibodies) and TIMP-1 expression in cholesteatoma tissues than either serum or plasma levels of these proteins
These results suggest that in the progression of renal aging, high expression of TIMP-1 up-regulates PTEN (show PTEN Antibodies) expression indicating that PTEN (show PTEN Antibodies) and TIMP-1 are involved in the aging-associated impairment of renal angiogenesis
MMP-1 (show MMP1 Antibodies) expression is increased in intervertebral disc degeneration, with higher expression observed in more severe cases, whereas TIMP-1 expression was similarly expressed in both normal and degenerated discs.
Metformin simultaneously increases VEGFA (show VEGFA Antibodies) and reduces CXCL10 (show CXCL10 Antibodies) and TIMP1 in CD34 (show CD34 Antibodies)(+) cells in a model of the diabetic state combined with hypoxia to stimulate angiogenesis.
It demonstrated that MMP-9 (show MMP9 Antibodies) to TIMP-1 ratio was positively associated with body weight and waist circumference 3 years after a 12-week low-calorie-diet weight-reduction program in men with metabolic syndrome.
These results show that increased MMP-8 (show MMP8 Antibodies) and decreased TIMP-1 expressions are closely related to the invasive pituitary adenoma, and can be helpful for the evaluation.
Genes expression of MMP9 (show MMP9 Antibodies), VEGFA (show VEGFA Antibodies) and TIMP1 in peripheral blood leukocytes may play a pivotal role in regulation of progression of bladder cancer; TIMP1 expression may be important factor for early recurrence.
High TIMP1 expression is associated with Sepsis.
Data show that serum neuron-specific enolase (show ENO2 Antibodies), cytokeratin 19 (show KRT19 Antibodies) fragment 21-1, pro-gastrin-releasing peptide (show GRP Antibodies), squamous cell carcinoma antigen, tissue inhibitor of metalloproteinase-1, and human epididymis protein 4 are not associated with brain metastases.
association of the TIMP-1 gene with recurrent aphthous stomatitis was ruled out based on our results.
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.
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.
Expansion of stem cells counteracts age-related mammary regression in compound Timp1/Timp3 (show TIMP3 Antibodies)-deficient mice.
TNF-alpha (show TNF Antibodies) produced by cholestasis can promote liver fibrosis via TIMP-1 production from hepatic stellate cells.
These data suggest an MMP-independent role of TIMP-1 in regulating CD4 (show CD4 Antibodies) T cell access into the CNS parenchyma during acute JHMV encephalitis
miR (show MLXIP Antibodies)-21 contributes to renal fibrosis by mediating MMP9 (show MMP9 Antibodies)/TIMP1
Gene expression of Mmp-12 (show MMP12 Antibodies) and Mmp-13 (show MMP13 Antibodies), and Timp-1 was strongly upregulated at all time points in RD compared with controls. Timp-2 (show TIMP2 Antibodies), Mmp-2 (show MMP2 Antibodies), and Mmp-9 (show MMP9 Antibodies) expression was modest.
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.
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.
, metalloproteinase inhibitor 1
, tissue inhibitor of metalloproteinase 1 (erythroid potentiating activity, collagenase inhibitor)
, tissue inhibitor of metalloproteinases 1
, tissue inhibitor of matrix metalloproteinase-1
, tissue inhibitor of metalloproteinase 1
, collagenase inhibitor
, erythroid potentiating activity
, erythroid-potentiating activity
, fibroblast collagenase inhibitor
, metalloproteinase tissue inhibitor 1
, tissue inhibitor of metallopeptidase 1
, metalloproteinase tissue inhibitor
, TPA-induced protein
, collagenase inhibitor 16C8 fibroblast
, tissue inhibitor of metalloproteinase-1