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TIMP1 belongs to the TIMP gene family. Additionally we are shipping TIMP1 Kits (140) and TIMP1 Proteins (58) and many more products for this protein.
Showing 10 out of 307 products:
Human Monoclonal TIMP1 Primary Antibody for CyTOF, ELISA (Capture) - ABIN4899801
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
Show all 13 Pubmed References
Human Monoclonal TIMP1 Primary Antibody for CyTOF, ELISA (Capture) - ABIN4899800
Naveau, Reinald, Fournier, Durand, Lafont, Coulomb, Gogly: Gingival fibroblasts inhibit MMP-1 and MMP-3 activities in an ex-vivo artery model. in Connective tissue research 2007
Show all 13 Pubmed References
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
Show all 11 Pubmed References
Mouse (Murine) Polyclonal TIMP1 Primary Antibody for WB - ABIN4886743
Xu, Ling, Zhu, Fan, Zhang: The effect of 2,3,4',5-tetrahydroxystilbene-2-0-?-D glucoside on neointima formation in a rat artery balloon injury model and its possible mechanisms. in European journal of pharmacology 2013
Show all 11 Pubmed References
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
Show all 6 Pubmed References
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 ELISA - ABIN2476829
Curzi-Dascalova: [Waking and sleeping E.E.G. in normal babies before 6 months of age (author's transl)]. in Revue d'électroencéphalographie et de neurophysiologie clinique 1978
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Human Monoclonal TIMP1 Primary Antibody for ELISA, WB - ABIN2476827
Koike, Vernon, Hamner, Sadoun, Reed: MT1-MMP, but not secreted MMPs, influences the migration of human microvascular endothelial cells in 3-dimensional collagen gels. in Journal of cellular biochemistry 2002
Cow (Bovine) Polyclonal TIMP1 Primary Antibody for IHC (p), ELISA - ABIN2476830
Goldraich, Ramos, Goldraich: Urography versus DMSA scan in children with vesicoureteric reflux. in Pediatric nephrology (Berlin, Germany) 1990
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CD82 (show CD82 Antibodies) is a component of the promiscuous TIMP-1 interacting protein complex on cell surface of human pancreatic adenocarcinoma cells. CD82 (show CD82 Antibodies) directly binds to TIMP-1 N-terminal region through its large extracellular loop and co-localizes with TIMP-1.
these results show here that EGFR signaling induces TIMP-1 expression in colorectal cancer cells, and that TIMP-1 promotes a more aggressive behavior, specifically in KRAS mutated cells
Our results provided evidence that polymorphisms in TIMP1, DLX1 and DLX2 genes may be associated with DF phenotypes.
The plasma levels of interleukin (IL)-1beta (show IL1B Antibodies), tumor necrosis factor (TNF)-alpha (show TNF Antibodies), tissue inhibitor of metalloproteinases (TIMP)-1 are increased in myelofibrosis (MF) patients.
The present study suggests that scoring of TIMP-1 immunoreactivity is a better choice than measuring of TIMP-1 plasma levels.
Results show that TIMP1 expression is significantly upregulated in human colon cancer. Its suppression decreases proliferation, and metastasis but increases apoptosis by inducing TIMP1 specific regulated FAK (show PTK2 Antibodies)-PI3K (show PIK3CA Antibodies)/AKT (show AKT1 Antibodies) and MAPK (show MAPK1 Antibodies) pathway. These results suggest that TIMP1 may play an important role in promoting tumorigenesis and metastasis of human colon cancer.
cancer associated fibroblasts (CAFs) promoted hepatocellular cancer (HCC) growth via IL-6/STAT3/AKT pathway and TIMP-1 over-expression driven by IL-6/STAT3 pathway in HCC cells brought in more CAFs through activating liver fibroblasts.
Tissue inhibitor of matrix metalloproteinases 1 (TIMP1) inhibition resensitized tumors to gemcitabine and radiotherapy.
Suggest that IL-6 (show IL6 Antibodies) could promote the invasiveness of breast cancer cells by inducing secretion of TIMP-1 and -2, causing a disturbance in TIMP/MMP balance.
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.
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
Results provide evidence for the utility of MMP9 (show MMP9 Antibodies) and TIMP1 as markers of age- and lactocrine-sensitive porcine female reproductive tract development.
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.
These results show that MMP-9 (show MMP9 Antibodies)/TIMP-1 system disturbance and changes of histological structure in uteri tissue are involved in fluoride-induced reproductive dysfunctions.
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.
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