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The interaction between tissue factor and filamin A (show FLNA Proteins) is dependent on the differential phosphorylation of Ser253 and Ser258. The interaction with filamin A (show FLNA Proteins) may translocate cell surface TF to cholesterol-rich lipid rafts, increasing cell surface TF activity as well as TF incorporation and release into microvesicles.
The induction of TG by BXPC3 cells was mainly driven by the TF pathway while TG generation triggered by MCF7 cells was also driven by FXII (show F12 Proteins) activation.
Our study identifies a previously undescribed role of miRNA in venous thrombosis by regulating TF expression. Therefore, restoration of miR (show MLXIP Proteins)-145 levels may serve as a promising therapeutic strategy for management of venous thrombosis
HUVEC and adult human dermal blood endothelial cells respond similarly to TNFalpha (show TNF Proteins) and IL-1beta (show IL1B Proteins) in terms of TF expression, and both are suitable models to examine cell surface TF activity and TF-positive microvesicle release in endothelial cells.
uPAR (show PLAUR Proteins) and TF could potentially be attractive targets for molecular imaging and therapy in oral squamous cell carcinoma due to high positive expression rates and tumor-specific expression patterns.
The highest tissue factor activity was detected in microparticles from monocytes, lower activity - in microparticles from endothelial cells and THP-1 cells, and no activity - in microparticles from platelets and granulocytes.
Patients with early onset preeclampsia are characterised by an attenuated coagulation response characterised by reduced thrombin (show F2 Proteins) generation stimulated by low-dose TF and elevated plasma TFPI (show TFPI Proteins) activity.
The proinflammatory cytokine IL-33 (show IL33 Proteins) induces differential tissue factor expression and activity in monocyte subsets, as well as the release of procoagulant microvesicless. In this manner, IL-33 (show IL33 Proteins) may contribute to the formation of a prothrombotic state characteristic for cardiovascular disease.
Pin1 (show PIN1 Proteins) is a fast-acting enzyme which may be utilised by cells to protect the phosphorylation state of TF in activated cells prolonging TF activity and release, and therefore ensuring adequate haemostasis.
Circulating pentraxin nCRP has little pro-angiogenic effect but when dissociated into mCRP on the surface of endothelial cells it is able to trigger potent proangiogenic effects by inducing F3-gene upregulation and TF signaling.
Tissue factor cytoplasmic domain is involved in TF-PAR-2 (show F2RL1 Proteins) signalling initiating hepatic fibrosis and is a potential therapeutic target, as its deletion would not impact coagulation.
Myeloid cell derived tissue factor dampens inflammation in acid-induced acute lung injury.
Ticagrelor, but not clopidogrel, reduces arterial thrombosis via endothelial tissue factor suppression. Ticagrelor reduced TNF-alpha (show TNF Proteins)-induced TF expression via proteasomal degradation.
Macrophage tissue factor prothrombotic activity is regulated by integrin-alpha4/arf6 (show ARF6 Proteins) trafficking.
Evening primrose oil and forskolin decreased the prothrombotic effect of celecoxib initiated by a LPS (show TLR4 Proteins) challenge in mice, and this effect was, at least partly, mediated by mitigating TF expression and activity.
Thrombin (show F2 Proteins)-independent contribution of tissue factor to inflammation and cardiac hypertrophy in a mouse model of sickle cell disease.
These findings reveal a novel biological function and mechanism of the protein C (show PROC Proteins) pathway in which protein S and the aPC (show APC Proteins)-cleaved form of fV are cofactors for anti-inflammatory cell signaling by aPC (show APC Proteins) in the context of endotoxemia and infection
Lung epithelial tissue factor regulates alveolar procoagulant activity and permeability in acute lung injury.
PGE2 increases both TF expression and activity through the regulation of the EP1 (show PTGER1 Proteins)/SIRT1 (show SIRT1 Proteins) pathway.
Fas (show FAS Proteins)-initiated, caspase-3 (show CASP3 Proteins)-dependent hepatocyte apoptosis increases tissue factor procoagulant activity through a mechanism involving phosphatidylserine externalization.
Tissue factor expression on porcine neonatal islet cell clusters is an important initiator of instant blood-mediated inflammatory reaction in islet xenotransplantation.
Prolonged clopidogrel treatment reduced coronary tissue factor (TF) expression and tended to reduce the blood TF level post-PCI (show SERPINA5 Proteins), thus possibly modulating the risk of late thrombosis.
Procoagulant porcine tissue factor is induced in primary pig aortic endothelial cells only by fresh human plasma, and not by heat-inactivated plasma.
myocardial infarction induced proinflammatory gene and protein expression in peripheral blood mononuclear cells of tissue factor cyclo-oxygenase-2, monocyte chemoattractant protein-1 (show CCL2 Proteins) and CRP (show CRP Proteins)
Arterial (18)F-fluorodeoxyglucose uptake reflects balloon catheter-induced thrombus formation and tissue factor expression via nuclear factor-kappaB in rabbit atherosclerotic lesions.
Polycations could present a new class of anticoagulants with such unique upstream downregulation of blood coagulation, selectively blocking tissue factor-dependent factor VII (show TH Proteins) activation.
Upregulated TF expression and increased plasma TF level during reperfusion period, reduced plasma TFPI-1 (show TFPI Proteins) level during reperfusion period.
lectin-like oxidized LDL receptor (show OLR1 Proteins) Oxidized low-density lipoprotein receptor (show LDLR Proteins) 1expression appears to be closely associated with tissue factor expression, apoptotic events and morphological vulnerability in atherosclerotic lesions
This gene encodes coagulation factor III which is a cell surface glycoprotein. This factor enables cells to initiate the blood coagulation cascades, and it functions as the high-affinity receptor for the coagulation factor VII. The resulting complex provides a catalytic event that is responsible for initiation of the coagulation protease cascades by specific limited proteolysis. Unlike the other cofactors of these protease cascades, which circulate as nonfunctional precursors, this factor is a potent initiator that is fully functional when expressed on cell surfaces. There are 3 distinct domains of this factor: extracellular, transmembrane, and cytoplasmic. This protein is the only one in the coagulation pathway for which a congenital deficiency has not been described. Alternate splicing results in multiple transcript variants.
, coagulation factor III
, coagulation factor 3
, brain tissue factor
, coagulation factor IIIb
, coagulation factor III (thromboplastin, tissue factor) S homeolog