Recombinant Human TF Protein (C-6His)

Name: Recombinant Human TF Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0495NP
Availability: InStock

BL-0495NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Coagulation Factor III/Tissue Factor is produced by our Mammalian expression system and the target gene encoding Gly34-Glu251 is expressed with a 6His tag at the C-terminus.
Accession	P13726
Synonym	Tissue Factor; TF; Coagulation Factor III; Thromboplastin; CD142; F3
Gene Background	Tissue Factor (TF) is a single-pass type I membrane glycoprotein member of the tissue factor family. TF expression is highly dependent upon cell type. This factor enables cells to initiate the blood coagulation cascades, and it functions as the high-affinity receptor for the coagulation factor VII. TF initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The complex activates factors IX or X by specific limited protolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade.
Molecular Mass	25.76 KDa
Apmol Mass	35-55 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited proteolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade.
Subcellular Location	[Isoform 1]: Membrane; Single-pass type I membrane protein.; [Isoform 2]: Secreted.
Protein Families	Tissue factor family
Database References	HGNC: 3541 OMIM: 134390 KEGG: hsa:2152 STRING: 9606.ENSP00000334145 UniGene: PMID: 29787758 Subjects with AG and GG genotype had significantly higher TF levels than AA genotype. GG genotype of 603A>G polymorphism augments the risk of thrombosis by 4.4 fold, thus highlighting the significance of this polymorphism in the development of DVT PMID: 29789989 Monocyte TF may be a relevant source of TF-mediated thrombogenicity in NSCLC patients and may be associated with prognosis in NSCLC. PMID: 28419722 plasma activity higher in women with pre-eclampsia than in those with infants small for gestational age or normal pregnancies PMID: 28521572 The interaction between tissue factor and filamin A is dependent on the differential phosphorylation of Ser253 and Ser258. The interaction with filamin A may translocate cell surface TF to cholesterol-rich lipid rafts, increasing cell surface TF activity as well as TF incorporation and release into microvesicles. PMID: 29044292 Our study identifies a previously undescribed role of miRNA in venous thrombosis by regulating TF expression. Therefore, restoration of miR-145 levels may serve as a promising therapeutic strategy for management of venous thrombosis PMID: 29217135 TF(+) microvesicless released from orthotopic pancreatic tumors increase venous thrombosis in mice. PMID: 28834179 HUVEC and adult human dermal blood endothelial cells respond similarly to TNFalpha and IL-1beta in terms of TF expression, and both are suitable models to examine cell surface TF activity and TF-positive microvesicle release in endothelial cells. PMID: 28151805 Cell lines with intrinsically high TF expression were associated with decreased cancer stem cell activity. Knockdown of TF was associated with increased cancer stem cell activity. Overexpression of TF was associated with decreased cancer stem cell activity. Expression of TF did not affect cellular viability but may increase proliferation. PMID: 29715083 uPAR 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. PMID: 28841839 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. PMID: 27926582 These results demonstrate that procoagulant microvesicles shed by head and neck squamous cell carcinoma line (UMSCC81B) induced a procoagulant effect in HUVECs through increased clotting activity and cell membrane surface expression of TF. PMID: 27841803 The proinflammatory cytokine IL-33 induces differential tissue factor expression and activity in monocyte subsets, as well as the release of procoagulant microvesicless. In this manner, IL-33 may contribute to the formation of a prothrombotic state characteristic for cardiovascular disease. PMID: 28492698 Pin1 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. PMID: 28962834 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. PMID: 27808345 In the presence of tissue factor-positive cancer cells, the CAR-modified T cells (TF-CAR T) were highly activated and showed specific cytotoxicity to TF-positive cancer cells. PMID: 28055955 TF is an angiogenic-specific receptor and the target molecule for fVII-targeted therapeutics. PMID: 27807692 The present study did not show significant association of TF gene -603A/G and +5466A>G polymorphisms with venous thromboembolism in malignancy, however, further larger studies including different ethnic population are needed to confirm our findings. PMID: 27685527 It was demonstrated that the nature of the clot formed, as determined from the quartz crystal microbalance parameters, was highly dependent on the rate of clot formation resulting from the TF concentration used for activation. These parameters could also be related to physical clot characteristics such as fibrin fibre diameter and fibre density, as determined by scanning electron microscopic image analysis. PMID: 27311950 Through induction of TF in vascular endothelial cells, IL-33 could enhance their thrombotic capacity and thereby might impact on thrombus formation in the setting of atherosclerosis. PMID: 27142573 Tissue Factor was highly expressed in 73.6 % of osteosarcoma biopsies, and expression associated significantly with disease-free survival. PMID: 26763081 Platelet tissue factor activity and membrane cholesterol are increased in hypercholesterolemia and normalized by rosuvastatin, but not by atorvastatin. PMID: 28142075 the identification of platelet TF and TLR4 as regulators of the effect of E. coli O111 might represent a novel therapeutic target to reduce the devastating consequences of the hemostatic disorder during sepsis. PMID: 28957360 A coagulation initiating pathway is revealed in which the TF-FVIIa-nascent FXa complex activates FVIII apart from thrombin feedback. PMID: 28729433 Ticagrelor, but not clopidogrel, reduces arterial thrombosis via endothelial tissue factor suppression. Ticagrelor reduced TNF-alpha-induced TF expression via proteasomal degradation. PMID: 28028070 The aim of this study was to evaluate the concentration of TF and its inhibitor TFPI in blood plasma, the impact of traditional and non-traditional cardiovascular risk factors on their concentration and the impact of both markers of haemostasis on the severity of subclinical atherosclerosis. PMID: 28749986 TF is highly expressed in breast neoplasms, but does not predict survival or correlate with tumor size. PMID: 28551673 Inhibition of the inflammatory signaling intermediate p38 MAPK reduced tissue factor (TF) mRNA by one third but increased tumor necrosis factor (TNF) and interleukin-1 beta (IL-1beta) mRNA. PMID: 28343272 TF levels were significantly elevated in type 2 diabetes mellitus (both with and without cardiovascular complications) when compared to the controls. We suggest that pathologic plasma TF activity, as marker of increased propensity of clot pathology, should be investigated. PMID: 28246677 our data show that a few select TF residues that are implicated in interacting with PS contribute to the TF coagulant activity at the cell surface. However, our data also indicate that TF regions outside of the putative lipid binding region may also contribute to PS-dependent decryption of TF. PMID: 27348126 These findings suggest that cancer cell-derived extracellular vesicles mediate coagulopathy resulting in ischemic stroke via TF-independent mechanisms. PMID: 27427978 Macrophage tissue factor prothrombotic activity is regulated by integrin-alpha4/arf6 trafficking. PMID: 28495929 this study shows that low levels of circulating tissue factor may contribute to the reduced coagulopathy reported in patients infected with Neisseria meningitidis lpxL1 mutants PMID: 28024455 Oligoubiquitination of Lys255 within TF permits PP2A to bind and dephosphorylate Ser253 and occurs to terminate TF release and contain its activity. PMID: 27599717 Circulating miR-126 exhibits antithrombotic properties via regulating post-transcriptional TF expression, thereby impacting the hemostatic balance of the vasculature in diabetes mellitus. PMID: 27127202 Data suggest that CAIX (carbonic anhydrase IX) is a novel downstream mediator of asTF (alternatively spliced tissue factor) in pancreatic ductal adenocarcinoma, particularly under hypoxic conditions that model late-stage tumor microenvironment; tumor hypoxia appears to lead to up-regulation of CAIX expression (or 'activation'), which is more pronounced in tumor cells overexpressing asTF. PMID: 27721473 Low concentrations of TF and exogenous FXIa, each too low to elicit a burst in thrombin production alone, act synergistically when in combination to cause substantial thrombin production. PMID: 27789475 In placenta of patients with preeclampsia, we detected abnormal expression of F3 and THBD with increased protein and mRNA levels. The role of these molecules in the pathogenesis of this disease and in alterations of hemostatic and histopathological aspects of placentas need further studying. PMID: 27002259 These findings suggest that activation of TF-pathway is an important component of dengue virus-related coagulation disorders. PMID: 27592310 in tumor microenvironment, TF-induced coagulation activated the complement system and subsequently recruited myeloid-derived suppressor cells to promote tumor growth. PMID: 28106852 Hypoxia increased the expression of TF in human podocytes NF-kappaB dependently. TF may have a critical role in the hypoxic podocyte injury. PMID: 26715508 These results reveal a functional link between VWF and TF under whole blood flow conditions, in which surface-immobilized TF and VWF mutually contribute to mural thrombus formation, which is essential for normal hemostasis. By contrast, TF circulating in blood may be involved in systemic hypercoagulability, as seen in sepsis caused by severe microbial infection, in which neutrophil inflammatory responses may be active. PMID: 27562418 TF expression significantly correlated with levels of CRP, TNF-alpha and MCP-1. These factors may play an important role in the development of chronic thromboembolic pulmonary hypertension. PMID: 26667361 Microvesicle-associated tissue factor procoagulant activity, but not plasma TF antigen, may provide valuable additional information for the diagnostic work-up of women with suspected ovarian cancer. PMID: 26967531 This brief review summarizes the contribution of the coagulation system and in particular the role of TF in brain hemostasis as well as to the pathophysiology of stroke and multiple sclerosis. [review] PMID: 27207429 stimulated von Willebrand factor secretion by umbilical vein endothelial cells PMID: 27766025 Circulating FVII, FVIIa and TFPI were significantly elevated in women with severe preeclampsia in the absence of comparable changes in plasma TF levels. PMID: 26765308 The data obtained indicate that active tissue factor, TF is present in membrane microparticles produced in vitro by endothelial cells, monocytes, and THP-1 cells, but not in microparticles derived from granulocytes and platelets. PMID: 27260391 Results indicate that granulocyte-colony stimulating factor receptor, tissue factor, and vascular endothelial growth factor receptor bound vascular endothelial growth factor expression as well as their co-expression might influence breast cancer biology. PMID: 27629739 the actin-binding protein filamin-A has a critical role in incorporation of Tissue factor into extracellular vesicles and secretion of extracellular vesicles from ovarian cancer cells exposed to hypoxia PMID: 26446354

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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Recombinant Human TF Protein (C-6His)

Recombinant Human TF Protein (C-6His)

Product Overview

Target Details

FAQs