Recombinant Human Tissue Factor Protein

Beta LifeScience SKU/CAT #: BLA-9035P

Recombinant Human Tissue Factor Protein

Beta LifeScience SKU/CAT #: BLA-9035P
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Product Overview

Host Species Human
Accession P13726
Synonym CD142 CD142 antigen Coagulation factor III Coagulation factor III (thromboplastin tissue factor) F3 FLJ17960 TF TF_HUMAN TFA Thromboplastin Tissue factor
Description Recombinant Human Tissue Factor Protein was expressed in E.coli. It is a Protein fragment
Source E.coli
Molecular Weight 28 kDa including tags
Purity >90% SDS-PAGE.The final product was refolded using our unique -€œtemperature shift inclusion body refolding-€ technology and chromatographically purified.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Upon delivery aliquot and store at -80°C. Avoid freeze / thaw cycle.

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
Tissue Specificity Lung, placenta and pancreas.

Gene Functions References

  1. TF knockout in MDA-MB-231cells reduced TF/FVIIa signaling and coagulation activity. Silencing of TF in MDA-MB-231cells decreased the release of microvesicles. PMID: 29787758
  2. 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
  3. Monocyte TF may be a relevant source of TF-mediated thrombogenicity in NSCLC patients and may be associated with prognosis in NSCLC. PMID: 28419722
  4. plasma activity higher in women with pre-eclampsia than in those with infants small for gestational age or normal pregnancies PMID: 28521572
  5. 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
  6. 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
  7. TF(+) microvesicless released from orthotopic pancreatic tumors increase venous thrombosis in mice. PMID: 28834179
  8. 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
  9. 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
  10. 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
  11. 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
  12. 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
  13. 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
  14. 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
  15. 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
  16. 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
  17. TF is an angiogenic-specific receptor and the target molecule for fVII-targeted therapeutics. PMID: 27807692
  18. 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
  19. 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
  20. 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
  21. Tissue Factor was highly expressed in 73.6 % of osteosarcoma biopsies, and expression associated significantly with disease-free survival. PMID: 26763081
  22. Platelet tissue factor activity and membrane cholesterol are increased in hypercholesterolemia and normalized by rosuvastatin, but not by atorvastatin. PMID: 28142075
  23. 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
  24. A coagulation initiating pathway is revealed in which the TF-FVIIa-nascent FXa complex activates FVIII apart from thrombin feedback. PMID: 28729433
  25. Ticagrelor, but not clopidogrel, reduces arterial thrombosis via endothelial tissue factor suppression. Ticagrelor reduced TNF-alpha-induced TF expression via proteasomal degradation. PMID: 28028070
  26. 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
  27. TF is highly expressed in breast neoplasms, but does not predict survival or correlate with tumor size. PMID: 28551673
  28. 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
  29. 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
  30. 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
  31. These findings suggest that cancer cell-derived extracellular vesicles mediate coagulopathy resulting in ischemic stroke via TF-independent mechanisms. PMID: 27427978
  32. Macrophage tissue factor prothrombotic activity is regulated by integrin-alpha4/arf6 trafficking. PMID: 28495929
  33. 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
  34. Oligoubiquitination of Lys255 within TF permits PP2A to bind and dephosphorylate Ser253 and occurs to terminate TF release and contain its activity. PMID: 27599717
  35. 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
  36. 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
  37. 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
  38. 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
  39. These findings suggest that activation of TF-pathway is an important component of dengue virus-related coagulation disorders. PMID: 27592310
  40. in tumor microenvironment, TF-induced coagulation activated the complement system and subsequently recruited myeloid-derived suppressor cells to promote tumor growth. PMID: 28106852
  41. 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
  42. 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
  43. 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
  44. 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
  45. 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
  46. stimulated von Willebrand factor secretion by umbilical vein endothelial cells PMID: 27766025
  47. 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
  48. 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
  49. 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
  50. 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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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