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The protein encoded by this intronless gene is an endothelial-specific type I membrane receptor that binds thrombin. Additionally we are shipping Thrombomodulin Antibodies (266) and Thrombomodulin Kits (91) and many more products for this protein.
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The finding of a previously unrecognized fibrinolytic phenotype indicates that bleeding in Thrombomodulin-associated coagulopathy has a complex pathogenesis and highlights the pivotal role of TM as a regulator of hemostasis.
TM mediates cell proliferation and migration via the Epithelial-To-Mesenchymal Transition (EMT (show ITK Proteins)) biomarkercyclooxygenase (COX)-2
the whole THBD gene sequenced in patients with recurrent venous thromboembolism (VTE); found 8 polymorphisms in the THBD gene in Swedish population; none of these polymorphisms was significantly associated with the risk of VTE recurrence; results indicate that THBD polymorphisms may not be a risk factor for VTE recurrence
CORM-2 protects human umbilical vein endothelial cells from lipopolysaccharide-induced injury, by way of suppressing NF-kappaB (show NFKB1 Proteins) activity, which downregulates TM and EPCR (show PROCR Proteins) mRNAs. It also decreases MMP-2 (show MMP2 Proteins) expression and prevents the shedding of TM and EPCR (show PROCR Proteins) from the surface of endothelial cells, so as to preserve their protective effect.
The results demonstrate that the LFA-1 (show ITGAL Proteins) and Mac-1 (show ITGAM Proteins) integrins on leukocytes bind to thrombomodulin (TM), thereby establishing the molecular and structural basis underlying LFA-1 (show ITGAL Proteins) and Mac-1 (show ITGAM Proteins) integrin interaction with TM on endothelial cells.
Human thrombomodulin transgenic aortic endothelial cells are less sensitive to activation by either HMGB1 or hTNFalpha, an effect that appears to be dependent on the lectin-like domain of TBM.
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.
TM up-regulated E-cadherin (show CDH1 Proteins) but down-regulated N-cadherin (show CDH2 Proteins) expression, resulting in reversal of epithelial-mesenchymal transition (EMT (show ITK Proteins)) in the lung cancer cells.
High serum thrombomodulin expression is associated with non-alcoholic fatty liver disease.
results do not suggest a predictive role for THBD c.1418C>T polymorphism in VTE recurrence
the lectin-like domain of thrombomodulin is critically involved in host defence against E. coli induced acute pyelonephritis
Identified Nur77 (show NR4A1 Proteins)/Nor1 (show NR4A3 Proteins) as novel regulators of thrombomodulin expression and function in vascular endothelial cells.
TM expression in corneal epithelium was modulated during the corneal wound healing process, and may be regulated by PDGF (show PDGFA Proteins)-BB. In addition, rTMD23 has therapeutic potential in corneal injury
Thrombomodulin contributes to gamma tocotrienol-mediated lethality protection and hematopoietic cell recovery in irradiated mice
the recombinant epidermal growth factor (show EGF Proteins)-like domain plus serine/threonine-rich domain of thrombomodulin suppresses the inflammatory response in mice
Thrombomodulin may modulate allergic responses by inhibiting the activation of both eosinophils and mast cells.
Thrombomodulin modulates dendritic cells via both antagonism of high mobility group protein B1 (show HMGB1 Proteins) and an independent mechanism.
The lectin-like domain of TM does not play an important role in the host response to M. tuberculosis infection in mice.
Recombinant thrombomodulin protects mice against histone-induced lethal thromboembolism.
TM's lectin-like domain constrains glucose-induced complement activation on endothelial cells and podocytes and ameliorates albuminuria and glomerular damage.
Atorvastin induces THBD expression in the aorta of cholesterol-fed rabbits.
The protein encoded by this intronless gene is an endothelial-specific type I membrane receptor that binds thrombin. This binding results in the activation of protein C, which degrades clotting factors Va and VIIIa and reduces the amount of thrombin generated. Mutations in this gene are a cause of thromboembolic disease, also known as inherited thrombophilia.
, CD141 antigen
, snoRNA MBII-339