Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
The glycoprotein encoded by VWF functions as both an antihemophilic factor carrier and a platelet-vessel wall mediator in the blood coagulation system.
Showing 10 out of 23 products:
von Willebrand Factor is steadily elevated throughout the course of dysrhythmia in NVAF patients treated with warfarin and in those with higher intensity of left atrium blood stasis.
The levels of VWF-cleaving protease ADAMTS13 (show ADAMTS13 Proteins) among neonates were higher as compared with healthy adults, despite a significant elevation of VWF antigen (Ag) and Ristocetin cofactor (RiCof) noted in all neonates.
The pathogenic effects of candidate VWF gene mutations were explored in this study. Molecular dynamic simulations on p.M771I mutant VWF revealed distinct structural rearrangements including a large deviation in the E' domain, and significant loss of beta-sheet secondary structure.
investigated the roles of ADAMTS13 (show ADAMTS13 Proteins) and VWF in thrombotic events of patients with Connective Tissue Diseases
vWF had a significant prognostic impact on cardiovascular mortality when OPG (show TNFRSF11B Proteins) levels were low. Low levels of both OPG (show TNFRSF11B Proteins) and act vWF were associated with a 99 % survival rate during the follow-up of five years.
Studied the significance of the von Willebrand factor (VWF)/ ADAMTS-13 (show ADAMTS13 Proteins) ratio in advanced non-small-cell lung cancer (NSCLC). Findings suggest that the imbalance between VWF secretion and ADAMTS-13 (show ADAMTS13 Proteins) may play a role in the hypercoagulability state in advanced NSCLC, and increase of the plasma VWF/ADAMTS-13 (show ADAMTS13 Proteins) ratio may serve as an independent predictive factor for mortality in patients with advanced NSCLC.
Type 3 von Willebrand disease patients with the Pro2808Leufs*24 have bioavailable platelet-derived VWF that may produce a milder bleeding phenotype than other type 3s
vaso-occlusive crisis in sickle cell disease is associated with increased reactivity of VWF, without a pronounced ADAMTS-13 (show ADAMTS13 Proteins) deficiency
Different patterns of VWF multimer loss were seen in heart failure patients treated with implantation of left ventricular assist device and total artificial heart, which may contribute to bleeding patterns.
Complex VWF-ADAMTS13 (show ADAMTS13 Proteins)-mediated mechanisms disturb haemostasis in inflammatory bowel disease.
In conclusion, endothelial vWF knockdown prevented angiotensin II-induced ET-1 (show EDN1 Proteins) upregulation through attenuation of NOX-mediated O2- production.
alterations in glycosylation of vWF and other adhesion proteins associated with the targeting of the alpha1,3-Gal (show GAL Proteins)-epitope in mutant swine may have salutatory effects on the primate platelet activation observed in these xenografts.
Hemodynamic activation of vWF and increased plasma ADAMTS-13 (show ADAMTS13 Proteins) may have contributed to reduced high-molecular-weight vWF multimers and impairment of the vWF-platelet aggregation pathway during mechanical circulatory support.
both the gpIb-VWF interaction and the integrin alpha(2 (show ITGA2 Proteins))beta(1)-collagen interaction contribute to platelet adhesion under high shear stress; integrin alpha(II (show GSTA3 Proteins))beta(1) makes a greater contribution to adhesion to type I collagen because less VWF is bound
this study shows that Von Willebrand factor protects against acute CCl4 (show CCL4 Proteins)-induced hepatotoxicity through phospho-p38 MAPK (show MAPK14 Proteins) signaling pathway inhibition
the ADAMTS13 (show ADAMTS13 Proteins)-vWF axis is partially involved in the pathophysiology of kidney ischemic reperfusion injury.
Type 2N von Willebrand disease variants were associated with decreased VWF secretion and impaired factor VIII binding/stability.
identify a critical role for VWF in cerebral inflammation and blood-brain barrier damage after intracerebral haemorrhage
The low-molecular-weight heparin (LMWH) Tinzaparin inhibited Von Willebrand factor (VWF) fiber formation and vessel occlusion in tumor vessels by blocking thrombin (show F2 Proteins)-induced endothelial cells (ECs) activation and vascular endothelial growth factor-A (VEGF-A (show VEGFA Proteins))-mediated VWF release.
In a laser injury-induced thrombosis model, P-selectin (show SELP Proteins) modulates thrombus propagation independently of VWF and TSP1 (show GZMA Proteins)
Refrigeration-induced binding of VWF to platelets facilitates their rapid clearance by inducing GPIbalpha (show GP1BA Proteins)-mediated signaling.
BLOC-2 (show HPS6 Proteins) subunit HPS6 (show HPS6 Proteins) deficiency affects the tubulation and secretion of von Willebrand factor from mouse endothelial cells
A novel single-domain antibody against von Willebrand factor A1 domain that interferes with VWF-platelet interactions in vivo. By using this sdAb, show that the A1 domain is pertinent to the participation of VWF in the inflammatory response.
These experiments delineate an unexpected pathway in which microbiota-triggered TLR2 signaling alters the synthesis of proadhesive VWF by the liver endothelium and favors platelet integrin-dependent thrombus growth.
The glycoprotein encoded by this gene functions as both an antihemophilic factor carrier and a platelet-vessel wall mediator in the blood coagulation system. It is crucial to the hemostasis process. Mutations in this gene or deficiencies in this protein result in von Willebrand's disease. An unprocessed pseudogene has been found on chromosome 22.
von Willebrand factor
, coagulation factor VIII VWF