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The glycoprotein encoded by VWF functions as both an antihemophilic factor carrier and a platelet-vessel wall mediator in the blood coagulation system. Additionally we are shipping VWF Antibodies (498) and VWF Kits (85) and many more products for this protein.
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Human VWF Protein expressed in CHO Cells - ABIN2003667
Nogami, Shima, Nishiya, Hosokawa, Saenko, Sakurai, Shibata, Suzuki, Tanaka, Yoshioka: A novel mechanism of factor VIII protection by von Willebrand factor from activated protein C-catalyzed inactivation. in Blood 2002
Show all 4 references for ABIN2003667
Low von Willebrand Factor expression is associated with severe aortic stenosis.
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.
Low serum albumin (show ALB Proteins) and high hsCRP and vWF levels, and their correlations with cIMT, indicate that patients could be at risk of developing malnutrition-inflammation-atherosclerosis syndrome
Von Willebrand factor deficiency (VWF) deficiency is associated with a decreased prevalence of cardiovascular disease. Subclinical carotid atherosclerosis is not reduced in VWF deficiency. VWF deficiency may prevent cardiovascular events but not affect atherosclerosis.
Data indicate that binding of hemoblobin (Hb) to glycoprotein1balpha (GP1balpha) induced platelet activation plays a crucial role in thrombus formation on immobilized von Willebrand factor (VWF) or type I collagen under shear stresses.
analysis of the O-glycosylation sites in VWF
As a clot (show TXNDC17 Proteins) grows, shear stresses can become sufficiently extreme in diseased arteries to drive von Willebrand Factor self-association into massive fibers, potentially the final burst of clot (show TXNDC17 Proteins) growth towards full thrombotic occlusion.
Neutrophil proteases in the glomerular basement membrane cleave von Willebrand factor (VWF) and may protect the kidney from microthrombi.
results of this study suggest that the assessment of the VWF genetic defect might be helpful to guide therapeutic decision-making in patients with von Willebrand disease type2
Tissue factor (show F3 Proteins) stimulated von Willebrand factor secretion by umbilical vein endothelial cells.
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
von Willebrand factor exerts beneficial effects in a mouse sepsis model via recruitment of neutrophils to inflammatory sites.
Staphylococcus lugdunensis binds directly to von Willebrand factor, which proved to be vital for withstanding shear forces and for its adhesion to the vessel wall and cardiac valves.
Clinical experimental cerebral malaria progression was delayed, and overall survival was significantly prolonged in VWF(-/-) mice compared with WT controls.
in stable compensated heart failure mice, disruptions in endothelial vWF expression and extrusion may reduce the incidence of endocardial thrombosis
VWF is expressed in a mosaic pattern in the capillaries of many vascular beds and in the aorta. Hearts of VWF-null mice demonstrate an abnormal endothelial phenotype as well as cardiac dysfunction.
SNAP23 (show SNAP23 Proteins) Regulates Endothelial Exocytosis of von Willebrand Factor
Both platelet-VWF and plasma-VWF are required for optimal platelet-derived FVIII (show F8 Proteins) gene therapy for hemophilia A in the presence of inhibitors.
a genetic link between EGLN1 (show EGLN1 Proteins) and VWF in a constitution specific manner which could modulate thrombosis/bleeding susceptibility and outcomes of hypoxia, is reported.
novel findings demonstrate a specific and critical role for the R1205 residue in modulating macrophage-mediated clearance of VWF in vivo
Clearance differences between blood group (show DARC Proteins) O and non-blood group (show DARC Proteins) O individuals may therefore be related to the blood group (show DARC Proteins) status of the individual rather than the ABH (show ALKBH Proteins) antigen loading on VWF itself.
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