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. Additionally we are shipping VWF Antibodies (333) and VWF Kits (75) and many more products for this protein.
Showing 10 out of 22 products:
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
ADAMTS13 (show ADAMTS13 Proteins) is the key protease that regulates the multimeric state of VWF. Without ADAMTS13 (show ADAMTS13 Proteins), VWF multimers can grow to pathologically large sizes. This is a risk factor for the life-threatening condition thrombotic thrombocytopenic purpura (TTP (show ADAMTS13 Proteins))
Stroke in human immunodeficiency virus infection is associated with a prothrombotic state, characterized by elevated von Willebrand factor and low ADAMTS13 (show ADAMTS13 Proteins) levels
An in vitro model for LVAD associated aVWD demonstrated that ADAMTS-13 (show ADAMTS13 Proteins) and platelets contribute to the depletion of HMWM of VWF.
free thiol groups are shown to be involved in VWF binding to both collagen III and platelet GP1b (show GP1BA Proteins) receptor.
Large cohort of Spanish von Willebrand disease patients in whom VWF mutations have been identified.
Type 2B mutations localized in the A1 domain could enhance the sensitivity to ADAMTS13 (show ADAMTS13 Proteins)-mediated proteolysis. When GPIbalpha (show GP1BA Proteins) participated, there was a dramatically increased proteolytic cleavage of VWF by ADAMTS13 (show ADAMTS13 Proteins) to rVWF-WT, excluding some type 2B mutants.
Study compared the force-induced domain unfolding of recombinant dimeric VWF with recombinant VWF multimers
Glycan stabilization of the VWF A2 domain acts together with the Ca(2 (show CA2 Proteins)+)binding site and vicinal cysteine disulfide bond to control unfolding and ADAMTS13 (show ADAMTS13 Proteins) proteolysis.
Based on prediction scores, four variants, namely, P1266L, H1268D, C1272R, and C1272F, were predicted as highly deleterious from a pool of 72 nsSNPs/variants in A1 domain of VWD belonging to type 2A and 2B
Interaction between VWF and FVIII (show F8 Proteins) in treating VWD.
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
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.
Certain VWD-type 2B mutations relieve the need for shear stress to induce LRP1 (show LRP1 Proteins) binding. Enhanced LRP1 (show LRP1 Proteins) binding coincides with a reduced survival of VWF/p.R1306Q and VWF/p.V1316M
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