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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 (335) and VWF Proteins (22) and many more products for this protein.
Showing 10 out of 75 products:
Rat (Rattus) VWF ELISA Kit for Sandwich ELISA - ABIN367459
Baraka, Guemei, Gawad: Role of modulation of vascular endothelial growth factor and tumor necrosis factor-alpha in gastric ulcer healing in diabetic rats. in Biochemical pharmacology 2010
Show all 6 references for ABIN367459
Human VWF ELISA Kit for Sandwich ELISA - ABIN365425
Tong, Wan, Zhang, Duan, Tang, Chen, Tang, Su: Vascular endothelial cell injury partly induced by mesenteric lymph in heat stroke. in Inflammation 2014
Show all 2 references for ABIN365425
Rabbit VWF ELISA Kit for Competition ELISA - ABIN415967
Du, Wu, Qing, Wang, Liang, Yu, Tang: Systemic and flap inflammatory response associates with thrombosis in flap venous crisis. in Inflammation 2015
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 ELISA Kits)+)binding site and vicinal cysteine disulfide bond to control unfolding and ADAMTS13 (show ADAMTS13 ELISA Kits) 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 ELISA Kits) in treating VWD.
direct binding of PDIA1 (show P4HB ELISA Kits) to VWF, is reported.
Pathological shear rates generate fibrous VWF from plasma. Its elastic modulus is ~50 MPa. It is non-amyloid, tPA (show PLAT ELISA Kits)-resistant, plasmin (show PLG ELISA Kits)-sensitive, and accumulates procoagulant factors to drive fibrin formation. Platelets roll and adhere to it.
rs216293T/G and rs1063857T/C polymorphisms of the vWF gene are associated with the risk for coronary artery disease.
These studies reveal a novel rheological strategy in which the incorporation of a single glycine within the GPIbalpha (show GP1BA ELISA Kits) binding interface of normal VWF enhances the probability of local unfolding
Decrease of ADAMTS13 (show ADAMTS13 ELISA Kits) is associated with the risk of platelet thrombosis within the allograft during Lung Transplantation.
results strongly argue against apoptosis as a mechanism for the thrombocytopenia of severe VWD-2B exhibiting the VWF/p.V1316M mutation
alterations in glycosylation of vWF and other adhesion proteins associated with the targeting of the alpha1,3-Gal (show GAL ELISA Kits)-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 ELISA Kits) 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 ELISA Kits))beta(1)-collagen interaction contribute to platelet adhesion under high shear stress; integrin alpha(II (show GSTA3 ELISA Kits))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 ELISA Kits) Regulates Endothelial Exocytosis of von Willebrand Factor
Both platelet-VWF and plasma-VWF are required for optimal platelet-derived FVIII (show F8 ELISA Kits) gene therapy for hemophilia A in the presence of inhibitors.
a genetic link between EGLN1 (show EGLN1 ELISA Kits) 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 ELISA Kits) O and non-blood group (show DARC ELISA Kits) O individuals may therefore be related to the blood group (show DARC ELISA Kits) status of the individual rather than the ABH (show ALKBH ELISA Kits) antigen loading on VWF itself.
Certain VWD-type 2B mutations relieve the need for shear stress to induce LRP1 (show LRP1 ELISA Kits) binding. Enhanced LRP1 (show LRP1 ELISA Kits) 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