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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 Kits (75) and VWF Proteins (22) and many more products for this protein.
Showing 10 out of 497 products:
Human Monoclonal VWF Primary Antibody for EIA, IHC (fro) - ABIN119340
am Orde, Glaesener, Exner, Gerner: [Results of extensive cervical laminectomy] in Zeitschrift für Orthopädie und ihre Grenzgebiete 1993
Show all 11 references for ABIN119340
Human Polyclonal VWF Primary Antibody for IHC (p) - ABIN115301
Bukh, Ingerslev, Stenbjerg, Muoller: The multimeric structure of plasma F VIII:RAg studied by electroelution and immunoperoxidase detection. in Thrombosis research 1986
Show all 3 references for ABIN115301
Human Monoclonal VWF Primary Antibody for IHC (fro), IHC (p) - ABIN114682
Naiem, Gerdes, Abdulaziz, Sunderland, Allington, Stein, Mason: The value of immunohistological screening in the production of monoclonal antibodies. in Journal of immunological methods 1982
Show all 2 references for ABIN114682
Human Polyclonal VWF Primary Antibody for IHC, ELISA - ABIN1585505
Wang, Fan, Yu, Liao, Zhao, Mandeville, Guo, Lo, Wang: Effects of tissue plasminogen activator and annexin A2 combination therapy on long-term neurological outcomes of rat focal embolic stroke. in Stroke; a journal of cerebral circulation 2014
Human Polyclonal VWF Primary Antibody for IF (cc), IF (p) - ABIN670506
Du, Wang, Zhao, Li, Kong, Yang, Zhang: Gradient nanofibrous chitosan/poly ?-caprolactone scaffolds as extracellular microenvironments for vascular tissue engineering. in Biomaterials 2011
ADAMTS13 (show ADAMTS13 Antibodies) is the key protease that regulates the multimeric state of VWF. Without ADAMTS13 (show ADAMTS13 Antibodies), VWF multimers can grow to pathologically large sizes. This is a risk factor for the life-threatening condition thrombotic thrombocytopenic purpura (TTP (show ADAMTS13 Antibodies))
Stroke in human immunodeficiency virus infection is associated with a prothrombotic state, characterized by elevated von Willebrand factor and low ADAMTS13 (show ADAMTS13 Antibodies) levels
An in vitro model for LVAD associated aVWD demonstrated that ADAMTS-13 (show ADAMTS13 Antibodies) 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 Antibodies) 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 Antibodies)-mediated proteolysis. When GPIbalpha (show GP1BA Antibodies) participated, there was a dramatically increased proteolytic cleavage of VWF by ADAMTS13 (show ADAMTS13 Antibodies) 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 Antibodies)+)binding site and vicinal cysteine disulfide bond to control unfolding and ADAMTS13 (show ADAMTS13 Antibodies) 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 Antibodies) in treating VWD.
alterations in glycosylation of vWF and other adhesion proteins associated with the targeting of the alpha1,3-Gal (show GAL Antibodies)-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 Antibodies) 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 Antibodies))beta(1)-collagen interaction contribute to platelet adhesion under high shear stress; integrin alpha(II (show GSTA3 Antibodies))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 Antibodies) Regulates Endothelial Exocytosis of von Willebrand Factor
Both platelet-VWF and plasma-VWF are required for optimal platelet-derived FVIII (show F8 Antibodies) gene therapy for hemophilia A in the presence of inhibitors.
a genetic link between EGLN1 (show EGLN1 Antibodies) 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 Antibodies) O and non-blood group (show DARC Antibodies) O individuals may therefore be related to the blood group (show DARC Antibodies) status of the individual rather than the ABH (show ALKBH Antibodies) antigen loading on VWF itself.
Certain VWD-type 2B mutations relieve the need for shear stress to induce LRP1 (show LRP1 Antibodies) binding. Enhanced LRP1 (show LRP1 Antibodies) 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