Von Willebrand Factor Proteins (VWF)

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 (519) and VWF Kits (104) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
VWF 7450 P04275
VWF 116669  
VWF 22371 Q8CIZ8
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Top VWF Proteins at antibodies-online.com

Showing 10 out of 21 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
Insect Cells Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 70 Days
CHO Cells Human His tag 100 μg Log in to see 20 to 21 Days
Escherichia coli (E. coli) Human His tag 100 μg Log in to see 15 to 18 Days
Escherichia coli (E. coli) Wild boar His tag 100 μg Log in to see 15 to 18 Days
Escherichia coli (E. coli) Human His-SUMO Tag   50 μg Log in to see 11 Days
Escherichia coli (E. coli) Rat His tag 100 μg Log in to see 15 to 18 Days
Insect cells (Sf9) Human DYKDDDDK Tag Validation with Western Blot 20 μg Log in to see 10 to 12 Days
Escherichia coli (E. coli) Mouse His tag 100 μg Log in to see 15 to 18 Days
Yeast Rat His tag   1 mg Log in to see 60 to 71 Days
Human Human Un-conjugated   100 μg Log in to see 6 to 8 Days

VWF Proteins by Origin and Source

Origin Expressed in Conjugate
Human , , , ,
, ,
Rat (Rattus) ,

Mouse (Murine)

More Proteins for Von Willebrand Factor (VWF) Interaction Partners

Human Von Willebrand Factor (VWF) interaction partners

  1. VWF binding to MMRN1 (show MMRN1 Proteins) was enhanced by shear exposure and ristocetin, and required VWF A1A2A3 region, specifically the A1 and A3 domains.

  2. coronary thrombi in STEMI patients resistant to fibrinolysis are characterised by higher fibrin, P-selectin (show SELP Proteins) and VWF content than lysis-sensitive thrombi

  3. We compared the classical Sanger sequencing approach and NGS to assess the value-added effect on the analysis of the mutation distribution in different types of VWD. Sixty-two different VWF mutations were identified, 27 of which had not been previously described. NGS detected 26 additional mutations, contributing to a broad overview of the mutant alleles present in each VWD type.

  4. These observations support the hypothesis that a significantly reduced ADAMTS13 (show ADAMTS13 Proteins)/VWF ratio in the coronary artery flow plays a pathogenic role in acute coronary syndromes (ACS (show PLA2G15 Proteins)) and suggest that transition from laminar to turbulent flow at sites of coronary stenosis further enhances VWF activation and deposition.

  5. the major genetic factors affecting plasma VWF levels, i.e. variants at ABO (show ABO Proteins), VWF and a locus on chromosome 2, operate primarily through their effects on VWF clearance

  6. The unique phenotype of VWD2 type IIC-Miami results from dominant impairment of multimer assembly, an aberrant structure of mutant mature VWF and reduced clearance in vivo

  7. Low ADAMTS-13 (show ADAMTS13 Proteins) activity is associated with an increased risk of coronary heart disease in the elderly, independently of VWF and established cardiovascular risk factors

  8. Very low birth weight preterm neonates have increased numbers of platelets interacting with von Willebrand Factor, and increased GPIbalpha (show GP1BA Proteins) expression on the platelet surface

  9. N-linked glycan truncation causes enhanced clearance of plasma-derived von Willebrand factor; variation in VWF glycosylation may be important in the pathophysiology underlying type 1C VWD

  10. Data suggest that an aspartate at position 1261 is the most critical residue of VWF N-terminal linker for inhibiting binding of VWF A1 domain to GP1BA (show GP1BA Proteins) on platelets in a model simulating blood flow velocity; network of salt bridges between Asp1261 and rest of VWF A1 domain lock N-terminal linker in place such that binding to GP1BA (show GP1BA Proteins) is reduced.

Pig (Porcine) Von Willebrand Factor (VWF) interaction partners

  1. 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.

Cow (Bovine) Von Willebrand Factor (VWF) interaction partners

  1. 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.

  2. 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

Mouse (Murine) Von Willebrand Factor (VWF) interaction partners

  1. Refrigeration-induced binding of VWF to platelets facilitates their rapid clearance by inducing GPIbalpha (show GP1BA Proteins)-mediated signaling.

  2. BLOC-2 (show HPS6 Proteins) subunit HPS6 (show HPS6 Proteins) deficiency affects the tubulation and secretion of von Willebrand factor from mouse endothelial cells

  3. 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.

  4. 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.

  5. ADAMTS13 (show ADAMTS13 Proteins) controls vascular remodeling by modifying VWF reactivity during stroke recovery.

  6. these novel findings support the hypothesis that conformation of the VWF A domains plays a critical role in modulating macrophage-mediated clearance of VWF in vivo.

  7. results revealed localized vascular expression of FVIII (show F8 Proteins) and von Willebrand factor and identified lymphatic endothelial cell as a major cellular source of FVIII (show F8 Proteins) in extrahepatic tissues.

  8. Endothelial cell derivedVWF is the major determinant that mediates VWF-dependent ischemic stroke by promoting postischemic thrombo-inflammation.

  9. VWF deficiency reduces the progression of liver fibrosis, suggesting a mechanistic role of elevated plasma VWF levels in cirrhosis

  10. von Willebrand factor exerts beneficial effects in a mouse sepsis model via recruitment of neutrophils to inflammatory sites.

VWF Protein Profile

Protein Summary

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.

Gene names and symbols associated with Von Willebrand Factor Proteins (VWF)

  • von Willebrand factor (VWF)
  • von Willebrand factor (vwf)
  • von Willebrand factor (Vwf)
  • Von Willebrand factor (Vwf)
  • 6820430P06Rik protein
  • AI551257 protein
  • B130011O06Rik protein
  • C630030D09 protein
  • F8VWF protein
  • si:ch1073-474e24.1 protein
  • VWD protein
  • VWF protein

Protein level used designations for Von Willebrand Factor Proteins (VWF)

von Willebrand factor , coagulation factor VIII VWF

451773 Pan troglodytes
493760 Felis catus
570643 Danio rerio
619381 Monodelphis domestica
722019 Macaca mulatta
7450 Homo sapiens
116669 Rattus norvegicus
399544 Canis lupus familiaris
100009165 Oryctolagus cuniculus
399543 Sus scrofa
280958 Bos taurus
100732530 Cavia porcellus
419031 Gallus gallus
101110931 Ovis aries
22371 Mus musculus
Selected quality suppliers for VWF Proteins (VWF)
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