Technozym® vWF:CBA ELISA is a research ELISA kit for determination of von Willebrand Factor collagen binding activity. In combination with Technozym® vWF Antigen ELISA, research of von Willebrand disease type 1, 2 and 3 is possible.

The von Willebrand Factor (vWF) is a large, multifunctional glycoprotein, occupying a key position in primary haemostasis. It has a multiple structure with several functions:

  • It is the carrier protein for Factor VIII in plasma; it forms a complex and thus protects Factor VIII from early proteolytic decomposition.
  • It acts as a mediator for platelet aggregation by attaching itself to platelet membrane receptors (GP Ib and GP lIb/IIIa) following previous platelet activation.
  • It plays a part in primary hemostasis by acting as a mediator between adhesioned platelets and the subendothelium (lesioned vascular wall).

In order to analyze the adhesive properties, as a rule the platelet aggregation is measured (measuring system = ristocetin-dependent platelet aggregation). However, this does not reflect the physiological setting nor the function of the vWF. For determining the adhesive properties of the vWF, its binding capacity to collagen serves as a parameter which corresponds to the physiological function of the vWF.

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What is the function of von Willebrand Factor? Briefly describe von Willebrand disease.
von Willebrand factor (vWf) is a glue-like adhesive protein that is responsible for the adhesion of platelets to damaged vascular endothelium. It also carries and protects factor VIII. von Willebrand disease is a hereditary bleeding disorder caused by moderate-to-severe factor VIII deficiency and low-levels of factor VIII-related antigen (substances necessary for blood clotting). Additionally, there is insufficient von Willebrand factor which also helps blood clot. The von Willebrand factor helps platelets to stick to the blood vessel wall and to each other, which is necessary for normal blood clotting.

Visit the vWF product pages for available kits to measure vWF antigen, activity, and collagen binding.