Von Willebrand factor (VWF) is a multifunctional plasma glycoprotein essential for hemostasis and vascular biology. VWF's primary function is promoting platelet adhesion at sites of vascular injury by forming a molecular bridge between subendothelial collagen and platelet-surface receptor complex GPIb-IX-V 1. Additionally, VWF serves as a chaperone for coagulation factor VIII (FVIII), protecting it from premature clearance and delivering it to injury sites 1 2. In von Willebrand disease patients, VWF absence leads to premature loss of endogenous FVIII, creating a dual hemostatic defect 2. VWF expression varies significantly among different endothelial cell types, with particularly high levels in lymphatic endothelial cells where it co-localizes with FVIII in Weibel-Palade bodies 3. Beyond hemostasis, VWF plays important roles in inflammation by directing Weibel-Palade body biogenesis and recruiting leukocytes either directly or through platelet-mediated interactions 1. VWF mutations cause three types of von Willebrand disease, with type 1 being most common and associated with reduced VWF levels 4. The protein's activity is regulated by ADAMTS13 protease, which cleaves VWF multimers under physiological conditions 5.