The secreted recombinant human vWF consists of 2802 amino acids after removal of the signal peptide and has a predicted molecular mass of 308 kDa. Purified rhvWf exists as both the pro form with the pro peptide (307 kDa) and the mature form (226 kDa), which migrates as doublets with apparent molecular mass of 260 and 350 kDa respectively in SDS-PAGE under reducing conditions due to glycosylation.
Lyophilized from sterile PBS, pH 7.4 Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃ Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Von Willebrand Factor/vWF Protein, Human, Recombinant (His Tag): Images
Von Willebrand Factor/vWF Protein, Human, Recombinant (His Tag): Alternative Names
F8VWF Protein, Human; Von Willebrand Factor Protein, Human; VWD Protein, Human
Von Willebrand Factor/vWF Background Information
Von Willebrand Factor (VWF) is a multimeric glycoprotein involved in hemostasis in blood, binds receptors on the surface of platelets and in connective tissue, thereby mediating the adhesion of platelets to sites of vascular injury. From studies it appears that VWF protein uncoils under these circumstances, decelerating passing platelets. VWF protein is deficient or defective in von Willebrand disease (VWD) and is involved in a large number of other diseases, including thrombosis, thrombotic thrombocytopenic purpura, Stroke, Heyde's syndrome, possibly hemolytic-uremic syndrome and so on.
von Willebrand factor
Sadler JE. (1998) Biochemistry and genetics of von Willebrand factor. Annu Rev Biochem, 67: 395-424.
Batlle J, et al. (2009) Von Willebrand factor/factor VIII concentrates in the treatment of von Willebrand disease. Blood Coagul Fibrinolysis. 20(2):89-100.
Sadler JE. (2009) von Willebrand factor assembly and secretion. J Thromb Haemost. 7 Suppl 1:24-7.
Auton M, et al. (2010) The mechanism of VWF-mediated platelet GPIbalpha binding. Biophys J. 99(4):1192-201.
Bowen DJ. (2010) Sugar targets VWF for the chop. Blood. 115(13):2565.
Lpez JA, et al. (2010) VWF self-association: more bands for the buck. Blood. 116(19):3693-4.
Novel antibodies against GPIbα inhibit pulmonary metastasis by affecting vWF-GPIbα interaction
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