vWF Protein Price Information
vWF Protein Product Information
||A DNA sequence encoding the pro form of human von Willebrand factor (NP_000543.2) (Met 1- Lys 2813) was expressed with a C-terminal polyhistidine tag.
vWF Protein QC Testing
||> 75%, as determined by SDS-PAGE
||< 1.0 EU per 1μg of the protein as determined by the LAL method.
||Samples are stable for up to twelve months from date of receipt at -70℃
|Predicted N terminal:
||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
- Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
- Please contact us for any concerns or special requirements.
vWF Protein Usage Guide
||Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage and be used as soon as possible. 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.
vWF Protein Related Products & Topics
vWF Protein Description
von Willebrand factor (vWF) is a large adhesive glycoprotein synthesized in megakaryocytes and endothelial cells and stored in platelet α-granules and Weibel-Palade bodies, respectively. vWF performs two important hemostatic functions as both an antihemophilic factor (factor VIII)carrier and a platelet-vessel wall mediator in the blood coagulation system. vWF regulates the synthesis and cofactor activity of FVIII circulating in plasma and protects it from degradation or inactivation as a noncovalent complex with FVIII. In high shear-stressed environment, vWF undergoes conformational change to expose a binding site for its receptor GPIbα and facilitates aggregation of platelets. The mature and efficient multimers of vWF circulates in plasma as a series ranging from 500 to 20 000 kDa. The size of the multimers is regulated through proteolysis within the A2 domain by a specific protease ADAMTS13 (a disintegrin-like and metalloprotease with thrombospondin type I repeats-13) and recent studies have suggested that this processing is regulated by FVIII under shear stress. Function defective or deficiency of vWF results in a secondary decrease of FVIII activity and a bleeding tendency known as von Willebrand disease, as well as a large number of other diseases, including thrombotic thrombocytopenic purpura (TTP), Heyde's syndrome, and possibly hemolytic-uremic syndrome.
- Sadler J E. 1998, Annu Rev Biochem. 67: 395-424.
- Nogami K. et al., 2002, Blood. 99: 3993-8.
- Moake JL. et al., 2004, Semin Hematol. 41: 4-14.
- Zanardelli S. et al., 2006, J Biol Chem. 281: 1555-63.
- Levy GG. et al., 2005, Blood. 106: 11-7.
- Cao W. et al., 2008, Proc Natl Acad Sci. 105: 7416-21.