Von Willebrand Factor, Factor VIII Free Protein

Multimeric Structure of von Willebrand Factor: Each vWF monomer (Mr = 260kD) contains a Factor VIII binding site near the NH2-terminal end of the molecule. The monomers are joined end-to-end (NH2 to NH2 and COOH to COOH) by disulfide bonds to form large multimers. The mature multimers can bind one Factor VIII molecule per monomeric subunit.

In addition to its role in platelet plug formation, vWF is also responsible for the binding and transport of Factor VIII (Antihemophilic Aactor) in plasma (15). It appears that this latter event is responsible for both the stability and effective delivery of functional Factor VIII. Studies indicate that Factor VIII binds to the NH2-terminal portion of the mature vWF subunit with a stoichiometry of one Factor VIII molecule per vWF monomer (16,17).
The single chain vWF monomer contains a large number of cysteine residues at both the NH2-terminal and COOH-terminal ends, which are involved in the multimer formation. Carbohydrate analyses indicate that nearly 15% of the mass of vWF is contributed by carbohydrate (18). It appears that the carbohydrate serves to protect vWF from proteolysis, but is not necessary for functional activity or multimer formation.

Small volumes of Von Willebrand Factor, Factor VIII Free protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

MBS635231 is a protein targeting Von Willebrand Factor, Factor VIII Free. Also known as Von Willebrand Factor, Factor VIII Free, Human (vWF, Factor VIII Related Antigen). Host: Human plasma.