ADAMTS13 Active Protein

ADAMTS13 (a disintegrin and metalloproteinase with thrombospondin motifs 13), also known as von Willebran Factor (vWF) cleaving protease, is a member of the family of secreted zinc proteases with a multi-domain structure (1-3). The protein precursors consist of a signal peptide and following domains: pro, catalytic, disintegrin-like, TS type 1 motif, cystein-rich, spacer, a second set of seven TSP1 repeats, and two CUB domins. The only known substrate of ADAMTS13 is vWF, a blood glycoprotein with two homeostatic functions (4). It is required for platelet adhesion to sites of vascular damage and acts as a carrier protein for blood-clotting factor VIII in the circulation. It exists in plasma as multimers, the largest of which effectively mediate platelet adhesion. ADAMTS13 cleaves multimeric vWF in the A2 domain at the position, Tyr 1605-Met 1606. Defect in ADAMTS13 activity is a cause of congenital thrombotic thrombocytopenic purpura (TTP), also known as Upshaw-Schulman syndrome. Lack of ADAMTS13 activity allows unusually large vWF (UlvWF) to occur in plasma (5). These UlvWF multimers have tendency to agglutinate circulating platelets at sites with high levels of shear stress to cause TTP.

Recombinant protein corresponding to Gln34-Trp688 with a C-terminal 10X-His tag from human ADAMTS13 (Accession #NP_620594), expressed in CHO cell line. The purified rhADAMTS13 starts at the N-terminus of the pro domain and ends in the spacer domain.

Small volumes of ADAMTS13 active 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.

MBS636953 is an active protein targeting ADAMTS13. Also known as ADAMTS13, Recombinant, Human (A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 13).