Human vWF-A2 Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: vWF-A2

von Willebrand Factor (vWF) is a large, multimeric glycoprotein made by endothelial cells and megakaryocytes. The pre-pro-vWF protein contains 2813 amino acids (aa), which consists of a 22 aa signal peptide, a 741 aa propeptide and a mature vWF monomer of 2050 aa (1‑4). The pro-vWF undergoes dimerization in the endoplasmic reticulum (ER) through a C-terminal “cysteine-knot” (CK) domain. The pro-vWF dimers are transported to the Golgi and associate into multimers by forming disulfide bonds in the amino‑terminal region of the mature form. Proteolytic processing of the pro-region also occurs in the Golgi. Mature vWF is stored in Weibel-Pallade bodies in endothelial cells and granules in megakaryocytes and platelets. The unusually-large vWF (ulvWF) multimers released from cells are very efficient in binding to platelets to form thrombus. The population of these highly active ulvWF multimers is controlled by a specific protease, ADAMTS13, which cleaves between residues Tyr1605 and Met1606 in the A2 domain of vWF. In the plasma, vWF appears as a series of large and intermediate size multimers with molecular masses from several thousand to 500 kDa. vWF also performs hemostatic functions (3‑5). In a high shear-stressed environment, vWF undergoes conformational changes to expose a binding site for glycoprotein Ib alpha. As a result, vWF facilitates the aggregation of platelets. In addition to platelet binding, vWF binds coagulation factor VIII to increase the lifetime of FVIII in plasma. The purified rhvWF-A2 contains the A2 domain of vWF.

Product Datasheets

Related Research Areas

• Alpha Granule Soluble Molecules
• Coagulation
• Endothelial Cell Coagulation Molecules
• Endothelial Cell Markers
• Extracellular Matrix Molecules
• Megakaryocytes
• Preeclampsia