Human vWF-A2 Antibody Summary
Accession # NP_000543
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.
Detection of Human vWF‑A2 by Western Blot. Western blot shows lysates of HUVEC human umbilical vein endothelial cells. PVDF membrane was probed with 0.5 µg/mL of Sheep Anti-Human vWF-A2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2764) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). Specific bands were detected for vWF-A2 at approximately 250-460 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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 22 aa signal peptide, 741 aa propeptide and mature vWF monomer of 2050 aa (1‑4). The pro-vWF undergoes dimerization in the endoplasmic reticulum (ER) through C-terminal “cysteine-knot” (CK) domain. The pro-vWF dimmers are transported to Golgi and form multimers by forming disulfide bond in amino‑terminal region of the mature form. The proteolytic processing of pro-region also occurs in Golgi. The matured 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 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 change to expose a binding site for glycoprotein Ib alpha. As a result, vWF facilitates 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.
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- Ruggeri, Z. M. (2003) Cur. Opin. Hemat. 10:142.
- Michiels, J. J. et al. (2006) Clin. Appl. Thromb. Hemost. 12:397.
- Groot, E. et al. (2007) Cur. Opin. Hemat. 14:284.
- Lenting, P. J. et al. (2007) J. Thromb. Haemos. 5:1353.
Citation for Human vWF-A2 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
Coronary angiogenic effect of long-term administration of Nigella sativa
Authors: LI Al Asoom
BMC Complement Altern Med, 2017;17(1):308.
Sample Types: Whole Tissue
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