Human vWF-A2 Antibody Summary
Asp1498-Val1665
Accession # P04275
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.
Scientific Data

Detection of vWF‑A2 in Human Placenta. vWF‑A2 was detected in immersion fixed paraffin-embedded sections of human placenta using Mouse Anti-Human vWF‑A2 Monoclonal Antibody (Catalog # MAB11543) at 25 µg/ml for 1 hour at room temperature followed by incubation with the Anti-Mouse IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC001) or the HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using VisUCyte Antigen Retrieval Reagent-Basic (Catalog # VCTS021). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the cytoplasm of endothelial cells. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
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.
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 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.
- Sadler, J.E. (1998) Annu. Rev. Biochem. 67:395.
- 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.
Product Datasheets
FAQs
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Isotype Controls
Reconstitution Buffers
Secondary Antibodies
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