Product Specifications for Recombinant Human vWF-A2 Protein, CF
E. coli-derived human vWF-A2 protein Asp1498-Val1665, with an N-terminal Met and 6-His tag
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
<1.0 EU per 1 μg of the protein by the LAL method.
N-terminal sequence Analysis
Predicted Molecular Mass
18 kDa, reducing conditions
Measured by its ability to be used as a protein substrate for ADAMTS13. >50% of rhvWF-A2 is cleaved as measured under the described conditions.
Formulation, Preparation and Storage
What does CF mean?
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our
Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant
protein to be stored at a more dilute concentration.
The carrier free version does not contain BSA.
What formulation is right for me?
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or
as an ELISA standard.
In contrast, the carrier free protein is recommended for applications, in which the presence of BSA
Supplied as a 0.2 μm filtered solution in Tris, NaCl and Glycerol.
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
6 months from date of receipt, -20 to -70 °C as supplied.
3 months, -20 to -70 °C under sterile conditions after opening.
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 recombinant human vWF-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.
von Willebrand Factor A2 Domain
Entrez Gene IDs
7450 (Human); 22371 (Mouse); 116669 (Rat)
F8VWF, VWD, VWF von Willebrand factor, vWF-A2, vWFA2
Citations for Recombinant Human vWF-A2 Protein, CF
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Product Documents for Recombinant Human vWF-A2 Protein, CF
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