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Recombinant Human vWF-A2 Protein, CF

Bio-Techne includes R&D Systems | Catalog # 2764-WF

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2764-WF-050

Key Product Details

Source

E. coli

Accession #

Conjugate

Unconjugated

Applications

Enzyme Activity

Product Specifications

Source

E. coli-derived human vWF-A2 protein
Asp1498-Val1665, with an N-terminal Met and 6-His tag

Purity

>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met

Predicted Molecular Mass

20 kDa

SDS-PAGE

18 kDa, reducing conditions

Activity

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

2764-WF
Formulation Supplied as a 0.2 μm filtered solution in Tris, NaCl and Glycerol.
Shipping 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.

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 recombinant human vWF-A2 contains the A2 domain of vWF.

References

  1. Sadler, J. E. (1998) Annu. Rev. Biochem. 67:395.
  2. Ruggeri, Z. M. (2003) Cur. Opin. Hemat. 10:142.
  3. Michiels, J. J. et al. (2006) Clin. Appl. Thromb. Hemost. 12:397.
  4. Groot, E. et al. (2007) Cur. Opin. Hemat. 14:284.
  5. Lenting, P. J. et al. (2007) J. Thromb. Haemos. 5:1353.

Long Name

von Willebrand Factor A2 Domain

Alternate Names

F8VWF, vWFA2

Entrez Gene IDs

7450 (Human); 22371 (Mouse); 116669 (Rat)

Gene Symbol

VWF

UniProt

Additional vWF-A2 Products

Product Documents for Recombinant Human vWF-A2 Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human vWF-A2 Protein, CF

For research use only