• Purity

  >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie? Blue Staining.

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its binding ability in a functional ELISA. When Human Activated Protein C is immobilized at 3 μg/mL (100 μL/well), the concentration of Recombinant Mouse EPCR that produces 50% of the optimal binding response is approximately 0.1-0.6 μg/mL

• Source

  Mouse myeloma cell line, NS0-derived Leu18-Ser214, with a C-terminal 10-His tag

• Accession #

• N-terminal Sequence    
  Analysis

  Leu18

• Predicted Molecular Mass

  24 kDa

• SDS-PAGE

  36-47 kDa, reducing conditions

Background: EPCR

The endothelial protein C receptor (EPCR), also known as CD201, is an approximately 50 kDa transmembrane glycoprotein expressed on vascular endothelial cells and functions as a negative regulator of thrombosis (1). Mature mouse EPCR consists of a 197 amino acid extracellular domain (ECD), a 21 aa transmembrane segment, and a 7 aa cytoplasmic tail (2). Within the ECD, mouse EPCR shares 65% and 85% aa sequence identity with human and rat EPCR, respectively. EPCR inhibits thrombosis through its interactions with Protein C, activated Protein C (APC), and Coagulation Factors VII, and VIIa (3, 4). It enhances the activation of Protein C in response to complexes of Thrombin-Thrombomodulin (5). In humans, a soluble form of EPCR can be produced by alternative splicing or ADAM17/TACE mediated shedding (6-9), and this protein inhibits the anti-coagulant activity of APC (10, 11). EPCR can be degraded on the surface of endothelial cells by Neutrophil Elastase (12). Activation of EPCR also protects vascular endothelial cells from Thrombin-induced apoptosis (13). EPCR binds to CD11b/CD18 (Mac-1) on monocytes and mediates monocyte adhesion to the vascular endothelium (14). In addition, EPCR binds to the antigen receptor on gamma δ T cells (15), promotes hematopoietic stem cell retention in the bone marrow (9), and binds to surface proteins of some species of Plasmodium, contributing to pathogenicity in severe malaria (16).

• References:

1. Montes, R. et al. (2012) Thromb. Haemost. 107:815.

2. Fukudome, K. and C.T. Esmon (1995) J. Biol. Chem. 270:5571.

3. Fukudome, K. and C.T. Esmon (1994) J. Biol. Chem. 269:26486.

4. Ghosh, S. et al. (2007) J. Biol. Chem. 282:11849.

5. Stearns-Kurosawa, D.J. et al. (1996) Proc. Natl. Acad. Sci. USA 93:10212.

6. Saposnik, B. et al. (2008) Blood 111:3442.

7. Qu, D. et al. (2007) J. Thromb. Haemost. 5:395.

8. Xu, J. et al. (2000) J. Biol. Chem. 275:6038.

9. Gur-Cohen, S. et al. (2015) Nat. Med. 21:1307.

10. Kurosawa, S. et al. (1997) J. Clin. Invest. 100:411.

11. Liaw, P.C. et al. (2000) J. Biol. Chem. 275:5447.

12. Villegas-Mendez, A. et al. (2007) J. Thromb. Haemost. 5:980.

13. Bae, J.-S. et al. (2007) Blood 110:3909.

14. Fink, K. et al. (2013) PLoS One 8:e53103.

15. Willcox, C.R. et al. (2012) Nat. Immunol. 13:872.

16. Turner, L. et al. (2013) Nature 498:502.

• Long Name:

  Endothelial Protein C Receptor

• Entrez Gene IDs:

  10544 (Human); 19124 (Mouse)

• Alternate Names:

  APC receptor; CCCA; CCD41; CCD41centrosome-associated protein; CD201 antigen; CD201; centrocyclin; Endothelial cell protein C receptor; endothelial protein C receptor; EPCR; EPCRMGC23024; PROCR; protein C receptor, endothelial