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Recombinant Human EPCR Protein, CF

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When human Activated Protein C is immobilized at 3 μg/mL, 100 μL/well, Recombinant Human EPCR (Catalog # 9557‑ER) binds with an ED50 of 1‑5 μg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human EPCR Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When human Activated Protein C (APC) is immobilized at 3 μg/mL, 100 μL/well, Recombinant Human EPCR binds with an ED50 of 1-5 μg/mL.
Source
Mouse myeloma cell line, NS0-derived human EPCR protein
Ser18-Ser210, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Ser18
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
23 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
36-45 kDa, reducing conditions
Publications
Read Publication using
9557-ER in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human EPCR Protein, CF

  • 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

Background

The endothelial protein C receptor (EPCR), also known as CD201, is a transmembrane glycoprotein expressed on vascular endothelial cells and functions as a negative regulator of thrombosis (1). Mature human EPCR consists of a 193 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 7 aa cytoplasmic tail (2). Within the ECD, human EPCR shares 63% and 66% aa sequence identity with mouse 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).
  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.

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