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
>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:
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).
Montes, R. et al. (2012) Thromb. Haemost. 107:815.
Fukudome, K. and C.T. Esmon (1995) J. Biol. Chem. 270:5571.
Fukudome, K. and C.T. Esmon (1994) J. Biol. Chem. 269:26486.
Ghosh, S. et al. (2007) J. Biol. Chem. 282:11849.
Stearns-Kurosawa, D.J. et al. (1996) Proc. Natl. Acad. Sci. USA 93:10212.
Saposnik, B. et al. (2008) Blood 111:3442.
Qu, D. et al. (2007) J. Thromb. Haemost. 5:395.
Xu, J. et al. (2000) J. Biol. Chem. 275:6038.
Gur-Cohen, S. et al. (2015) Nat. Med. 21:1307.
Kurosawa, S. et al. (1997) J. Clin. Invest. 100:411.
Liaw, P.C. et al. (2000) J. Biol. Chem. 275:5447.
Villegas-Mendez, A. et al. (2007) J. Thromb. Haemost. 5:980.
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