Leu18-Ser214, with C-terminal Human IgG Fc LCNSDGSQSLHMLQISYFQDNHHVRHQGNASLGKLLTHTLEGPSQNVTILQLQPWQDPESWERTESGLQIYLTQFESLVKLVYRERKENVFFPLTVSCSLGCELPEEEEEGSEPHVFFDVAVNGSAFVSFRPKTAVWVSGSQEPSKAANFTLKQLNAYNRTRYELQEFLQDTCVEFLENHITTQNMKGSQTGRSYTSIEGRMDPKSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
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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. EPCR inhibits thrombosis through its interactions with Protein C, activated Protein C (APC), and Coagulation Factors VII, and VIIa. It enhances the activation of Protein C in response to complexes of Thrombin-Thrombomodulin. In humans, a soluble form of EPCR can be produced by alternative splicing or ADAM17/TACE mediated shedding, and this protein inhibits the anti-coagulant activity of APC. EPCR can be degraded on the surface of endothelial cells by Neutrophil Elastase. Activation of EPCR also protects vascular endothelial cells from Thrombin-induced apoptosis.EPCR binds to CD11b/CD18 (Mac-1) on monocytes and mediates monocyte adhesion to the vascular endothelium. In addition, EPCR binds to the antigen receptor on gamma δ T cells, promotes hematopoietic stem cell retention in the bone marrow, and binds to surface proteins of some species of Plasmodium, contributing to pathogenicity in severe malaria.
1μg (R: reducing condition, N: non-reducing condition).
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