Anti-endothelial cell protein C receptor antibody, rat monoclonal (EPCR) (rat IgG1 isotype) is derived from the RCR-252 hybridoma produced by the fusion of mouse SP2/0 myeloma cells and cells isolated from the superficial inguinal lymph nodes from Wister rats immunized with human EPCR-positive RE-1 cells. Endothelial protein C receptor (EPCR), also known as activated protein C receptor (APC receptor) is a protein encoded by the PROCR gene in humans. It is predominantly expressed in endothelial. The EPCR is also expressed in small vessels such as capillaries of the alveolar wall in the lung. EPCR is a member of the CD1/major histocompatibility complex superfamily.
Immunogen
human EPCR-positive RE-1 cells.
Application
Anti-endothelial cell protein C receptor antibody, rat monoclonal has been used in flow cytometry (FACS analysis) and in blocking the binding of the antigen presenting cell (APC) ligand to the EPCR.
Biochem/physiol Actions
Endothelial protein C receptor (EPCR) is involved in regulation of the cytoprotective and anticoagulant pathways of protein C. EPCR plays an important role in regulating the inflammatory response. It is also identified as an endothelial receptor for specific P. falciparum erythrocyte membrane protein 1 (PfEMP1) subtypes. EPCR is associated with an increased risk of venous thromboembolism (VTE).
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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The endothelial cell protein C receptor (EPCR) functions as a primary receptor for protein C activation on endothelial cells in arteries, veins, and capillaries
Ye X, et al.
Biochemical and biophysical research communications, 259(3), 671-677 (1999)
Intensive care medicine, 39(10), 1752-1759 (2013-07-25)
Endothelial protein C receptor (EPCR) is expressed mainly in endothelial cells and is involved in regulation of the cytoprotective and anticoagulant pathways of protein C. We assessed whether haplotypes in the EPCR gene modify the risk of severe sepsis and/or
Cerebral malaria is a severe neurological complication associated with sequestration of Plasmodium falciparum-infected erythrocytes (IE) in the brain microvasculature, but the specific binding interactions remain under debate. Here, we have generated an engineered three-dimensional (3D) human brain endothelial microvessel model
Plasmodium falciparum-infected erythrocytes (IRBC) expressing the domain cassettes (DC) 8 and 13 of the cytoadherent ligand P. falciparum erythrocyte membrane protein 1 adhere to the endothelial protein C receptor (EPCR). By interfering with EPCR anti-coagulant and pro-endothelial barrier functions, IRBC adhesion
Intercellular adhesion molecule 1 (ICAM-1) and the endothelial protein C receptor (EPCR) are candidate receptors for the deadly complication cerebral malaria. However, it remains unclear if Plasmodium falciparum parasites with dual binding specificity are involved in cytoadhesion or different parasite
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