E6280
Anti-Endothelial Cell Protein C Receptor antibody, Rat monoclonal
clone RCR-252, purified from hybridoma cell culture
Synonym(s):
Anti-EPCR
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About This Item
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biological source
rat
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
RCR-252, monoclonal
form
buffered aqueous solution
mol wt
antigen 49 kDa
species reactivity
human
technique(s)
flow cytometry: 5-20 μg/mL using HUVEC cells
microarray: suitable
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... PROCR(10544)
General description
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.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Mark R Gillrie et al.
Cellular microbiology, 17(12), 1883-1899 (2015-06-30)
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
Marion Avril et al.
mBio, 7(4) (2016-07-14)
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
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)
Alice G Vassiliou et al.
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
Maria Bernabeu et al.
mBio, 10(3) (2019-05-30)
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
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