Recombinant Human Endothelial Protein C Receptor/EPCR is produced with our mammalian expression system in human cells. The target protein is expressed with sequence (Ser18-Ser210) of Human EPCR fused with a polyhistidine tag at the C-terminus.
Reinheit
> 95 % as determined by reducing SDS-PAGE.
Sterilität
0.2 μm filtered
Endotoxin-Niveau
Less than 0.1 ng/μg (1 IEU/μg) as determined by LAL test
Crystallography grade
PROCR
Spezies: Human
Wirt: Escherichia coli (E. coli)
Recombinant
>95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
SDS, WB, ELISA, Crys
Crystallography grade
PROCR
Spezies: Human
Wirt: Insektenzellen
Recombinant
>95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
SDS, WB, ELISA, Crys
PROCR
Spezies: Huhn
Wirt: Escherichia coli (E. coli)
Recombinant
> 97 %
SDS, WB, Imm, PC
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Rekonstitution
It is not recommended to reconstitute to a concentration less than 100 μg/mL. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Buffer
Lyophilized from a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.2.
Handhabung
Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
Lagerung
4 °C/-20 °C/-80 °C
Informationen zur Lagerung
Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
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Sub Type
Fusionprotein
Hintergrund
Endothelial Protein C Receptor (EPCR) is a Vitamin K-dependent Serine Protease that plays a major role in blood coagulation. Binding of Protein C to EPCR leads to the proteolytic activation of PAR1 (Protease-Activated Receptor 1) on endothelial cells and subsequent up-regulation of Protein C-induced genes. EPCR is a type I transmembrane glycoprotein in the CD1/MHC family. It is expressed most strongly in the endothelial cells of arteries and veins in heart and lung. Membrane bound EPCR is released by metalloproteolytic cleavage to generate the soluble receptor. The extracellular domain of human and mouse EPCR shares approximately 61% amino acid sequence homology. EPCR plays an important role in augmenting Protein C activation by the Thrombin-Thrombomodulin complex and in regulating blood coagulation and inflammation. EPCR is found primarily on endothelial cells. Deletion of EPCR function results in embryonic death, at least in part due to placental thrombosis. Alternative Names: Endothelial Protein C Receptor, Activated Protein C Receptor, APC Receptor, Endothelial Cell Protein C Receptor, CD201, PROCR, EPCR