Recombinant Human EPCR Protein (C-6His)

Name: Recombinant Human EPCR Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0417NP
Availability: InStock

BL-0417NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Endothelial Protein C Receptor is produced by our Mammalian expression system and the target gene encoding Ser18-Ser210 is expressed with a 6His tag at the C-terminus.
Accession	Q9UNN8
Synonym	Endothelial Protein C Receptor; Activated Protein C Receptor; APC Receptor; Endothelial Cell Protein C Receptor; CD201; PROCR; EPCR
Gene Background	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.
Molecular Mass	23.06 KDa
Apmol Mass	35 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.2.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation.
Subcellular Location	Membrane; Single-pass type I membrane protein.
Database References	HGNC: 9452 OMIM: 600646 KEGG: hsa:10544 STRING: 9606.ENSP00000216968 UniGene: PMID: 30048851 this is the first comprehensive study of PROCR signaling in breast cancer cells, and its findings also shed light on the molecular mechanisms of PROCR in stem cells in normal tissue. PMID: 29217770 The activation of PAR-1 on the cell surface of SGC7901 and AGS cells was significantly reduced after the knockdown of EPCR. By contrast, blockade of PAR-1 reduced the proliferation and migration of gastric cells in vitro PMID: 29484413 analysis of DC8 and DC13 PfEMP1 variants reveals that Plasmodium falciparum-infected erythrocytes-endothelial protein C receptor interaction may be prevented by plasma components under physiological conditions PMID: 29339517 Low EPCR expression is associated with meningococcal purpura fulminans. PMID: 29630665 Our findings suggested that breast cancer patients with expression of PROCR is more prone to suffer from distant metastasis and bad clinical outcomes. PMID: 28756987 Plasma levels of Ang2 were associated with markers of malaria severity and levels of var transcripts encoding P. falciparum Erythrocyte Membrane Protein 1 (PfEMP1) containing Cysteine Rich Inter Domain Region alpha1 (CIDRalpha1) domains predicted to bind Endothelial Protein C receptor (EPCR). PMID: 27784899 The EPCR rs867186-GG genotype is associated with increased soluble protein, and it could mediate protection against severe malaria. PMID: 27255786 The data indicate that EPCR can regulate p63, is associated with highly proliferative keratinocytes, and is a potential human epidermal stem cell marker. PMID: 28480559 Analysis of a cohort of breast cancer patients revealed an association of high EPCR levels with adverse clinical outcome. Interestingly, EPCR knockdown did not affect cell growth kinetics in 2D but reduced cell growth in 3D cultures. EPCR silencing reduced primary tumor growth and secondary outgrowths at metastatic sites. EPCR via SPOCK1 confers a cell growth advantage in 3D promoting breast tumorigenesis and metastasis. PMID: 28103946 analysis of renal endothelial PROCR expression and shedding during diabetic nephropathy PMID: 26990852 EPCR occupancy recruits G-protein coupled receptor kinase 5, thereby inducing beta-arrestin-2 biased PAR1 signaling by both APC and thrombin. In PMID: 27561318 EPCR polymorphisms may be associated with increased risk of sepsis, but this has no effect on the release of soluble EPCR in patients with sepsis. PMID: 28415941 Elevated endothelium-related mediators (vWF, E-selectin and EPCR) appear to participate in the development of pancreatic necrosis and may be a potential indicator of overall prognosis. PMID: 28007459 The results showed that AS-IV could significantly inhibit PMA-induced EPCR shedding. PMID: 28367652 CORM-2 protects human umbilical vein endothelial cells from lipopolysaccharide-induced injury, by way of suppressing NF-kappaB activity, which downregulates TM and EPCR mRNAs. It also decreases MMP-2 expression and prevents the shedding of TM and EPCR from the surface of endothelial cells, so as to preserve their protective effect. PMID: 28538400 This study shows that ICAM-1 is a coreceptor for a subset of EPCR-binding Plasmodium falciparum parasites and provides the first evidence of how EPCR and ICAM-1 interact to mediate parasite binding to both resting and TNF-alpha-activated primary brain and lung endothelial cells. PMID: 27406562 This study demonstrates that impaired EPCR function can be detected by thrombin generation and clot lysis assays on cells expressing thrombomodulin and EPCR. Deficiency in EPCR has procoagulant effects that lead to a delay in clot lysis. PMID: 28219843 Observations that binding of P. falciparum erythrocyte membrane protein 1 to EPCR results in an acquired functional protein C system deficiency support the new paradigm that EPCR plays a central role in the pathogenesis of severe malaria. [review] PMID: 27207424 data suggest that either the lack of the protective EPCR 4678C allele or the presence of EPCR 4600G allele may be associated with earlier development of thrombosis. PMID: 25760048 These data suggest that 6936A/G polymorphism is a risk factor for deep venous thrombosis and is associated with elevated plasma levels of soluble EPCR, while 4678G/C polymorphism plays a role in protection against deep venous thrombosis. PMID: 26340463 Upon ICU admission, sEPCR levels in initially non-septic critically-ill patients appear elevated in the subjects who will subsequently become septic PMID: 25220546 These data reveal a previously unknown functional heterogeneity in the interaction between Plasmodium falciparum PfEMP1 CIDRalpha1domain binding to EPCR and have major implications for understanding the distinct clinical pathologies of cerebral malaria. PMID: 26118955 Overall, these findings reveal a much greater complexity of how Plasmodium falciparum PfEMP1 CIDRalpha1 domain-expressing parasites may modulate malaria pathogenesis through EPCR adhesion. PMID: 26119044 In this Tanzanian population, neither PROCR haplotype nor level of soluble EPCR was associated with severe malaria. PMID: 26620701 Serum soluble EPCR is elevated in Alzheimer's disease. The degree of cognitive impairment is significantly correlated with serum sEPCR levels in Alzheimer's disease and mild cognitive impairment patients and healthy controls. PMID: 25588409 Report activation of protein C and down-regulation of EPCR in trophobolasts stimulated with TNF-alpha. PMID: 25667200 This effect of EPCR may be dependent on PAR1. PMID: 25895599 results did not conclusively identify a direct role of sEPCR in HSP, but our findings warrant further investigations, especially in severe HSP cases characterized by gastrointestinal bleeding or renal involvement PMID: 24308805 The degree of arteriovenous fistula stenosis was not correlated with serum EPCR PMID: 24627030 results demonstrate that EPCR is overexpressed and mediates the aggressive behavior of rheumatoid synovial fibroblasts, and is likely driven by group V secretory phospholipase A2 PMID: 24495480 Individuals exposed to high levels of Plasmodium falciparum PfEMP1 acquire antibodies to EPCR-binding CIDR domains early in life. PMID: 26015475 genetic variation in the PROCR gene in our study population does not influence susceptibility to major severe malaria phenotypes PMID: 25541704 Low PROCR mRNA expression levels associated with a poor prognosis in patients with disseminated intravascular coagulation (DIC) represents an exhaustion of the natural anticoagulant system, and reflects the final decompensate stage of DIC. PMID: 25246042 Increased coagulation activity and genetic polymorphisms in the F5, F10 and EPCR genes are associated with breast cancer. PMID: 25407022 It was concluded that measuring EPCR levels at admission could provide an early biological marker of the outcome of cerebral malaria. PMID: 25425698 EPCR expression in breast cancer cells, despite having initial growth advantage, may have a role in limiting cancer progression at an advanced stage PMID: 24024878 Blocking antibodies to EPCR attenuate in vivo tumor growth and proliferation specifically of EPCR(+) cells on defined integrin matrices in vitro. PMID: 24862151 Elevated levels of soluble endothelial protein C receptor, a sensitive marker of endothelial damage, indicated a low level of inflammation and coagulation activation in Maraviroc treated patients not picked up by other widely used markers. PMID: 22715361 Piperlonguminine might have potential as an anti-sEPCR shedding reagent against PMA-mediated EPCR shedding. PMID: 24127121 The association of PROCR rs867186 with severe malaria is examined in Thai population and showed significant association with protection from severe malaria. PMID: 24635948 The study suggests a putative role of EPCR SNPs in the development of thrombosis in multiple myeloma patients. PMID: 23993723 The EPCR AA genotype was significantly more frequent in the healthy volunteers free of venous thrombosis. PMID: 24158116 3 polymorphisms in the EPCR gene were genotyped in 389 critically ill Greek patients to assess genetic risk for developing severe sepsis or septic shock. H2 carriers had an excess of ss/ss vs. genotypes H1 and H3. PMID: 23881209 PROCR H1 protects against venous thromboembolism. There is an increased risk of VTE associated with the H3 haplotype. PMID: 24436369 sEPCR acts on the innate immune response by decreasing effector cells such as natural killer and T helper cells (TH2, TH17 and TH21). PMID: 23877403 Increased EPCR-levels correlate with accelerated mortality in patients with melioidosis. PMID: 23875041 EPCR is expressed not only by a wide range of human malignant hematological cells but also the detection of plasma sEPCR levels provides a powerful insight into thrombotic risk assessment in cancer patients, especially when it surpasses 200 ng/mL. PMID: 23342274 conclude that urinary sEPCR could be a novel non-invasive biomarker of antibody mediated rejection in renal transplantation PMID: 23717683 Our data suggest that mutations that impair PC-EPCR interactions may be associated with an increased risk of venous thromboembolism. PMID: 24051141

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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