The urokinase plasminogen activator receptor (Upar) plays a multifaceted role in almost every process in which the migration of cells and tissue-remodeling involved such as inflammation, but also in diseases such as arthritis and cancer. Typically,
Upar not in healthy tissue. With carefully orchestrated interactions with protease urokinase plasminogen activator and its inhibitor (plasminogen activator inhibitor-1), Upar localize cascade of proteolytic activity, allowing the (patho) physiological cell migration. In addition, through interaction with various cell membrane proteins, such as vitronectin and various integrin, Upar played a significant, but not yet fully understood, role in the differentiation and proliferation of cells, affects also the development of the disease.
The implications of this process, either for diagnostic or therapeutic, has received much attention in oncology, but only limited outside. Nonetheless, Upar role in different diseases provides many opportunities to exploit new applications for targeting. Especially in the fields of oncology, cardiology, rheumatology, neurology, and infectious diseases, Upar targeted molecular imaging can offer insights for a new direction in the selection of the diagnosis, monitoring or treatment.
A thrombolytic therapy using diagnostic ultrasound combined with microbubbles targeted RGDS and urokinase in a rabbit model
This study aims to explore thrombolysis therapy based on ultrasound combined with urokinase and Arg-Gly-Asp sequence (RGDS) -targeted microbubbles to evaluate the histological changes in a rabbit model of thrombotic. Forty-two New Zealand rabbits displaying platelet-rich thrombi in the femoral artery at random (n = 6 / group): ultrasound alone (AS); Any urokinase (UK); Ultrasound plus non-targeted microbubbles (US + M); Ultrasound plus RGDS-targeted microbubbles (US + R); RGDS targeted microbubbles plus urokinase (R + UK); Ultrasound, micro bubbles and non-targeted urokinase (AS + M + UK); and ultrasound, microbubbles targeted RGDS and urokinase (AS + R + UK) group. Diagnostic ultrasound is used transcutaneously on thrombus for 30 minutes.
We evaluated the effect of thrombolytic based ultrasound detection of thrombus, blood flow, and histological observations. Among all study groups, complete recanalization was achieved in the group AS + R + UK. Hematoxylin and eosin staining showed that the thrombus is completely dissolved.
Scanning electron microscope examination showed that the structure of the fiber network of the thrombus is broken. Transmission electron microscopy showed that the thrombus is broken down into particles high electron-dense. Histology for von Willebrand factor and tissue factor negative both in the US group + R + UK. The study reveals that thrombolytic therapy comprising RGDS diagnostic ultrasound with microbubbles targeted and urokinase plus.
PHI and uPA was significantly higher in patients with BPH and PCa relevant to healthy controls (p ≤ 0.001). Both markers outperformed all biomarkers were assessed and showed the highest area under the curve (AUC) in the ROC curve analysis. Both were significantly higher in patients with PCa {Gleason score ≥ 7, the final stage (cT2b, c; T3), extension and distant metastases LN} relative to their peers.
Description: A polyclonal antibody raised in Goat that recognizes and binds to Human uPAR . This antibody is tested and proven to work in the following applications:
Description: PLAUR (Plasminogen activator receptor, urokinase-type), also known as uPAR or CD87, is multidomain glycoprotein tethered to the cell membrane with a glycosylphosphotidylinositol(GPI) anchor. It consists of three different domains of the Ly-6/uPAR/alpha-neurotoxin family. The protein was originally identified as a saturable binding site for urokinase on the cell surface. The gene plays an important role in many normal as well as pathologic processes. It is localized to 19q13.31. uPAR is a part of the plasminogen activation system, which in the healthy body is involved in tissue reorganization events such as mammary gland involution and wound healing. It binds urokinase and thus restricts plasminogen activation to the immediate vicinity of the cell membrane, indicating it is an important player in the regulation of this process. In human coronary artery vascular smooth muscle cells, UPA stimulates cell migration via a uPAR signaling complex containing TYK2 and phosphatidylinositol 3-kinase.
Description: PLAUR (Plasminogen Activator Receptor, Urokinase-Type), also known as UPAR (uPA Receptor) or CD87, is multidomain glycoprotein tethered to the cell membrane with a glycosylphosphotidylinositol (GPI) anchor. PLAUR consists of three different domains of the Ly-6/uPAR/alpha-neurotoxin family. PLAUR is originally identified as a saturable binding site for urokinase on the cell surface. And the gene plays an important role in many normal as well as pathologic processes. The PLAUR gene is localized to 19q13.31. PLAUR is a part of the plasminogen activation system, which in the healthy body is involved in tissue reorganization events such as mammary gland involution and wound healing. PLAUR binds urokinase and thus restricts plasminogen activation to the immediate vicinity of the cell membrane. Thus it seems to be an important player in the regulation of this process. In human coronary artery vascular smooth muscle cells, UPA stimulates cell migration via a UPAR signaling complex containing TYK2 and phosphatidylinositol 3-kinase.
Description: PLAUR (PLASMINOGEN ACTIVATOR RECEPTOR, UROKINASE-TYPE), also known as UPAR or CD87, is multidomain glycoprotein tethered to the cell membrane with a glycosylphosphotidylinositol (GPI) anchor. PLAUR consists of three different domains of the Ly-6/uPAR/alpha-neurotoxin family. PLAUR is originally identified as a saturable binding site for urokinase on the cell surface. And the gene plays an important role in many normal as well as pathologic processes. The PLAUR gene is localized to 19q13.31. PLAUR is a part of the plasminogen activation system, which in the healthy body is involved in tissue reorganization events such as mammary gland involution and wound healing. PLAUR binds urokinase and thus restricts plasminogen activation to the immediate vicinity of the cell membrane. Thus it seems to be an important player in the regulation of this process. In human coronary artery vascular smooth muscle cells, UPA stimulates cell migration via a UPAR signaling complex containing TYK2 and phosphatidylinositol 3-kinase.
Description: PLAUR (Plasminogen activator receptor, urokinase-type), also known as UPAR or CD87, is multidomain glycoprotein tethered to the cell membrane with a glycosylphosphotidylinositol (GPI) anchor. PLAUR consists of three different domains of the Ly-6/uPAR/alpha-neurotoxin family. PLAUR is originally identified as a saturable binding site for urokinase on the cell surface. And the gene plays an important role in many normal as well as pathologic processes. The PLAUR gene is localized to 19q13.31. PLAUR is a part of the plasminogen activation system, which in the healthy body is involved in tissue reorganization events such as mammary gland involution and wound healing. PLAUR binds urokinase and thus restricts plasminogen activation to the immediate vicinity of the cell membrane. Thus it seems to be an important player in the regulation of this process. In human coronary artery vascular smooth muscle cells, UPA stimulates cell migration via a UPAR signaling complex containing TYK2 and phosphatidylinositol 3-kinase.
Description: PLAUR (PLASMINOGEN ACTIVATOR RECEPTOR, UROKINASE-TYPE), also known as UPAR or CD87, is multidomain glycoprotein tethered to the cell membrane with a glycosylphosphotidylinositol (GPI) anchor. PLAUR consists of three different domains of the Ly-6/uPAR/alpha-neurotoxin family. PLAUR is originally identified as a saturable binding site for urokinase on the cell surface. And the gene plays an important role in many normal as well as pathologic processes. The PLAUR gene is localized to 19q13.31. PLAUR is a part of the plasminogen activation system, which in the healthy body is involved in tissue reorganization events such as mammary gland involution and wound healing. PLAUR binds urokinase and thus restricts plasminogen activation to the immediate vicinity of the cell membrane. Thus it seems to be an important player in the regulation of this process. In human coronary artery vascular smooth muscle cells, UPA stimulates cell migration via a UPAR signaling complex containing TYK2 and phosphatidylinositol 3-kinase.
Description: The urokinase-type plasminogen activator (uPA) is one of two activators that converts plasminogen to plasmin. uPA binds with high-affinity to the cell surface via the GPI-linked receptor uPAR, which serves to localize uPA proteolytic activity. Human uPAR cDNA encodes a 335 amino acid (aa) precursor protein with a 22 aa signal peptide, five potential N-linked glycosylation sites and a C-terminal GPI-anchor site.
Description: The urokinase-type plasminogen activator (uPA) is one of two activators that converts plasminogen to plasmin. uPA binds with high-affinity to the cell surface via the GPI-linked receptor uPAR, which serves to localize uPA proteolytic activity. Human uPAR cDNA encodes a 335 amino acid (aa) precursor protein with a 22 aa signal peptide, five potential N-linked glycosylation sites and a C-terminal GPI-anchor site.
Description: Human uPAR Recombinant Protein expressed in Baculovirus with His-tag. Sequence domain: 23-305aa. Application(s): SDS-PAGE. Endotoxin: < 1 EU per 1ug of protein (determined by LAL method).
Description: Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. It is subject to negative-feedback regulation by U-PA which cleaves it into an inactive form.|Contains 3 UPAR/Ly6 domains.|subunit:Monomer (Probable). Interacts with MRC2.|
Description: Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. It is subject to negative-feedback regulation by U-PA which cleaves it into an inactive form.|Contains 3 UPAR/Ly6 domains.|subunit:Monomer (Probable). Interacts with MRC2.|
Description: Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. It is subject to negative-feedback regulation by U-PA which cleaves it into an inactive form.|Contains 3 UPAR/Ly6 domains.|subunit:Monomer (Probable). Interacts with MRC2.|
Description: Description of target: The urokinase-type plasminogen activator receptor (uPAR) is a key molecule in the regulation of cell-surface plasminogen activation and, as such, plays an important role in many normal as well as pathological processes.1 The cDNA for Mo3, an activation antigen expressed by human monocytes and myelomonocytic cell lines after stimulation by a variety of agents. Mo3 expression in vivo is associated predominantly with macrophages in inflammatory sites. It is a highly glycosylated protein of about 50 kD in monocytes where it is anchored to the plasma membrane by glycosyl-phosphatidylinositol linkage. The complete coding sequence of the cDNA has been found to encode 335 amino acids including a predicted signal peptide of 22 residues and a hydrophobic C-terminal portion. Mo3 is identical to the human receptor for the urokinase plasminogen activator.2 UPAR is a useful prognostic marker for biologically aggressive forms of endometrial cancer.3 PLAUR is located at chromosome 19q13.1-q13.2.1;Species reactivity: Mouse;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: <= 5 pg/mL
Description: Description of target: The urokinase-type plasminogen activator receptor (uPAR) is a key molecule in the regulation of cell-surface plasminogen activation and, as such, plays an important role in many normal as well as pathological processes.1 The cDNA for Mo3, an activation antigen expressed by human monocytes and myelomonocytic cell lines after stimulation by a variety of agents. Mo3 expression in vivo is associated predominantly with macrophages in inflammatory sites. It is a highly glycosylated protein of about 50 kD in monocytes where it is anchored to the plasma membrane by glycosyl-phosphatidylinositol linkage. The complete coding sequence of the cDNA has been found to encode 335 amino acids including a predicted signal peptide of 22 residues and a hydrophobic C-terminal portion. Mo3 is identical to the human receptor for the urokinase plasminogen activator.2 UPAR is a useful prognostic marker for biologically aggressive forms of endometrial cancer.3 PLAUR is located at chromosome 19q13.1-q13.2.1 The standard product used in this kit is recombinant human uPAR, consisting of 287 amino acids with the molecular mass of 31KDa.;Species reactivity: Human;Application: ELISA;Assay info: ;Sensitivity: < 4 pg/mL
Description: Tumors are the result of uncontrolled proliferation of cells in different organs. Tumor development is a multistage process, that includes the generation of primary tumors, separation of tumors from primary sites, degradation of extracellular matrix (ECM), and distant metastasis of tumors. A variety of genes play important roles in the development of tumors, including the cell surface receptor urokinase-type plasminogen activator receptor (uPAR). uPAR is highly expressed in a variety of tumor cells, and a variety of signals regulated by uPAR play significant roles in tumor cell proliferation and metastasis, tumor-related glycolysis, the tumor microenvironment and angiogenesis. Studies have found that some specific drugs and antibodies have unique inhibitory effects on uPAR.
In addition, the IRC and the uPA and independent predictor of distant metastasis and Gleason score ≥ 7, while PHI is a predictor of LN invasion (β = 0.25, p = 0.004) and uPA .PHI be of potential value in distinguishing between PCa, BPH and healthy men in addition, both are promising as independent predictors of adverse pathological features.
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