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Catalog Number: (BOSSBS-9507R-CY5.5)
Supplier: Bioss
Description: Cellular receptors for blood proteases regulate chemotaxis, extracellular proteolysis, and growth behavior of normal and malignant cells. Effector cell protease receptor-1 (EPR1) is a receptor for the coagulation protease factor Xa. EPR1 is characterized by a cysteine-rich extracellular module, a single membrane-spanning domain, and a serine-rich cytoplasmic tail featuring at least 15 potential phosphorylation sites. EPR1 also contains 2 N-linked glycosylation sites, 4 O-linked glycosylation sites, and a chondroitin sulfate attachment site, which may provide anchoring for carbohydrate chains, EPR1 transfectants bind to factor Xa in a specific and saturable manner, and in the absence of factor V/Va promote prothrombin activation in a factor Xa concentration-dependent reaction. Activated platelets and megakaryocytes express EPR1. Both EPR1 and membrane-bound factor Va are thought to be required to mediate factor Xa binding to the activated platelet to form a functional prothrombinase complex.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-7063R-A350)
Supplier: Bioss
Description: Apoptotic signals are often triggered by cell surface death receptors through protein-protein interactions mediated by conserved domains such as the death effector domain. A novel death effector domain (DED)-containing protein, DEDD2, has been recently identified. Over-expression of DEDD2 in transfected cells induces moderate apoptosis and results in substantial sensitization to apoptosis induced by Fas, TRAIL, and FADD. More recently, it has been shown that DEDD2 can bind caspase-8 and -10 in addition to FLIP but not FADD. Like the related protein DEDD, DEDD2 translocates from the cytosol to the nucleus upon induction of apoptosis, and it has been suggested that DEDD2 may target caspase-8 to the nucleus and that DEDD2 thus plays a critical role in death receptor-induced apoptosis. At least two alternatively spliced transcript variants encoding distinct isoforms have been found for DEDD2.
UOM: 1 * 100 µl


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Catalog Number: (BOSSBS-9507R-A750)
Supplier: Bioss
Description: Cellular receptors for blood proteases regulate chemotaxis, extracellular proteolysis, and growth behavior of normal and malignant cells. Effector cell protease receptor-1 (EPR1) is a receptor for the coagulation protease factor Xa. EPR1 is characterised by a cysteine-rich extracellular module, a single membrane-spanning domain, and a serine-rich cytoplasmic tail featuring at least 15 potential phosphorylation sites. EPR1 also contains 2 N-linked glycosylation sites, 4 O-linked glycosylation sites, and a chondroitin sulfate attachment site, which may provide anchoring for carbohydrate chains, EPR1 transfectants bind to factor Xa in a specific and saturable manner, and in the absence of factor V/Va promote prothrombin activation in a factor Xa concentration-dependent reaction. Activated platelets and megakaryocytes express EPR1. Both EPR1 and membrane-bound factor Va are thought to be required to mediate factor Xa binding to the activated platelet to form a functional prothrombinase complex.
UOM: 1 * 100 µl


Supplier: Corning
Description: PS coated with porcine gelatin. Corning® BioCoat™ gelatin provides an attachment and growth promoting substrate for the culture of a variety of cell types. Gelatin is commonly used in the culture of normal and transfected cell types, including vascular endothelial, muscle, embryonic stem (ES) and F9 teratocarcinoma cells.

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Catalog Number: (BOSSBS-7063R-CY5.5)
Supplier: Bioss
Description: Apoptotic signals are often triggered by cell surface death receptors through protein-protein interactions mediated by conserved domains such as the death effector domain. A novel death effector domain (DED)-containing protein, DEDD2, has been recently identified. Over-expression of DEDD2 in transfected cells induces moderate apoptosis and results in substantial sensitization to apoptosis induced by Fas, TRAIL, and FADD. More recently, it has been shown that DEDD2 can bind caspase-8 and -10 in addition to FLIP but not FADD. Like the related protein DEDD, DEDD2 translocates from the cytosol to the nucleus upon induction of apoptosis, and it has been suggested that DEDD2 may target caspase-8 to the nucleus and that DEDD2 thus plays a critical role in death receptor-induced apoptosis. At least two alternatively spliced transcript variants encoding distinct isoforms have been found for DEDD2.
UOM: 1 * 100 µl


Supplier: Biotium
Description: Recognizes a protein of 33-55 kDa, identified as CD53 (Workshop VI; Code N-L033). It is expressed on monocytes and macrophages, dendritic cells, osteoblasts and osteoclasts, and on T and B cells from every stage of differentiation but is absent from platelets, red blood cells. CD53 appears to be the marker with widest reactivity as well as the marker with the strictest specificity to hematopoietic cells. CD53 is a type III membrane with both termini in the cytoplasm and two loops in the extracellular environment. This molecule, in common with other members of tetraspan family, is involved in cellular activation as part of a signal transduction complex involving other membrane glycoproteins. CD53 crosslinking induces calcium flux on human monocyte and B cells. Cross-linking of CD53 promotes activation of resting human B-lymphocytes. This MAb recognizes CD53 transfected cells and partially inhibits T-cell proliferation induced by CD3 antibody (clone: UCHT1).

Catalog Number: (BOSSBS-5814R-A488)
Supplier: Bioss
Description: Prominin 2 is a 112 kDa glycoporotein structurally related to Prominin 1 (CD133) although amino acid similarity is not more than 30%, but their genomic organization is strikingly similar. Like Prominin 1, the prominin 2 exhibit similar membrane topology with 5 trans-membrane domains and two large glycosylated extracellular domains. Similar to Prominin1 localization, the Prominin 2 is also associated with membrane protrusions of the epithelial cells from adult kidney, and all along the digestive track and other epithelial tissues.Prominin 2 expression is down-regulated in aggressive prostate cancer cell lines and transient transfection of PROML2 expression vectors has been shown to induce apoptosis in cultured prostate cancer cells, suggesting a tumor suppressive role for Prominin 2. Prominin 2 expression is likely to be involved in growth suppression in the prostate, and down-regulation of Prominin 2 may disrupt normal prostatic homeostasis and lead to uncontrolled prostatic growth.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-7063R-CY7)
Supplier: Bioss
Description: Apoptotic signals are often triggered by cell surface death receptors through protein-protein interactions mediated by conserved domains such as the death effector domain. A novel death effector domain (DED)-containing protein, DEDD2, has been recently identified. Over-expression of DEDD2 in transfected cells induces moderate apoptosis and results in substantial sensitization to apoptosis induced by Fas, TRAIL, and FADD. More recently, it has been shown that DEDD2 can bind caspase-8 and -10 in addition to FLIP but not FADD. Like the related protein DEDD, DEDD2 translocates from the cytosol to the nucleus upon induction of apoptosis, and it has been suggested that DEDD2 may target caspase-8 to the nucleus and that DEDD2 thus plays a critical role in death receptor-induced apoptosis. At least two alternatively spliced transcript variants encoding distinct isoforms have been found for DEDD2.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-5814R-CY5)
Supplier: Bioss
Description: Prominin 2 is a 112 kDa glycoporotein structurally related to Prominin 1 (CD133) although amino acid similarity is not more than 30%, but their genomic organization is strikingly similar. Like Prominin 1, the prominin 2 exhibit similar membrane topology with 5 trans-membrane domains and two large glycosylated extracellular domains. Similar to Prominin1 localization, the Prominin 2 is also associated with membrane protrusions of the epithelial cells from adult kidney, and all along the digestive track and other epithelial tissues.Prominin 2 expression is down-regulated in aggressive prostate cancer cell lines and transient transfection of PROML2 expression vectors has been shown to induce apoptosis in cultured prostate cancer cells, suggesting a tumor suppressive role for Prominin 2. Prominin 2 expression is likely to be involved in growth suppression in the prostate, and down-regulation of Prominin 2 may disrupt normal prostatic homeostasis and lead to uncontrolled prostatic growth.
UOM: 1 * 100 µl


Supplier: Biotium
Description: Recognizes a protein of 33-55 kDa, identified as CD53 (Workshop VI; Code N-L033). It is expressed on monocytes and macrophages, dendritic cells, osteoblasts and osteoclasts, and on T and B cells from every stage of differentiation but is absent from platelets, red blood cells. CD53 appears to be the marker with widest reactivity as well as the marker with the strictest specificity to hematopoietic cells. CD53 is a type III membrane with both termini in the cytoplasm and two loops in the extracellular environment. This molecule, in common with other members of tetraspan family, is involved in cellular activation as part of a signal transduction complex involving other membrane glycoproteins. CD53 crosslinking induces calcium flux on human monocyte and B cells. Cross-linking of CD53 promotes activation of resting human B-lymphocytes. This MAb recognizes CD53 transfected cells and partially inhibits T-cell proliferation induced by CD3 antibody (clone: UCHT1).

Catalog Number: (BOSSBS-9507R-FITC)
Supplier: Bioss
Description: Cellular receptors for blood proteases regulate chemotaxis, extracellular proteolysis, and growth behavior of normal and malignant cells. Effector cell protease receptor-1 (EPR1) is a receptor for the coagulation protease factor Xa. EPR1 is characterized by a cysteine-rich extracellular module, a single membrane-spanning domain, and a serine-rich cytoplasmic tail featuring at least 15 potential phosphorylation sites. EPR1 also contains 2 N-linked glycosylation sites, 4 O-linked glycosylation sites, and a chondroitin sulfate attachment site, which may provide anchoring for carbohydrate chains, EPR1 transfectants bind to factor Xa in a specific and saturable manner, and in the absence of factor V/Va promote prothrombin activation in a factor Xa concentration-dependent reaction. Activated platelets and megakaryocytes express EPR1. Both EPR1 and membrane-bound factor Va are thought to be required to mediate factor Xa binding to the activated platelet to form a functional prothrombinase complex.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-7063R-HRP)
Supplier: Bioss
Description: Apoptotic signals are often triggered by cell surface death receptors through protein-protein interactions mediated by conserved domains such as the death effector domain. A novel death effector domain (DED)-containing protein, DEDD2, has been recently identified. Over-expression of DEDD2 in transfected cells induces moderate apoptosis and results in substantial sensitization to apoptosis induced by Fas, TRAIL, and FADD. More recently, it has been shown that DEDD2 can bind caspase-8 and -10 in addition to FLIP but not FADD. Like the related protein DEDD, DEDD2 translocates from the cytosol to the nucleus upon induction of apoptosis, and it has been suggested that DEDD2 may target caspase-8 to the nucleus and that DEDD2 thus plays a critical role in death receptor-induced apoptosis. At least two alternatively spliced transcript variants encoding distinct isoforms have been found for DEDD2.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-7063R-A555)
Supplier: Bioss
Description: Apoptotic signals are often triggered by cell surface death receptors through protein-protein interactions mediated by conserved domains such as the death effector domain. A novel death effector domain (DED)-containing protein, DEDD2, has been recently identified. Over-expression of DEDD2 in transfected cells induces moderate apoptosis and results in substantial sensitization to apoptosis induced by Fas, TRAIL, and FADD. More recently, it has been shown that DEDD2 can bind caspase-8 and -10 in addition to FLIP but not FADD. Like the related protein DEDD, DEDD2 translocates from the cytosol to the nucleus upon induction of apoptosis, and it has been suggested that DEDD2 may target caspase-8 to the nucleus and that DEDD2 thus plays a critical role in death receptor-induced apoptosis. At least two alternatively spliced transcript variants encoding distinct isoforms have been found for DEDD2.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9507R-HRP)
Supplier: Bioss
Description: Cellular receptors for blood proteases regulate chemotaxis, extracellular proteolysis, and growth behavior of normal and malignant cells. Effector cell protease receptor-1 (EPR1) is a receptor for the coagulation protease factor Xa. EPR1 is characterized by a cysteine-rich extracellular module, a single membrane-spanning domain, and a serine-rich cytoplasmic tail featuring at least 15 potential phosphorylation sites. EPR1 also contains 2 N-linked glycosylation sites, 4 O-linked glycosylation sites, and a chondroitin sulfate attachment site, which may provide anchoring for carbohydrate chains, EPR1 transfectants bind to factor Xa in a specific and saturable manner, and in the absence of factor V/Va promote prothrombin activation in a factor Xa concentration-dependent reaction. Activated platelets and megakaryocytes express EPR1. Both EPR1 and membrane-bound factor Va are thought to be required to mediate factor Xa binding to the activated platelet to form a functional prothrombinase complex.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9507R-A647)
Supplier: Bioss
Description: Cellular receptors for blood proteases regulate chemotaxis, extracellular proteolysis, and growth behavior of normal and malignant cells. Effector cell protease receptor-1 (EPR1) is a receptor for the coagulation protease factor Xa. EPR1 is characterized by a cysteine-rich extracellular module, a single membrane-spanning domain, and a serine-rich cytoplasmic tail featuring at least 15 potential phosphorylation sites. EPR1 also contains 2 N-linked glycosylation sites, 4 O-linked glycosylation sites, and a chondroitin sulfate attachment site, which may provide anchoring for carbohydrate chains, EPR1 transfectants bind to factor Xa in a specific and saturable manner, and in the absence of factor V/Va promote prothrombin activation in a factor Xa concentration-dependent reaction. Activated platelets and megakaryocytes express EPR1. Both EPR1 and membrane-bound factor Va are thought to be required to mediate factor Xa binding to the activated platelet to form a functional prothrombinase complex.
UOM: 1 * 100 µl


Catalog Number: (BNUM0182-50)
Supplier: Biotium
Description: Reacts with human CD59, a 20 kDa glycosyl phosphatidyl-inositol (GPI)-anchored cell surface protein (Workshop VI; Code N-L036). CD59 regulates complement-mediated cell lysis, and it is involved in lymphocyte signal transduction. This protein is a potent inhibitor of the complement membrane attack complex, whereby it binds complement C8 and/or C9 during the assembly of this complex, thereby inhibiting the incorporation of multiple copies of C9 into the complex, which is necessary for osmolytic pore formation. CD59 is widely distributed on cells in all tissues. It inhibits formation of MAC, thus protecting cells from complement-mediated lysis. The expression of CD59 on erythrocytes is important for their survival. Genetic defects in GPI-anchor attachment, that cause a reduction or loss of CD59 and CD55 on erythrocytes produce the symptoms of the disease paroxysmal hemoglobinuria (PNH). This MAb recognizes CD59 transfected cells. It is useful for study on GPI-anchored proteins, PNH and CD59 functions.
UOM: 1 * 50 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at eurega_services@eu.vwr.com
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