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Catalog Number: (BOSSBS-5814R-HRP)
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-5814R-A750)
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 organisation 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-9507R-CY7)
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-A350)
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-CY5)
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-5814R-FITC)
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-A647)
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-A680)
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 sensitisation 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-CY3)
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


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.

Catalog Number: (786-651)
Supplier: G-Biosciences
Description: β-Galactosidase assay is for determining the β-galactosidase activity in the lysates of cells transfected with a β-galactosidase expression construct. It uses chlorophenol red-β-D-galactopyranoside (CPRG), which is up to 10 times more sensitive than the classic O-nitrophenyl-β-D-galactopyranoside (ONPG) β-Galactosidase assays. This increased sensitivity makes it simpler to measure β-galactosidase activity in cells that are difficult to transfect or have low β-galactosidase activity expression. β-Galactosidase activity is measured using a spectrophotometer or a microplate reader to determine the amount of substrate converted at 570 to 595 nm.
UOM: 1 * 500 Assays


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


Catalog Number: (BOSSBS-5814R-A680)
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 organisation 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-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


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: (OZBISP00500)
Supplier: OZ BIOSCIENCES
Description: SEAP assay kit (Secreted Alkaline Phosphatase) is a colorimetric assay for sensitive quantification of SEAP in culture medium from transfected cells or tissues.
UOM: 1 * 1 KIT


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