You Searched For: Molecular+sieve+3A+(0.3+nm,+3+Å)


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Supplier: Trajan Scientific and Medical
Description: Pure gas is a crictical requirement in gas chromatography, spectroscopy, optics, lithography and numerous other applications in manufacturing and laboratories. The SPure™ H₂O filters removes moisture, oil and dust from air and inert gases.

Catalog Number: (531-0217)
Supplier: LABCONCO
Description: Solvent trap insert, contains molecular sieve, protects the rotary vane pump, For: Labconco CentriVap®
UOM: 1 * 1 items


Supplier: Apollo Scientific
Description: BMS-309403 is an inhibitor of fatty acid binding protein 4 FABP4 with Ki of less than 2 nM that decreases fatty acid uptake in adipocytes in vitro.

Supplier: ENZO LIFE SCIENCES
Description: A potent and selective cell permeable calpain inhibitor. Inhibits oxidative damage-induced apoptosis in PC12 cells and capsaicin-induced apoptosis in dorsal root ganglion neurons. It protects against anoxia in rat optic nerves and reduces neuronal damage in an animal model of global cerebral ischemia(50 mg/kg). In isolated hippocampal pyramidal neurons, it inhibits Ca²⁺-induced suppression of neurite outgrowth (complete inhibition at 20 µM). Calpain I Ki = 8 nM; Cathepsin B Ki = 24 nM in isolated enzyme assays. IC50 = 0,3 µM in intact cell assay.

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Catalog Number: (SCOI285226010)
Supplier: SI Analytics
Description: Molecular sieve, 200 g in 250 ml glass bottle, TZ 1781
UOM: 1 * 1 items


Catalog Number: (BOSSBS-13280R-A680)
Supplier: Bioss
Description: The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating protein (GAP) can increase hydrolysis of p21Ras-bound GTP by as much as 1000-fold (4,5). The product of the neurofibromatosis type 1 gene (NF1) has also been shown to exhibit p21Ras GAP activity (6,7), and proteins that stimulate the GTPase activity of three other low molecular weight GTPases, including Rho, Rab 3A and Rap 1, have also been described (8,9).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13281R-A680)
Supplier: Bioss
Description: The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating protein (GAP) can increase hydrolysis of p21Ras-bound GTP by as much as 1000-fold (4,5). The product of the neurofibromatosis type 1 gene (NF1) has also been shown to exhibit p21Ras GAP activity (6,7), and proteins that stimulate the GTPase activity of three other low molecular weight GTPases, including Rho, Rab 3A and Rap 1, have also been described (8,9).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13281R-A647)
Supplier: Bioss
Description: The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating protein (GAP) can increase hydrolysis of p21Ras-bound GTP by as much as 1000-fold (4,5). The product of the neurofibromatosis type 1 gene (NF1) has also been shown to exhibit p21Ras GAP activity (6,7), and proteins that stimulate the GTPase activity of three other low molecular weight GTPases, including Rho, Rab 3A and Rap 1, have also been described (8,9).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13281R-A350)
Supplier: Bioss
Description: The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating protein (GAP) can increase hydrolysis of p21Ras-bound GTP by as much as 1000-fold (4,5). The product of the neurofibromatosis type 1 gene (NF1) has also been shown to exhibit p21Ras GAP activity (6,7), and proteins that stimulate the GTPase activity of three other low molecular weight GTPases, including Rho, Rab 3A and Rap 1, have also been described (8,9).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13280R-CY7)
Supplier: Bioss
Description: The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating protein (GAP) can increase hydrolysis of p21Ras-bound GTP by as much as 1000-fold (4,5). The product of the neurofibromatosis type 1 gene (NF1) has also been shown to exhibit p21Ras GAP activity (6,7), and proteins that stimulate the GTPase activity of three other low molecular weight GTPases, including Rho, Rab 3A and Rap 1, have also been described (8,9).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13280R-HRP)
Supplier: Bioss
Description: The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating protein (GAP) can increase hydrolysis of p21Ras-bound GTP by as much as 1000-fold (4,5). The product of the neurofibromatosis type 1 gene (NF1) has also been shown to exhibit p21Ras GAP activity (6,7), and proteins that stimulate the GTPase activity of three other low molecular weight GTPases, including Rho, Rab 3A and Rap 1, have also been described (8,9).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13281R-A555)
Supplier: Bioss
Description: The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating protein (GAP) can increase hydrolysis of p21Ras-bound GTP by as much as 1000-fold (4,5). The product of the neurofibromatosis type 1 gene (NF1) has also been shown to exhibit p21Ras GAP activity (6,7), and proteins that stimulate the GTPase activity of three other low molecular weight GTPases, including Rho, Rab 3A and Rap 1, have also been described (8,9).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13281R-CY7)
Supplier: Bioss
Description: The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating protein (GAP) can increase hydrolysis of p21Ras-bound GTP by as much as 1000-fold (4,5). The product of the neurofibromatosis type 1 gene (NF1) has also been shown to exhibit p21Ras GAP activity (6,7), and proteins that stimulate the GTPase activity of three other low molecular weight GTPases, including Rho, Rab 3A and Rap 1, have also been described (8,9).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13281R-CY5)
Supplier: Bioss
Description: The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating protein (GAP) can increase hydrolysis of p21Ras-bound GTP by as much as 1000-fold (4,5). The product of the neurofibromatosis type 1 gene (NF1) has also been shown to exhibit p21Ras GAP activity (6,7), and proteins that stimulate the GTPase activity of three other low molecular weight GTPases, including Rho, Rab 3A and Rap 1, have also been described (8,9).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13280R-FITC)
Supplier: Bioss
Description: The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating protein (GAP) can increase hydrolysis of p21Ras-bound GTP by as much as 1000-fold (4,5). The product of the neurofibromatosis type 1 gene (NF1) has also been shown to exhibit p21Ras GAP activity (6,7), and proteins that stimulate the GTPase activity of three other low molecular weight GTPases, including Rho, Rab 3A and Rap 1, have also been described (8,9).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13281R-A488)
Supplier: Bioss
Description: The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating protein (GAP) can increase hydrolysis of p21Ras-bound GTP by as much as 1000-fold (4,5). The product of the neurofibromatosis type 1 gene (NF1) has also been shown to exhibit p21Ras GAP activity (6,7), and proteins that stimulate the GTPase activity of three other low molecular weight GTPases, including Rho, Rab 3A and Rap 1, have also been described (8,9).
UOM: 1 * 100 µl


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