2796 Results for: "Benzo[b]thiophene-7-carboxylic+acid&pageNo=89"

Supplier: Bioss

KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterized by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.

Supplier: Bioss

KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterized by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.

Supplier: ProSci Inc.

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. It acts as a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: ProSci Inc.

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. It acts as a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: ProSci Inc.

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. It acts as a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: ProSci Inc.

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. antibody to NKX2.2 detects a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: ProSci Inc.

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. Antibody to NKX2.2 detects a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: ProSci Inc.

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. antibody to NKX2.2 detects a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: ProSci Inc.

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. Antibody to NKX2.2 detects a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: VWR Chemicals

A standard mixture, typically used for food testing, containing the following components: 100 ug/ml each of Abamectin [CAS:71751-41-2] ; Acetamiprid [CAS:135410-20-7] ; Ametryn [CAS:834-12-8] ; Amitraz [CAS:33089-61-1] ; Azoxystrobin [CAS:131860-33-8] ; Benalaxyl [CAS:71626-11-4] ; Benzoximate [CAS:29104-30-1] ; Boscalid [CAS:188425-85-6] ; Butafenacil [CAS:134605-64-4] ; Carbetamide [CAS:16118-49-3] ; Carfentrazone-ethyl [CAS:128639-02-1] ; Chlorantraniliprole [CAS:500008-45-7] ; Clofentezine [CAS:74115-24-5] ; Cymoxanil [CAS:57966-95-7] ; Cyprodinil [CAS:121552-61-2] ; Cyromazine [CAS:66215-27-8] ; Dimoxystrobin [CAS:149961-52-4] ; Dinotefuran [CAS:165252-70-0] ; Doramectin [CAS:117704-25-3] ; Eprinomectin [CAS:123997-26-2] ; Famoxadone [CAS:131807-57-3] ; Fenazaquin [CAS:120928-09-8] ; Fenhexamid [CAS:126833-17-8] ; Fenpyroximate [CAS:111812-58-9] ; Flonicamid [CAS:158062-67-0] ; Fluazinam [CAS:79622-59-6] ; Fludioxonil [CAS:131341-86-1] ; Fluoxastrobin [CAS:361377-29-9] ; Flutolanil [CAS:66332-96-5] ; Furalaxyl [CAS:57646-30-7] ; Halofenozide [CAS:112226-61-6] ; Imazalil [CAS:35554-44-0] ; Imidacloprid [CAS:138261-41-3] ; Ivermectine [CAS:70288-86-7] ; Kresoxim-methyl [CAS:143390-89-0] ; Mandipropamid [CAS:374726-62-2] ; Mepanipyrim [CAS:110235-47-7] ; Mepronil [CAS:55814-41-0] ; Metaflumizone [CAS:139968-49-3] ; Metalaxyl [CAS:57837-19-1] ; Methoxyfenozide [CAS:161050-58-4] ; Moxidectin [CAS:113507-06-5] ; Myclobutanil [CAS:88671-89-0] ; Nitenpyram [CAS:150824-47-8] ; Oxadixyl [CAS:77732-09-3] ; Picoxystrobin [CAS:117428-22-5] ; Piperonyl butoxide [CAS:51-03-6] ; Prochloraz [CAS:67747-09-5] ; Prometon [CAS:1610-18-0] ; Pymetrozine [CAS:123312-89-0] ; Pyracarbolid [CAS:24691-76-7] ; Pyrimethanil [CAS:53112-28-0] ; Pyriproxyfen [CAS:95737-68-1] ; Quinoxyfen [CAS:124495-18-7] ; Rotenone [CAS:83-79-4] ; Secbumeton [CAS:26259-45-0] ; Spiroxamine [CAS:118134-30-8] ; Tebufenozide [CAS:112410-23-8] ; Tebufenpyrad [CAS:119168-77-3] ; Terbumeton [CAS:33693-04-8] ; Triadimefon [CAS:43121-43-3] ; Trifloxystrobin [CAS:141517-21-7] ; Zoxamide [CAS:156052-68-5] in Acetonitrile

Supplier: ProSci Inc.

KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterized by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.

Supplier: ProSci Inc.

KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterized by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.

Supplier: Bioss

The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterised by a canonical death domain fold, which consists of a bundle of five or six antiparallel -helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localised to the cytoplasm, ASC2 interacts with ASC to modulate NF-B and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier: VWR Chemicals

A standard mixture, typically used for food testing, containing the following components: 100 ug/ml each of Acrinathrin [CAS:101007-06-1] ; Anthraquinone [CAS:84-65-1] ; cis-Bifenthrin [CAS:82657-04-3] ; Bioallethrin [CAS:584-79-2] ; Cyfluthrin [CAS:68359-37-5] ; lambda-Cyhalothrin [CAS:91465-08-6] ; Cypermethrin [CAS:52315-07-8] ; Deltamethrin [CAS:52918-63-5] ; Fenvalerate [CAS:51630-58-1] ; Flucythrinate [CAS:70124-77-5] ; tau-Fluvalinate [CAS:102851-06-9] ; cis-Permethrine [CAS:61949-76-6] ; trans-Permethrine [CAS:61949-77-7] ; Phenothrin [CAS:26002-80-2] ; Resmethrin [CAS:10453-86-8] ; Tefluthrin [CAS:79538-32-2] ; Tetramethrin [CAS:7696-12-0] ; Transfluthrin [CAS:118712-89-3] in Toluene

Supplier: Bioss

The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier: Bioss

The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier: Bioss

The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier: Bioss

The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier: Bioss

The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier: Bioss

The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier: Bioss

The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterised by a canonical death domain fold, which consists of a bundle of five or six antiparallel -helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localised to the cytoplasm, ASC2 interacts with ASC to modulate NF-B and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier: Bioss

The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier: Bioss

The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier: Bioss

The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier: Bioss

The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier: Bioss

The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

Supplier: Bioss

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).

Supplier: Bioss

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).

Supplier: Bioss

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).

Supplier: Bioss

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).