Descrição: cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP dependent protein kinase (AMPK), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of AMPK is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits of AMPK have been identified in humans. PKA beta (catalytic subunit) is a member of the Ser/Thr protein kinase family and is a catalytic subunit of AMPK.

Código de Artigo: BOSSBS-2371R

UOM: 1 * 100 µl

Fornecedor: Bioss

Promoção

Descrição: The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.

Código de Artigo: BOSSBS-8682R-CY7

UOM: 1 * 100 µl

Fornecedor: Bioss

Promoção

Descrição: For direct quantification of cAMP from a variety of biological samples.

Código de Artigo: CAYM501040-480

UOM: 1 * 480 Tests

Fornecedor: Cayman Chemical

Promoção

Descrição: Anti-CAMP Rabbit Polyclonal Antibody (HRP (Horseradish Peroxidase))

Código de Artigo: USBI033171-HRP

UOM: 1 * 200 µl

Fornecedor: US Biological

Promoção

Descrição: The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.

Código de Artigo: BOSSBS-8682R-CY3

UOM: 1 * 100 µl

Fornecedor: Bioss

Promoção

Descrição: The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.

Código de Artigo: BOSSBS-8682R-HRP

UOM: 1 * 100 µl

Fornecedor: Bioss

Promoção

Descrição: Anti-cAMP Protein Kinase Catalytic subunit Rabbit Polyclonal Antibody

Código de Artigo: ABCAAB26322-100

UOM: 1 * 100 µl

Fornecedor: Abcam

Promoção

Descrição: CREM is a a bZIP transcription factor that binds to the cAMP responsive element found in many viral and cellular promoters. It is derived from a multiexonic gene that encodes both activators and antagonists of cAMP-inducible transcription by differential splicing. Splice variants with antagonistic function lack 2 glutamine-rich domains and block cAMP-induced transcription, whereas an isoform that includes these glutamine-rich domains is a transcriptional activator.

Código de Artigo: BOSSBS-5135R-CY3

UOM: 1 * 100 µl

Fornecedor: Bioss

Promoção

Descrição: CREM is a a bZIP transcription factor that binds to the cAMP responsive element found in many viral and cellular promoters. It is derived from a multiexonic gene that encodes both activators and antagonists of cAMP-inducible transcription by differential splicing. Splice variants with antagonistic function lack 2 glutamine-rich domains and block cAMP-induced transcription, whereas an isoform that includes these glutamine-rich domains is a transcriptional activator.

Código de Artigo: BOSSBS-5135R-CY7

UOM: 1 * 100 µl

Fornecedor: Bioss

Promoção

Descrição: CREM is a a bZIP transcription factor that binds to the cAMP responsive element found in many viral and cellular promoters. It is derived from a multiexonic gene that encodes both activators and antagonists of cAMP-inducible transcription by differential splicing. Splice variants with antagonistic function lack 2 glutamine-rich domains and block cAMP-induced transcription, whereas an isoform that includes these glutamine-rich domains is a transcriptional activator.

Código de Artigo: BOSSBS-5135R-CY5.5

UOM: 1 * 100 µl

Fornecedor: Bioss

Promoção

Descrição: CREM is a a bZIP transcription factor that binds to the cAMP responsive element found in many viral and cellular promoters. It is derived from a multiexonic gene that encodes both activators and antagonists of cAMP-inducible transcription by differential splicing. Splice variants with antagonistic function lack 2 glutamine-rich domains and block cAMP-induced transcription, whereas an isoform that includes these glutamine-rich domains is a transcriptional activator.

Código de Artigo: BOSSBS-5135R-FITC

UOM: 1 * 100 µl

Fornecedor: Bioss

Promoção

Descrição: PRKACA and PRKACB are members of the Ser/Thr protein kinase family and are a catalytic subunit of cAMP-dependent protein kinase. cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits.PKA alpha + beta (catalytic subunits) (phospho Thr198)

Código de Artigo: BOSSBS-3725R-A350

UOM: 1 * 100 µl

Fornecedor: Bioss

Promoção

Descrição: PRKACA and PRKACB are members of the Ser/Thr protein kinase family and are a catalytic subunit of cAMP-dependent protein kinase. cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits.PKA alpha + beta (catalytic subunits) (phospho Thr198).

Código de Artigo: BOSSBS-3725R-A750

UOM: 1 * 100 µl

Fornecedor: Bioss

Promoção

Descrição: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in the control of cAMP-mediated neural activity and cAMP metabolism in the brain.

Código de Artigo: BOSSBS-11576R-A350

UOM: 1 * 100 µl

Fornecedor: Bioss

Promoção

Descrição: The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.

Código de Artigo: BOSSBS-8682R-A555

UOM: 1 * 100 µl

Fornecedor: Bioss

Promoção

Descrição: The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilise the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilised antigen based chromatography.

Código de Artigo: BOSSBS-8682R-A680

UOM: 1 * 100 µl

Fornecedor: Bioss

Promoção