220 Results for: "Acide 3-phénoxybenzoïque&amp"

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localised to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localised to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: Bioss

Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.

Supplier: ProSci Inc.

The protein encoded by this gene is a catalytic subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Biosensis

Adenylate cyclases are enzymes which interact with and are activated by the GTP bound alpha subunits of trimeric G-proteins. Activated adenylate cyclases are responsible for the production of the important "second messenger" signalling molecule cyclic-AMP, which is generated from ATP. The type III adenylate cyclase enzyme is localized in the membranes surrounding the cilia in neurons, and our antibody is an excellent marker of neuronal cilia in the brain and in cells in tissue culture. Adenylate cyclase type III is a large complex molecule of, in the human, 1145 amino acids with a deduced molecular weight of 129kDa. The protein may be variably glycosylated, so that on SDS-PAGE and western blots it runs as a diffuse band of about 160kDa in cortex and about 200kDa in olfactory epithelium. The molecule has a complex structure, with 12 transmembrane domains and two cyclase domains. Each cyclase domain is immediately C-terminal to 6 transmembrane segments, but only the second, C-terminal cyclase is believed to be catalytically active.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Bioss

PKA (or cAPK) is a cyclic AMP dependent protein kinase. When activated by the second messenger cAMP, PKA mediates diverse cellular mechanisms, including proliferation, ion transport, regulation of metabolism, plus gene transcription. PKA is comprised of two dimers of two subunits, R (regulatory) and C (catalytic). Two families of R subunit (RI and RII) and three C subunit isoforms (C alpha, C beta, and C gamma) have been identified each possessing distinct cAMP binding properties and resulting in different phosphorylation states. C subunit is activated through autophosphorylation and direct phosphorylation at Thr197 by PDK-1. Tissue specific expression of C gamma, indicates pressure on C gamma during evolution, acting to modulate it in a functionally specific way. Certain amino acid substitutions make C gamma a distinct member of the cAMP dependent subfamily of protein kinases, and suggest that C gamma may be distinct in its protein substrate specificity or its interaction with the different regulatory subunits.

Supplier: Bioss

Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response.

Supplier: Bioss

Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response.

Supplier: Bioss

Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response.