1848 Results for: "Magnesio+citrato+nonaidrato&amp"

Supplier: Bioss

Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor.

Supplier: Bioss

Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor.

Supplier: Bioss

Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor.

Supplier: Bioss

Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor.

Supplier: ProSci Inc.

This gene is a member of the type IV, cyclic AMP (cAMP)-specific, cyclic nucleotide phosphodiesterase (PDE) family. Cyclic nucleotides are important second messengers that regulate and mediate a number of cellular responses to extracellular signals, such as hormones, light, and neurotransmitters. The cyclic nucleotide phosphodiesterases (PDEs) regulate the cellular concentrations of cyclic nucleotides and thereby play a role in signal transduction. This gene encodes a protein that specifically hydrolyzes cAMP. Altered activity of this protein has been associated with schizophrenia and bipolar affective disorder. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

Supplier: Bioss

G protein-coupled receptors (GPCRs) represent a large superfamily of cell-surface receptors that are involved in a multitude of physiological processes such as perception of sensory information, modulation of synaptic transmission, hormone release/actions, regulation of cell contraction/migration and cell growth/differentiation. GPCRs interact with G proteins (heterotrimeric GTPases) to synthesise intracellular second messengers, such as diacylglycerol, cyclic AMP, inositol phosphates and calcium ions. Their diverse biological functions range from vision and olfaction to neuronal and endocrine signaling and are involved in many pathological conditions. GRIN2 (G protein-regulated inducer of neurite outgrowth 2), also known as GPRIN2, is a 458 amino acid protein that is expressed in cerebellum and is thought to play a role in neurite outgrowth. GRIN2 interacts with activated G?oand G?, and is encoded by a gene that maps to human chromosome 10q11.22.

Supplier: Bioss

Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor.

Supplier: Bioss

Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor.

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. 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: ProSci Inc.

L-glutamate is the major excitatory neurotransmitter in the central nervous system and activates both ionotropic and metabotropic glutamate receptors. Glutamatergic neurotransmission is involved in most aspects of normal brain function and can be perturbed in many neuropathologic conditions. The metabotropic glutamate receptors are a family of G protein-coupled receptors, that have been divided into 3 groups on the basis of sequence homology, putative signal transduction mechanisms, and pharmacologic properties. Group I includes GRM1 and GRM5 and these receptors have been shown to activate phospholipase C. Group II includes GRM2 and GRM3 while Group III includes GRM4, GRM6, GRM7 and GRM8. Group II and III receptors are linked to the inhibition of the cyclic AMP cascade but differ in their agonist selectivities.L-glutamate is the major excitatory neurotransmitter in the central nervous system and activates both ionotropic and metabotropic glutamate receptors. Glutamatergic neurotransmission is involved in most aspects of normal brain function and can be perturbed in many neuropathologic conditions. The metabotropic glutamate receptors are a family of G protein-coupled receptors, that have been divided into 3 groups on the basis of sequence homology, putative signal transduction mechanisms, and pharmacologic properties. Group I includes GRM1 and GRM5 and these receptors have been shown to activate phospholipase C. Group II includes GRM2 and GRM3 while Group III includes GRM4, GRM6, GRM7 and GRM8. Group II and III receptors are linked to the inhibition of the cyclic AMP cascade but differ in their agonist selectivities.

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.

PIT1 is a pituitary-specific transcription factor responsible for pituitary development and hormone expression in mammals and is a member of the POU family of transcription factors that regulate mammalian development. The POU family is so named because the first 3 members identified were PIT1 and OCT1 of mammals, and Unc-86 of C. elegans. PIT1 contains 2 protein domains, termed POU-specific and POU-homeo, which are both necessary for high affinity DNA binding on genes encoding growth hormone and prolactin. PIT1 is also important for regulation of the genes encoding prolactin and thyroid-stimulating hormone beta subunit by thyrotropin-releasing hormone and cyclic AMP.

Supplier: ProSci Inc.

PIT1 is a pituitary-specific transcription factor responsible for pituitary development and hormone expression in mammals and is a member of the POU family of transcription factors that regulate mammalian development. The POU family is so named because the first 3 members identified were PIT1 and OCT1 of mammals, and Unc-86 of C. elegans. PIT1 contains 2 protein domains, termed POU-specific and POU-homeo, which are both necessary for high affinity DNA binding on genes encoding growth hormone and prolactin. PIT1 is also important for regulation of the genes encoding prolactin and thyroid-stimulating hormone beta subunit by thyrotropin-releasing hormone and cyclic AMP.

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: ProSci Inc.

HINT1 Antibody: Histidine triad nucleotide-binding protein 1 (HINT1) is a member of the histidine triad (HIT) protein family, a group of small nucleotide-binding and -hydrolyzing proteins. HINT1 interacts with several diverse proteins and has been suggested to have tumor suppressive activities. HINT1 catalyzes the hydrolysis of adenosine 5'-monophoramidate substrates such as AMP-morpholidate, but its enzymatic function does not appear to play a role in its tumor suppression. Recent experiments demonstrate that HINT1 forms a complex with POSH and JNK in vivo, inhibiting AP-1 activity and the phosphorylation of c-Jun, and this action could contribute to the tumor suppressor activity of HINT1. Other studies raise the possibility of HINT1 as a candidate gene for schizophrenia.

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

Cyclic AMP-regulated gene expression frequently involves a DNA element designated the cAMP-regulated enhancer (CRE). Many transcription factors bind to this element, including the protein CREB which is activated as a result of phosphorylation by protein kinase A. It has been shown that protein kinase A-mediated CREB phosphorylation results in its binding to a nuclear protein designated CBP (for CREB-binding protein). These findings suggest that CBP has many of the properties expected of a CREB co-activator. Another high molecular weight transcriptional adapter protein, designated p300, is characterized by three cysteine- and histidine-rich regions, of which the most carboxy terminal region specifically binds the adenovirus E1A protein. p300 molecules lacking an intact E1A binding site bypass E1A repression even in the presence of high concentrations of E1A. Sequence analysis of CBP and p300 has revealed substantial homology, arguing that these proteins are members of a conserved family of co-activators.