1389 Results for: "Rulleflasker&amp"

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localised to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR?target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR?target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

ACSF1 is a 672 amino acid protein belonging to the ATP-dependent AMP-binding enzyme family. Encoded by a gene that maps to human chromosome 12q24.31, ACSF1 is highly expressed in kidney, heart and brain, and shows similar neural expression as HMGCR (3-hydroxy-3-methylglutaryl-CoA reductase). Existing as three alternatively spliced isoforms, ACSF1 participates in ATP binding, ligase activity, acetoacetate-CoA ligase activity and nucleotide binding. The ACSF1 promoter is a known PPAR?target gene, with the nuclear receptor recruited to the ACSF1 promoter by direct interaction with stimulating protein-1 (Sp1). ACSF1 activates acetoacetate and is highly regulated by modulators that affect HMGCR and cholesterol biosynthesis.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits 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 and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

G protein-coupled receptors (GPCRs), also designated seven transmembrane (7TM) receptors and heptahelical receptors, are a protein family which interact with G proteins (heterotrimeric GTPases) to synthesize 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. G protein receptor 128 (GPR128), a member of the secretin family of GCPRs with a GPS domain in its N-terminal domain, may mediate signaling processes to the interior of the cell via activation of G proteins. GPR128 represents an allopeptide which may be involved in T cell mediated transplant rejection as it is able to stimulate 2.102 T cells.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits 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 and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits 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 and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits 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 and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

Uridine diphosphatase (UDPase) that promotes protein N-glycosylation and ATP level regulation. UDP hydrolysis promotes protein N-glycosylation and folding in the endoplasmic reticulum, as well as elevated ATP consumption in the cytosol via an ATP hydrolysis cycle. Together with CMPK1 and AK1, constitutes an ATP hydrolysis cycle that converts ATP to AMP and results in a compensatory increase in aerobic glycolysis. The nucleotide hydrolyzing preference is GDP > IDP > UDP, but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. Plays a key role in the AKT1-PTEN signaling pathway by promoting glycolysis in proliferating cells in response to phosphoinositide 3-kinase (PI3K) signaling.

Supplier: Bioss

Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.

Supplier: Bioss

Uridine diphosphatase (UDPase) that promotes protein N-glycosylation and ATP level regulation. UDP hydrolysis promotes protein N-glycosylation and folding in the endoplasmic reticulum, as well as elevated ATP consumption in the cytosol via an ATP hydrolysis cycle. Together with CMPK1 and AK1, constitutes an ATP hydrolysis cycle that converts ATP to AMP and results in a compensatory increase in aerobic glycolysis. The nucleotide hydrolyzing preference is GDP >IDP >UDP, but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. Plays a key role in the AKT1-PTEN signaling pathway by promoting glycolysis in proliferating cells in response to phosphoinositide 3-kinase (PI3K) signaling.

Supplier: Bioss

Cyclin M3 is a 707 amino acid multi-pass membrane protein that shares weak sequence similarity with cyclin proteins, yet displays no cyclin-like function in vivo. Though ubiquitously expressed, Cyclin M3 is found at highest levels in kidney, brain, spleen and heart. Cyclin M3 is localized to the nucleus where it is likely a metal transporter. Cyclin M3 contains two CBS domains, which appear to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet and may play a regulatory role in sensitizing proteins to adenosyl-carrying ligands. There are three isoforms of Cyclin M3 that are produced as a result of alternative splicing events.

Supplier: Bioss

G protein-coupled receptors (GPCRs), also designated seven transmembrane (7TM) receptors and heptahelical receptors, are a protein family which interact with G proteins (heterotrimeric GTPases) to synthesize 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. G protein receptor 84 (GPR84), a member of the GCPR 1 family, is an orphan GCPR expressed in bone marrow, brain, heart, muscle, colon, thymus, spleen, kidney, liver, placenta, intestine, lung and peripheral blood leukocytes. In activated T cells, GPR84 regulates early interleukin-4 (IL-4) gene expression.

Supplier: Bioss

G protein-coupled receptors (GPCRs), also designated seven transmembrane (7TM) receptors and heptahelical receptors, are a protein family which interact with G proteins (heterotrimeric GTPases) to synthesize 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. G protein receptor 128 (GPR128), a member of the secretin family of GCPRs with a GPS domain in its N-terminal domain, may mediate signaling processes to the interior of the cell via activation of G proteins. GPR128 represents an allopeptide which may be involved in T cell mediated transplant rejection as it is able to stimulate 2.102 T cells.

Supplier: Bioss

Cyclic AMP-dependent phosphodiesterase type D (PDE4D) family is comprise of 5 variants (PDE4D1, D2, D3, D4 and D5). One or more PDE4D subtype variants are ubiquitously present in all mammalian cells. In CNS all five PDE4D subtype variants are expressed in varying ratios and their activity is regulated in tandem with GPCRs stimulation. Peripheral tissues also exhibit differential expression of PDE4D variants. PDE4D1/D2 mRNA levels rise in response to an increase in cAMP. Short term regulation of PDE4D variants involved PKA, MAP kinases and Erk2 phosphorylation that results in rapid change in their enzymatic activities. Other regulatory mechanism involved protein protein interactions with cytoskeletal scaffolding proteins.

Supplier: Bioss

Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).

Supplier: Bioss

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

May be involved in neurite outgrowth.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/action, regulation of cell contraction/migration and cell growth/differentiation. GPCRs interact with G proteins (heterotrimeric GTPases) to synthesize 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. GRIN3 (G protein-regulated inducer of neurite outgrowth 3), also known as GPRIN3, is a 776 amino acid protein that contains a C-terminal region which shares a high homology with GRIN2 and GRIN1, and may function in neurite outgrowth.

Supplier: Bioss

May be involved in neurite outgrowth.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/action, regulation of cell contraction/migration and cell growth/differentiation. GPCRs interact with G proteins (heterotrimeric GTPases) to synthesize 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. GRIN3 (G protein-regulated inducer of neurite outgrowth 3), also known as GPRIN3, is a 776 amino acid protein that contains a C-terminal region which shares a high homology with GRIN2 and GRIN1, and may function in neurite outgrowth.

Supplier: Bioss

Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).

Supplier: Bioss

The protein encoded by this gene is a regulatory 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. This subunit may be a positive regulator of AMPK activity. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex. [provided by RefSeq, Jul 2008].

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits 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 and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).

Supplier: Bioss

Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).

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

May be involved in neurite outgrowth.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/action, regulation of cell contraction/migration and cell growth/differentiation. GPCRs interact with G proteins (heterotrimeric GTPases) to synthesize 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. GRIN3 (G protein-regulated inducer of neurite outgrowth 3), also known as GPRIN3, is a 776 amino acid protein that contains a C-terminal region which shares a high homology with GRIN2 and GRIN1, and may function in neurite outgrowth.