126020 Results for: "3-Bromopropionic acid&amp"

Supplier: Bioss

By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity and function.

Supplier: Bioss

Probably important in cardiac repolarization. Associates with KCNE1 (MinK) to form the I(Ks) cardiac potassium current. Elicits a rapidly activating, potassium-selective outward current. Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current in CHO cells in which cloned KCNQ1/KCNE1 channels were coexpressed with M1 muscarinic receptors. May associate also with KCNE3 (MiRP2) to form the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions, which is reduced in cystic fibrosis and pathologically stimulated in cholera and other forms of secretory diarrhea.

Supplier: Bioss

Probably important in cardiac repolarization. Associates with KCNE1 (MinK) to form the I(Ks) cardiac potassium current. Elicits a rapidly activating, potassium-selective outward current. Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current in CHO cells in which cloned KCNQ1/KCNE1 channels were coexpressed with M1 muscarinic receptors. May associate also with KCNE3 (MiRP2) to form the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions, which is reduced in cystic fibrosis and pathologically stimulated in cholera and other forms of secretory diarrhea.

Supplier: Bioss

GTP-binding proteins (G-proteins)are a family of heterotrimeric proteins that play a critical role in signal transduction by coupling cell surface, 7-transmembrane domain receptors to intracellular signaling pathways including second messenger generation (such as cyclic AMP, calcium and diacylglycerol), protein phosphorylation, ion channel activation, gene induction, cell growth and differentiation. Receptor activation catalyzes the exchange of GTP for GDP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit.

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

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

GTP-binding proteins (G-proteins)are a family of heterotrimeric proteins that play a critical role in signal transduction by coupling cell surface, 7-transmembrane domain receptors to intracellular signaling pathways including second messenger generation (such as cyclic AMP, calcium and diacylglycerol), protein phosphorylation, ion channel activation, gene induction, cell growth and differentiation. Receptor activation catalyzes the exchange of GTP for GDP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit.

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

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 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

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

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

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

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

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

GTP-binding proteins (G-proteins)are a family of heterotrimeric proteins that play a critical role in signal transduction by coupling cell surface, 7-transmembrane domain receptors to intracellular signaling pathways including second messenger generation (such as cyclic AMP, calcium and diacylglycerol), protein phosphorylation, ion channel activation, gene induction, cell growth and differentiation. Receptor activation catalyzes the exchange of GTP for GDP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit.

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

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

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

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

GTP-binding proteins (G-proteins)are a family of heterotrimeric proteins that play a critical role in signal transduction by coupling cell surface, 7-transmembrane domain receptors to intracellular signaling pathways including second messenger generation (such as cyclic AMP, calcium and diacylglycerol), protein phosphorylation, ion channel activation, gene induction, cell growth and differentiation. Receptor activation catalyzes the exchange of GTP for GDP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit.

Supplier: Bioss

GTP-binding proteins (G-proteins)are a family of heterotrimeric proteins that play a critical role in signal transduction by coupling cell surface, 7-transmembrane domain receptors to intracellular signaling pathways including second messenger generation (such as cyclic AMP, calcium and diacylglycerol), protein phosphorylation, ion channel activation, gene induction, cell growth and differentiation. Receptor activation catalyzes the exchange of GTP for GDP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit.

Supplier: Bioss

GTP-binding proteins (G-proteins)are a family of heterotrimeric proteins that play a critical role in signal transduction by coupling cell surface, 7-transmembrane domain receptors to intracellular signaling pathways including second messenger generation (such as cyclic AMP, calcium and diacylglycerol), protein phosphorylation, ion channel activation, gene induction, cell growth and differentiation. Receptor activation catalyzes the exchange of GTP for GDP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit.

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

GTP-binding proteins (G-proteins)are a family of heterotrimeric proteins that play a critical role in signal transduction by coupling cell surface, 7-transmembrane domain receptors to intracellular signaling pathways including second messenger generation (such as cyclic AMP, calcium and diacylglycerol), protein phosphorylation, ion channel activation, gene induction, cell growth and differentiation. Receptor activation catalyzes the exchange of GTP for GDP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit.

Supplier: Bioss

GTP-binding proteins (G-proteins)are a family of heterotrimeric proteins that play a critical role in signal transduction by coupling cell surface, 7-transmembrane domain receptors to intracellular signaling pathways including second messenger generation (such as cyclic AMP, calcium and diacylglycerol), protein phosphorylation, ion channel activation, gene induction, cell growth and differentiation. Receptor activation catalyzes the exchange of GTP for GDP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit.

Supplier: Bioss

GTP-binding proteins (G-proteins)are a family of heterotrimeric proteins that play a critical role in signal transduction by coupling cell surface, 7-transmembrane domain receptors to intracellular signaling pathways including second messenger generation (such as cyclic AMP, calcium and diacylglycerol), protein phosphorylation, ion channel activation, gene induction, cell growth and differentiation. Receptor activation catalyzes the exchange of GTP for GDP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit.

Supplier: Bioss

GTP-binding proteins (G-proteins)are a family of heterotrimeric proteins that play a critical role in signal transduction by coupling cell surface, 7-transmembrane domain receptors to intracellular signaling pathways including second messenger generation (such as cyclic AMP, calcium and diacylglycerol), protein phosphorylation, ion channel activation, gene induction, cell growth and differentiation. Receptor activation catalyzes the exchange of GTP for GDP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit.

Supplier: Bioss

GTP-binding proteins (G-proteins)are a family of heterotrimeric proteins that play a critical role in signal transduction by coupling cell surface, 7-transmembrane domain receptors to intracellular signaling pathways including second messenger generation (such as cyclic AMP, calcium and diacylglycerol), protein phosphorylation, ion channel activation, gene induction, cell growth and differentiation. Receptor activation catalyzes the exchange of GTP for GDP bound to the inactive G protein alpha subunit resulting in a conformational change and dissociation of the complex. The G protein alpha and beta-gamma subunits are capable of regulating various cellular effectors. Activation is terminated by a GTPase intrinsic to the G-alpha subunit.