20855 Results for: "Allura red AC&amp"

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

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

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

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

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

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

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) 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 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. 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

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

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

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

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

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

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.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

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

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

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

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

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 54 (GPR54), a member of the rhodopsin family of GCPRs, is the receptor for the Kiss1 gene product, metastin. Mutations in GPCR54 are associated with a lack of puberty onset and autosomal recessive idiopathic hypogonadotropic hypogonadism, a deficient or decreased function of the gonads. Proper function of GRP54 is essential for puberty. In the rat, GRP54 is expressed in the liver, intestine and most areas of the brain, while in the human it is expressed in the placenta, pituitary, pancreas and spinal cord.