1146 Results for: "Nitric Acid"

Supplier: Bioss

Members of the class-III pyridoxal-phosphate-dependent aminotransferase family, such as AGXT2, catalyze the conversion of glyoxylate to glycine using L-alanine as the amino donor. AGXT2 protects from asymmetric dimethylarginine (ADMA)-induced inhibition in nitric oxide (NO) production. Elevated blood concentrations of ADMA, a methyl derivate of the amino acid arginine and an endogenous inhibitor of nitric oxide (NO) synthase, is produced by the physiological degradation of methylated proteins and is found in association with diabetes, hypertension, congestive heart failure and atherosclerosis. AGXT2L2 (alanine-glyoxylate aminotransferase 2-like 2) is a 450 amino acid pyridoxal phosphate that exists as a homotetramer. Belonging to the class-III pyridoxal-phosphate-dependent aminotransferase family, AGXT2L2 localises to the mitochondria and exists as three alternatively spliced isoforms. Encoded by a gene located on human chromosome 5q35.3, AGXT2L2 may have similar functions as AGXT2.

Supplier: Bioss

Members of the class-III pyridoxal-phosphate-dependent aminotransferase family, such as AGXT2, catalyze the conversion of glyoxylate to glycine using L-alanine as the amino donor. AGXT2 protects from asymmetric dimethylarginine (ADMA)-induced inhibition in nitric oxide (NO) production. Elevated blood concentrations of ADMA, a methyl derivate of the amino acid arginine and an endogenous inhibitor of nitric oxide (NO) synthase, is produced by the physiological degradation of methylated proteins and is found in association with diabetes, hypertension, congestive heart failure and atherosclerosis. AGXT2L2 (alanine-glyoxylate aminotransferase 2-like 2) is a 450 amino acid pyridoxal phosphate that exists as a homotetramer. Belonging to the class-III pyridoxal-phosphate-dependent aminotransferase family, AGXT2L2 localizes to the mitochondria and exists as three alternatively spliced isoforms. Encoded by a gene located on human chromosome 5q35.3, AGXT2L2 may have similar functions as AGXT2.

Supplier: Bioss

Members of the class-III pyridoxal-phosphate-dependent aminotransferase family, such as AGXT2, catalyze the conversion of glyoxylate to glycine using L-alanine as the amino donor. AGXT2 protects from asymmetric dimethylarginine (ADMA)-induced inhibition in nitric oxide (NO) production. Elevated blood concentrations of ADMA, a methyl derivate of the amino acid arginine and an endogenous inhibitor of nitric oxide (NO) synthase, is produced by the physiological degradation of methylated proteins and is found in association with diabetes, hypertension, congestive heart failure and atherosclerosis. AGXT2L2 (alanine-glyoxylate aminotransferase 2-like 2) is a 450 amino acid pyridoxal phosphate that exists as a homotetramer. Belonging to the class-III pyridoxal-phosphate-dependent aminotransferase family, AGXT2L2 localizes to the mitochondria and exists as three alternatively spliced isoforms. Encoded by a gene located on human chromosome 5q35.3, AGXT2L2 may have similar functions as AGXT2.

Supplier: Bioss

Members of the class-III pyridoxal-phosphate-dependent aminotransferase family, such as AGXT2, catalyze the conversion of glyoxylate to glycine using L-alanine as the amino donor. AGXT2 protects from asymmetric dimethylarginine (ADMA)-induced inhibition in nitric oxide (NO) production. Elevated blood concentrations of ADMA, a methyl derivate of the amino acid arginine and an endogenous inhibitor of nitric oxide (NO) synthase, is produced by the physiological degradation of methylated proteins and is found in association with diabetes, hypertension, congestive heart failure and atherosclerosis. AGXT2L2 (alanine-glyoxylate aminotransferase 2-like 2) is a 450 amino acid pyridoxal phosphate that exists as a homotetramer. Belonging to the class-III pyridoxal-phosphate-dependent aminotransferase family, AGXT2L2 localizes to the mitochondria and exists as three alternatively spliced isoforms. Encoded by a gene located on human chromosome 5q35.3, AGXT2L2 may have similar functions as AGXT2.

Supplier: Bioss

CAPON (carboxy-terminal PDZ ligand of nNOS) selectively binds within the 100 amino acid PDZ domain of the neuronal nitric oxide synthase (nNOS), but not to endothelial NOS or inducible NOS, and sequesters nNOS in the cytosol. Biosynthesis of the neurotransmitter nitric oxide (NO) requires the association of nNOS with various synaptic proteins, including syntrophin, postsynaptic density (PSD)95 and PSD93 through a scaffolding PDZ domain. These proteins facilitate the transport of nNOS to the plasma membrane, where it is catalytically activated by NMDA-receptor mediated calcium channels. The association of nNOS with PSD95 or PSD93 is regulated by CAPON. The carboxy terminus of CAPON binds to the PDZ domain, competes with PSD95 and PSD93 for binding to nNOS and in turn prevents the translocation and catalytic activation of nNOS.

Supplier: Bioss

CAPON (carboxy-terminal PDZ ligand of nNOS) selectively binds within the 100 amino acid PDZ domain of the neuronal nitric oxide synthase (nNOS), but not to endothelial NOS or inducible NOS, and sequesters nNOS in the cytosol. Biosynthesis of the neurotransmitter nitric oxide (NO) requires the association of nNOS with various synaptic proteins, including syntrophin, postsynaptic density (PSD)95 and PSD93 through a scaffolding PDZ domain. These proteins facilitate the transport of nNOS to the plasma membrane, where it is catalytically activated by NMDA-receptor mediated calcium channels. The association of nNOS with PSD95 or PSD93 is regulated by CAPON. The carboxy terminus of CAPON binds to the PDZ domain, competes with PSD95 and PSD93 for binding to nNOS and in turn prevents the translocation and catalytic activation of nNOS.

Supplier: Bioss

CAPON (carboxy-terminal PDZ ligand of nNOS) selectively binds within the 100 amino acid PDZ domain of the neuronal nitric oxide synthase (nNOS), but not to endothelial NOS or inducible NOS, and sequesters nNOS in the cytosol. Biosynthesis of the neurotransmitter nitric oxide (NO) requires the association of nNOS with various synaptic proteins, including syntrophin, postsynaptic density (PSD)95 and PSD93 through a scaffolding PDZ domain. These proteins facilitate the transport of nNOS to the plasma membrane, where it is catalytically activated by NMDA-receptor mediated calcium channels. The association of nNOS with PSD95 or PSD93 is regulated by CAPON. The carboxy terminus of CAPON binds to the PDZ domain, competes with PSD95 and PSD93 for binding to nNOS and in turn prevents the translocation and catalytic activation of nNOS.

Supplier: Bioss

CAPON (carboxy-terminal PDZ ligand of nNOS) selectively binds within the 100 amino acid PDZ domain of the neuronal nitric oxide synthase (nNOS), but not to endothelial NOS or inducible NOS, and sequesters nNOS in the cytosol. Biosynthesis of the neurotransmitter nitric oxide (NO) requires the association of nNOS with various synaptic proteins, including syntrophin, postsynaptic density (PSD)95 and PSD93 through a scaffolding PDZ domain. These proteins facilitate the transport of nNOS to the plasma membrane, where it is catalytically activated by NMDA-receptor mediated calcium channels. The association of nNOS with PSD95 or PSD93 is regulated by CAPON. The carboxy terminus of CAPON binds to the PDZ domain, competes with PSD95 and PSD93 for binding to nNOS and in turn prevents the translocation and catalytic activation of nNOS.

Supplier: Bioss

CAPON (carboxy-terminal PDZ ligand of nNOS) selectively binds within the 100 amino acid PDZ domain of the neuronal nitric oxide synthase (nNOS), but not to endothelial NOS or inducible NOS, and sequesters nNOS in the cytosol. Biosynthesis of the neurotransmitter nitric oxide (NO) requires the association of nNOS with various synaptic proteins, including syntrophin, postsynaptic density (PSD)95 and PSD93 through a scaffolding PDZ domain. These proteins facilitate the transport of nNOS to the plasma membrane, where it is catalytically activated by NMDA-receptor mediated calcium channels. The association of nNOS with PSD95 or PSD93 is regulated by CAPON. The carboxy terminus of CAPON binds to the PDZ domain, competes with PSD95 and PSD93 for binding to nNOS and in turn prevents the translocation and catalytic activation of nNOS.

Supplier: Bioss

CAPON (carboxy-terminal PDZ ligand of nNOS) selectively binds within the 100 amino acid PDZ domain of the neuronal nitric oxide synthase (nNOS), but not to endothelial NOS or inducible NOS, and sequesters nNOS in the cytosol. Biosynthesis of the neurotransmitter nitric oxide (NO) requires the association of nNOS with various synaptic proteins, including syntrophin, postsynaptic density (PSD)95 and PSD93 through a scaffolding PDZ domain. These proteins facilitate the transport of nNOS to the plasma membrane, where it is catalytically activated by NMDA-receptor mediated calcium channels. The association of nNOS with PSD95 or PSD93 is regulated by CAPON. The carboxy terminus of CAPON binds to the PDZ domain, competes with PSD95 and PSD93 for binding to nNOS and in turn prevents the translocation and catalytic activation of nNOS.

Supplier: Bioss

CAPON (carboxy-terminal PDZ ligand of nNOS) selectively binds within the 100 amino acid PDZ domain of the neuronal nitric oxide synthase (nNOS), but not to endothelial NOS or inducible NOS, and sequesters nNOS in the cytosol. Biosynthesis of the neurotransmitter nitric oxide (NO) requires the association of nNOS with various synaptic proteins, including syntrophin, postsynaptic density (PSD)95 and PSD93 through a scaffolding PDZ domain. These proteins facilitate the transport of nNOS to the plasma membrane, where it is catalytically activated by NMDA-receptor mediated calcium channels. The association of nNOS with PSD95 or PSD93 is regulated by CAPON. The carboxy terminus of CAPON binds to the PDZ domain, competes with PSD95 and PSD93 for binding to nNOS and in turn prevents the translocation and catalytic activation of nNOS.

Supplier: Bioss

CAPON (carboxy-terminal PDZ ligand of nNOS) selectively binds within the 100 amino acid PDZ domain of the neuronal nitric oxide synthase (nNOS), but not to endothelial NOS or inducible NOS, and sequesters nNOS in the cytosol. Biosynthesis of the neurotransmitter nitric oxide (NO) requires the association of nNOS with various synaptic proteins, including syntrophin, postsynaptic density (PSD)95 and PSD93 through a scaffolding PDZ domain. These proteins facilitate the transport of nNOS to the plasma membrane, where it is catalytically activated by NMDA-receptor mediated calcium channels. The association of nNOS with PSD95 or PSD93 is regulated by CAPON. The carboxy terminus of CAPON binds to the PDZ domain, competes with PSD95 and PSD93 for binding to nNOS and in turn prevents the translocation and catalytic activation of nNOS.

Supplier: MP Biomedicals

L-Ascorbic Acid is used as an Antimicrobial and Antioxidant in foodstuffs. Reductant for the isolation of chloroplasts. It has an effect on the nonspecific immune system. Preserves nitric oxide (NO) which may help prevent endothelial dysfunction. It also helps prevent and reverse the oxidative damage done to proteins and lipids as a result of cigarette smoke.

Supplier: Bioss

CAPON (carboxy-terminal PDZ ligand of nNOS) selectively binds within the 100 amino acid PDZ domain of the neuronal nitric oxide synthase (nNOS), but not to endothelial NOS or inducible NOS, and sequesters nNOS in the cytosol. Biosynthesis of the neurotransmitter nitric oxide (NO) requires the association of nNOS with various synaptic proteins, including syntrophin, postsynaptic density (PSD)95 and PSD93 through a scaffolding PDZ domain. These proteins facilitate the transport of nNOS to the plasma membrane, where it is catalytically activated by NMDA-receptor mediated calcium channels. The association of nNOS with PSD95 or PSD93 is regulated by CAPON. The carboxy terminus of CAPON binds to the PDZ domain, competes with PSD95 and PSD93 for binding to nNOS and in turn prevents the translocation and catalytic activation of nNOS.

Supplier: Bioss

CAPON (carboxy-terminal PDZ ligand of nNOS) selectively binds within the 100 amino acid PDZ domain of the neuronal nitric oxide synthase (nNOS), but not to endothelial NOS or inducible NOS, and sequesters nNOS in the cytosol. Biosynthesis of the neurotransmitter nitric oxide (NO) requires the association of nNOS with various synaptic proteins, including syntrophin, postsynaptic density (PSD)95 and PSD93 through a scaffolding PDZ domain. These proteins facilitate the transport of nNOS to the plasma membrane, where it is catalytically activated by NMDA-receptor mediated calcium channels. The association of nNOS with PSD95 or PSD93 is regulated by CAPON. The carboxy terminus of CAPON binds to the PDZ domain, competes with PSD95 and PSD93 for binding to nNOS and in turn prevents the translocation and catalytic activation of nNOS.

Supplier: Bioss

CAPON (carboxy-terminal PDZ ligand of nNOS) selectively binds within the 100 amino acid PDZ domain of the neuronal nitric oxide synthase (nNOS), but not to endothelial NOS or inducible NOS, and sequesters nNOS in the cytosol. Biosynthesis of the neurotransmitter nitric oxide (NO) requires the association of nNOS with various synaptic proteins, including syntrophin, postsynaptic density (PSD)95 and PSD93 through a scaffolding PDZ domain. These proteins facilitate the transport of nNOS to the plasma membrane, where it is catalytically activated by NMDA-receptor mediated calcium channels. The association of nNOS with PSD95 or PSD93 is regulated by CAPON. The carboxy terminus of CAPON binds to the PDZ domain, competes with PSD95 and PSD93 for binding to nNOS and in turn prevents the translocation and catalytic activation of nNOS.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerisation at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerisation at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, retinoid and xenobiotics. Preferentially oxidizes 17beta-estradiol to the carcinogenic 4-hydroxy derivative, and a variety of procarcinogenic compounds to their activated forms, including polycyclic aromatic hydrocarbons. Promotes angiogenesis by removing cellular oxygenation products, thereby decreasing oxidative stress, release of antiangiogenic factor THBS2, then allowing endothelial cells migration, cell adhesion and capillary morphogenesis. These changes are concommitant with the endothelial nitric oxide synthase activity and nitric oxide synthesis. Plays an important role in the regulation of perivascular cell proliferation, migration, and survival through modulation of the intracellular oxidative state and NF-kappa-B expression and/or activity, during angiogenesis. Contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression.

Supplier: Bioss

Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, retinoid and xenobiotics. Preferentially oxidizes 17beta-estradiol to the carcinogenic 4-hydroxy derivative, and a variety of procarcinogenic compounds to their activated forms, including polycyclic aromatic hydrocarbons. Promotes angiogenesis by removing cellular oxygenation products, thereby decreasing oxidative stress, release of antiangiogenic factor THBS2, then allowing endothelial cells migration, cell adhesion and capillary morphogenesis. These changes are concommitant with the endothelial nitric oxide synthase activity and nitric oxide synthesis. Plays an important role in the regulation of perivascular cell proliferation, migration, and survival through modulation of the intracellular oxidative state and NF-kappa-B expression and/or activity, during angiogenesis. Contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression.