Supplier: Bioss

Highly selective for arachidonate-containing species of diacylglycerol (DAG). May terminate signals transmitted through arachidonoyl-DAG or may contribute to the synthesis of phospholipids with defined fatty acid composition.

Supplier: Bioss

Catalyzes the hydrolysis of diacylglycerol (DAG) to 2-arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in tissues. Required for axonal growth during development and for retrograde synaptic signaling at mature synapses.

Supplier: Bioss

Catalyzes the hydrolysis of diacylglycerol (DAG) to 2-arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in tissues. Required for axonal growth during development and for retrograde synaptic signaling at mature synapses.

Supplier: Bioss

Catalyzes the hydrolysis of diacylglycerol (DAG) to 2-arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in tissues. Required for axonal growth during development and for retrograde synaptic signaling at mature synapses.

Supplier: Bioss

Highly selective for arachidonate-containing species of diacylglycerol (DAG). May terminate signals transmitted through arachidonoyl-DAG or may contribute to the synthesis of phospholipids with defined fatty acid composition.

Supplier: ProSci Inc.

The protein encoded by this gene is a catalytic subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.

Supplier: Bioss

CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Supplier: Bioss

CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Supplier: Bioss

CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyse the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukaemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Supplier: Bioss

CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Supplier: Bioss

Highly selective for arachidonate-containing species of diacylglycerol (DAG). May terminate signals transmitted through arachidonoyl-DAG or may contribute to the synthesis of phospholipids with defined fatty acid composition.

Supplier: Thermo Fisher Scientific

N-(2-Acetamido)-2-aminoethanesulphonic acid (ACES) ≥99%

Supplier: Thermo Fisher Scientific

N-(2-Acetamido)-2-aminoethanesulphonic acid (ACES) 99%, Extra Pure

Supplier: Cayman Chemical

Taurodeoxycholic acid is a taurine-conjugated form of the secondary bile acid deoxycholic acid. Taurodeoxycholic acid stimulates chloride ion secretion through calcium-activated chloride ion channels and cystic fibrosis transmembrane conductance regulator (CFTR) in Calu-3 airway epithelial cell monolayers when applied basolaterally. Serum levels of taurodeoxycholic acid increase approximately 5-fold in within two hours during an oral lipid tolerance test in humans.

Supplier: Bioss

CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyse the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukaemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Supplier: Bioss

CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Supplier: Bioss

CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Supplier: Bioss

CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Supplier: Bioss

CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Supplier: Bioss

CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Supplier: Bioss

CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Supplier: Bioss

GLYATL2 is a 294 amino acid mitochondrial acyltransferase that transfers the acyl group to the N-terminus of glycine. GLYATL2 can also conjugate a multitude of substrates, including oleoyl-CoA and arachidonoyl-CoA, to form a variety of N-acylglycines. A member of the glycine N-acyltransferase family, GLYATL2 is encoded by a gene that maps to human chromosome 11q12.1. Chromosome 11 houses over 1,400 genes and comprises nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that maps to chromosome 11.

Supplier: Bioss

G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis (By similarity). Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury.

Supplier: Bioss

G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis (By similarity). Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury.

Supplier: Bioss

CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Supplier: Bioss

CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Supplier: Bioss

GLYATL2 is a 294 amino acid mitochondrial acyltransferase that transfers the acyl group to the N-terminus of glycine. GLYATL2 can also conjugate a multitude of substrates, including oleoyl-CoA and arachidonoyl-CoA, to form a variety of N-acylglycines. A member of the glycine N-acyltransferase family, GLYATL2 is encoded by a gene that maps to human chromosome 11q12.1. Chromosome 11 houses over 1,400 genes and comprises nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that maps to chromosome 11.

Supplier: Bioss

Involved in bile acid metabolism. In liver hepatocytes catalyses the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyse the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyses the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs.

Supplier: Bioss

Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs.

Supplier: Thermo Fisher Scientific

Taurodeoxycholic acid sodium salt hydrate 97%