Votre recherche pour: N-Lignoceroyl+taurine

Fournisseur: Cayman Chemical

Description: 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.

Numéro de catalogue: (BOSSBS-5808R-A350)

Fournisseur: Bioss

Description: 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.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5808R-A555)

Fournisseur: Bioss

Description: 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.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5808R-A680)

Fournisseur: Bioss

Description: 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.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5808R-CY5)

Fournisseur: Bioss

Description: 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.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5808R-HRP)

Fournisseur: Bioss

Description: 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.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5808R-FITC)

Fournisseur: Bioss

Description: 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.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5808R-CY5.5)

Fournisseur: Bioss

Description: 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.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5808R-CY3)

Fournisseur: Bioss

Description: 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.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5808R-A647)

Fournisseur: Bioss

Description: 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.

UOM: 1 * 100 µl

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Numéro de catalogue: (PRSI26-066)

Fournisseur: ProSci Inc.

Description: BAAT is a liver enzyme that catalyzes the transfer of C24 bile acids from the acyl-CoA thioester to either glycine or taurine, the second step in the formation of bile acid-amino acid conjugates. The bile acid conjugates then act as a detergent in the gastrointestinal tract, which enhances lipid and fat-soluble vitamin absorption. Defects in this gene are a cause of familial hypercholanemia (FHCA). The protein encoded by this gene is a liver enzyme that catalyzes the transfer of C24 bile acids from the acyl-CoA thioester to either glycine or taurine, the second step in the formation of bile acid-amino acid conjugates. The bile acid conjugates then act as a detergent in the gastrointestinal tract, which enhances lipid and fat-soluble vitamin absorption. Defects in this gene are a cause of familial hypercholanemia (FHCA). Two transcript variants encoding the same protein have been found for this gene.

UOM: 1 * 50 µG

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Numéro de catalogue: (BOSSBS-5040R-A750)

Fournisseur: Bioss

Description: 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.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5040R-A555)

Fournisseur: Bioss

Description: 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.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5040R-CY5.5)

Fournisseur: Bioss

Description: 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.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5040R-FITC)

Fournisseur: Bioss

Description: 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.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5040R-CY7)

Fournisseur: Bioss

Description: 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.

UOM: 1 * 100 µl

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