1377 Results for: "(Methylamino)acetaldehyde+dimethylacetal"

Supplier: Bioss

Aldehyde dehydrogenases (ALDHs) mediate the NADP+-dependent oxidation of aldehydes into acids and play an important role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH3A2 (aldehyde dehydrogenase 3 family, member A2), also known as SLS, FALDH or ALDH10, is a 485 amino acid single-pass membrane protein that localizes to the cytoplasmic side of the endoplasmic reticulum and belongs to the aldehyde dehydrogenase family. Expressed in a variety of tissues, including liver, heart, lung, brain, kidney and placenta, ALDH3A2 catalyzes the NAD+-dependent oxidation of long-chain aliphatic aldehydes to fatty acids, a process that is necessary for detoxification and lipid metabolism. Defects in the gene encoding ALDH3A2 are the cause of Sjoegren-Larsson syndrome (SLS), an autosomal recessive neurocutaneous disorder characterized by severe mental retardation, seizures and speech defects. Multiple isoforms of ALDH3A2 exist due to alternative splicing events.

Supplier: Bioss

Aldehyde dehydrogenases (ALDHs) mediate the NADP+-dependent oxidation of aldehydes into acids and play an important role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH3A2 (aldehyde dehydrogenase 3 family, member A2), also known as SLS, FALDH or ALDH10, is a 485 amino acid single-pass membrane protein that localizes to the cytoplasmic side of the endoplasmic reticulum and belongs to the aldehyde dehydrogenase family. Expressed in a variety of tissues, including liver, heart, lung, brain, kidney and placenta, ALDH3A2 catalyses the NAD+-dependent oxidation of long-chain aliphatic aldehydes to fatty acids, a process that is necessary for detoxification and lipid metabolism. Defects in the gene encoding ALDH3A2 are the cause of Sjoegren-Larsson syndrome (SLS), an autosomal recessive neurocutaneous disorder characterised by severe mental retardation, seizures and speech defects. Multiple isoforms of ALDH3A2 exist due to alternative splicing events.

Supplier: USP

3-Desmethyl Ivabradine Hydrochloride (25 mg) (1,3,4,5-tetrahydro-3-[3-[[[(7S)-3-hydroxy-4-methoxybicyclo[4.2.0]octa-1,3,5-trien-7-yl ]methyl]methylamino]propyl]-7,8-dimethoxy-2H-3-benzazepin-2-one, hydrochloride) 1 * 25 mg

Supplier: Bioss

Aldehyde dehydrogenases (ALDHs) mediate the NADP+-dependent oxidation of aldehydes into acids and play an important role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH3A2 (aldehyde dehydrogenase 3 family, member A2), also known as SLS, FALDH or ALDH10, is a 485 amino acid single-pass membrane protein that localizes to the cytoplasmic side of the endoplasmic reticulum and belongs to the aldehyde dehydrogenase family. Expressed in a variety of tissues, including liver, heart, lung, brain, kidney and placenta, ALDH3A2 catalyzes the NAD+-dependent oxidation of long-chain aliphatic aldehydes to fatty acids, a process that is necessary for detoxification and lipid metabolism. Defects in the gene encoding ALDH3A2 are the cause of Sjoegren-Larsson syndrome (SLS), an autosomal recessive neurocutaneous disorder characterized by severe mental retardation, seizures and speech defects. Multiple isoforms of ALDH3A2 exist due to alternative splicing events.

Supplier: Bioss

Aldehyde dehydrogenases (ALDHs) mediate the NADP+-dependent oxidation of aldehydes into acids and play an important role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH3A2 (aldehyde dehydrogenase 3 family, member A2), also known as SLS, FALDH or ALDH10, is a 485 amino acid single-pass membrane protein that localizes to the cytoplasmic side of the endoplasmic reticulum and belongs to the aldehyde dehydrogenase family. Expressed in a variety of tissues, including liver, heart, lung, brain, kidney and placenta, ALDH3A2 catalyzes the NAD+-dependent oxidation of long-chain aliphatic aldehydes to fatty acids, a process that is necessary for detoxification and lipid metabolism. Defects in the gene encoding ALDH3A2 are the cause of Sjoegren-Larsson syndrome (SLS), an autosomal recessive neurocutaneous disorder characterized by severe mental retardation, seizures and speech defects. Multiple isoforms of ALDH3A2 exist due to alternative splicing events.

Supplier: Bioss

Aldehyde dehydrogenases (ALDHs) mediate the NADP+-dependent oxidation of aldehydes into acids and play an important role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH3A2 (aldehyde dehydrogenase 3 family, member A2), also known as SLS, FALDH or ALDH10, is a 485 amino acid single-pass membrane protein that localizes to the cytoplasmic side of the endoplasmic reticulum and belongs to the aldehyde dehydrogenase family. Expressed in a variety of tissues, including liver, heart, lung, brain, kidney and placenta, ALDH3A2 catalyzes the NAD+-dependent oxidation of long-chain aliphatic aldehydes to fatty acids, a process that is necessary for detoxification and lipid metabolism. Defects in the gene encoding ALDH3A2 are the cause of Sjoegren-Larsson syndrome (SLS), an autosomal recessive neurocutaneous disorder characterized by severe mental retardation, seizures and speech defects. Multiple isoforms of ALDH3A2 exist due to alternative splicing events.

Supplier: Bioss

Aldehyde dehydrogenases (ALDHs) mediate the NADP+-dependent oxidation of aldehydes into acids and play an important role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH3A2 (aldehyde dehydrogenase 3 family, member A2), also known as SLS, FALDH or ALDH10, is a 485 amino acid single-pass membrane protein that localizes to the cytoplasmic side of the endoplasmic reticulum and belongs to the aldehyde dehydrogenase family. Expressed in a variety of tissues, including liver, heart, lung, brain, kidney and placenta, ALDH3A2 catalyzes the NAD+-dependent oxidation of long-chain aliphatic aldehydes to fatty acids, a process that is necessary for detoxification and lipid metabolism. Defects in the gene encoding ALDH3A2 are the cause of Sjoegren-Larsson syndrome (SLS), an autosomal recessive neurocutaneous disorder characterized by severe mental retardation, seizures and speech defects. Multiple isoforms of ALDH3A2 exist due to alternative splicing events.

Supplier: Bioss

Aldehyde dehydrogenases (ALDHs) mediate the NADP+-dependent oxidation of aldehydes into acids and play an important role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH3A2 (aldehyde dehydrogenase 3 family, member A2), also known as SLS, FALDH or ALDH10, is a 485 amino acid single-pass membrane protein that localizes to the cytoplasmic side of the endoplasmic reticulum and belongs to the aldehyde dehydrogenase family. Expressed in a variety of tissues, including liver, heart, lung, brain, kidney and placenta, ALDH3A2 catalyzes the NAD+-dependent oxidation of long-chain aliphatic aldehydes to fatty acids, a process that is necessary for detoxification and lipid metabolism. Defects in the gene encoding ALDH3A2 are the cause of Sjoegren-Larsson syndrome (SLS), an autosomal recessive neurocutaneous disorder characterized by severe mental retardation, seizures and speech defects. Multiple isoforms of ALDH3A2 exist due to alternative splicing events.

Supplier: Bioss

Aldehyde dehydrogenases (ALDHs) mediate the NADP+-dependent oxidation of aldehydes into acids and play an important role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH3A2 (aldehyde dehydrogenase 3 family, member A2), also known as SLS, FALDH or ALDH10, is a 485 amino acid single-pass membrane protein that localizes to the cytoplasmic side of the endoplasmic reticulum and belongs to the aldehyde dehydrogenase family. Expressed in a variety of tissues, including liver, heart, lung, brain, kidney and placenta, ALDH3A2 catalyzes the NAD+-dependent oxidation of long-chain aliphatic aldehydes to fatty acids, a process that is necessary for detoxification and lipid metabolism. Defects in the gene encoding ALDH3A2 are the cause of Sjoegren-Larsson syndrome (SLS), an autosomal recessive neurocutaneous disorder characterized by severe mental retardation, seizures and speech defects. Multiple isoforms of ALDH3A2 exist due to alternative splicing events.

Supplier: Bioss

Aldehyde dehydrogenases (ALDHs) mediate the NADP+-dependent oxidation of aldehydes into acids and play an important role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH3A2 (aldehyde dehydrogenase 3 family, member A2), also known as SLS, FALDH or ALDH10, is a 485 amino acid single-pass membrane protein that localizes to the cytoplasmic side of the endoplasmic reticulum and belongs to the aldehyde dehydrogenase family. Expressed in a variety of tissues, including liver, heart, lung, brain, kidney and placenta, ALDH3A2 catalyzes the NAD+-dependent oxidation of long-chain aliphatic aldehydes to fatty acids, a process that is necessary for detoxification and lipid metabolism. Defects in the gene encoding ALDH3A2 are the cause of Sjoegren-Larsson syndrome (SLS), an autosomal recessive neurocutaneous disorder characterized by severe mental retardation, seizures and speech defects. Multiple isoforms of ALDH3A2 exist due to alternative splicing events.

Supplier: Bioss

Aldehyde dehydrogenases (ALDHs) mediate the NADP+-dependent oxidation of aldehydes into acids and play an important role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH3A2 (aldehyde dehydrogenase 3 family, member A2), also known as SLS, FALDH or ALDH10, is a 485 amino acid single-pass membrane protein that localizes to the cytoplasmic side of the endoplasmic reticulum and belongs to the aldehyde dehydrogenase family. Expressed in a variety of tissues, including liver, heart, lung, brain, kidney and placenta, ALDH3A2 catalyzes the NAD+-dependent oxidation of long-chain aliphatic aldehydes to fatty acids, a process that is necessary for detoxification and lipid metabolism. Defects in the gene encoding ALDH3A2 are the cause of Sjoegren-Larsson syndrome (SLS), an autosomal recessive neurocutaneous disorder characterized by severe mental retardation, seizures and speech defects. Multiple isoforms of ALDH3A2 exist due to alternative splicing events.

Supplier: Bioss

Aldehyde dehydrogenases (ALDHs) mediate the NADP+-dependent oxidation of aldehydes into acids and play an important role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH3A2 (aldehyde dehydrogenase 3 family, member A2), also known as SLS, FALDH or ALDH10, is a 485 amino acid single-pass membrane protein that localizes to the cytoplasmic side of the endoplasmic reticulum and belongs to the aldehyde dehydrogenase family. Expressed in a variety of tissues, including liver, heart, lung, brain, kidney and placenta, ALDH3A2 catalyses the NAD+-dependent oxidation of long-chain aliphatic aldehydes to fatty acids, a process that is necessary for detoxification and lipid metabolism. Defects in the gene encoding ALDH3A2 are the cause of Sjoegren-Larsson syndrome (SLS), an autosomal recessive neurocutaneous disorder characterised by severe mental retardation, seizures and speech defects. Multiple isoforms of ALDH3A2 exist due to alternative splicing events.

Supplier: Bioss

Aldehyde dehydrogenases (ALDHs) mediate NADP+-dependent oxidation of aldehydes into acids during the detoxification of alcohol-derived acetaldehyde; metabolism of corticosteroids, biogenic amines and neurotransmitters; and lipid peroxidation. ALDH1A1, also designated retinal dehydrogenase 1 (RalDH1 or RALDH1), aldehyde dehydrogenase family 1 member A1, aldehyde dehydrogenase cytosolic, ALDHII, ALDH-E1 or ALDH E1, is a retinal dehydrogenase that participates in the biosynthesis of retinoic acid (RA). There are two major liver isoforms of ALDH1 that can localize to cytosolic or mitochondrial space. The ALDH1A2 (RALDH2, RALDH2-T) gene produces three different transcripts and also catalyzes the synthesis of RA from retinaldehyde. ALDH1A3 (ALDH6, RALDH3, ALDH1A6) is a 37 kb gene that consists of 13 exons and produces a major transcript of approximately 3.5 kb most abundant in salivary gland, stomach and kidney. ALDH3A1 (stomach type, ALDH3, ALDHIII) forms a cytoplasmic homodimer that preferentially oxidizes aromatic aldehyde substrates. ALDH genes upregulate as a part of the oxidative stress response, and appear to be abundant in certain tumors that have an accelerated metabolism toward chemotherapy agents.

Supplier: Bioss

Aldehyde dehydrogenases (ALDHs) mediate NADP+-dependent oxidation of aldehydes into acids during the detoxification of alcohol-derived acetaldehyde; metabolism of corticosteroids, biogenic amines and neurotransmitters; and lipid peroxidation. ALDH1A1, also designated retinal dehydrogenase 1 (RalDH1 or RALDH1), aldehyde dehydrogenase family 1 member A1, aldehyde dehydrogenase cytosolic, ALDHII, ALDH-E1 or ALDH E1, is a retinal dehydrogenase that participates in the biosynthesis of retinoic acid (RA). There are two major liver isoforms of ALDH1 that can localize to cytosolic or mitochondrial space. The ALDH1A2 (RALDH2, RALDH2-T) gene produces three different transcripts and also catalyzes the synthesis of RA from retinaldehyde. ALDH1A3 (ALDH6, RALDH3, ALDH1A6) is a 37 kb gene that consists of 13 exons and produces a major transcript of approximately 3.5 kb most abundant in salivary gland, stomach and kidney. ALDH3A1 (stomach type, ALDH3, ALDHIII) forms a cytoplasmic homodimer that preferentially oxidizes aromatic aldehyde substrates. ALDH genes upregulate as a part of the oxidative stress response, and appear to be abundant in certain tumors that have an accelerated metabolism toward chemotherapy agents.

Supplier: MP Biomedicals

Storage: +4 °C
Pyruvic acid is an intermediate in sugar metabolism and in enzymatic carbohydrate degradation (alcoholic fermentation) where it is converted to acetaldehyde and CO2 by carboxylase. In muscle, pyruvic acid (derived from glycogen) is reduced to lactic acid during exertion, which is reoxidized and partially retransformed to glycogen during rest. It improves coliform recovery when present in culture medium. It is involved in a metabolic regulatory pathway activated by mitochondrial oxidants. Pyruvate is involved in respiratory regulation in plants by interacting with alternative oxidase at a conserved cysteine residue. It may help prevent hydrogen peroxide mediated cell death.
Sodium pyruvate is utilized as a component in culture broth and media. Sodium pyruvate is used in Wallen fermentation medium to enhance the conversion of oleic acid to 10-ketostearic acid by Bacillus sphaericus. Sodium pyruvate has also been used to establish stably transfected human B cell lines.
Sodium Pyruvate has shown antioxidant properties and protective effects against oxygen radicals. Pyruvate is produced as part of glycolysis and is an intermediate in many metabolic pathways. It can be converted into acetyl CoA and enter the TCA Cycle.

Supplier: Thermo Fisher Scientific

Formaldehyde dimethyl acetal ≥98%

Supplier: Merck

Formaldehyde dimethyl acetal for synthesis, Sigma-Aldrich®

Supplier: Merck

Acetal ≥98% for synthesis, Sigma-Aldrich®

Supplier: Apollo Scientific

2-Cyano-2-methylpropanoic acid 98%

Supplier: Merck

Acetonedimethyl acetal, Supelco®

Supplier: Thermo Fisher Scientific

Formaldehyde dimethyl acetal 99.5+%

Supplier: Apollo Scientific

Methyl-2-cyano-2-methylpropanoate 95+%

Supplier: Merck

For full details of specification and hazards please see www.vwr.com or the VWR Chemicals catalogues.

Supplier: Thermo Fisher Scientific

Acetal 99%

Supplier: Thermo Fisher Scientific

4-(Trifluoromethyl)phenylglyoxal hydrate 98%

Supplier: Apollo Scientific

4-(Trifluoromethyl)phenylglyoxal hydrate 97%

Supplier: Thermo Fisher Scientific

Acetonedimethyl acetal 98+%

Supplier: Thermo Fisher Scientific

Metaldehyde 98%

Supplier: Apollo Scientific

3-Methoxyphenylglyoxal hydrate 96%

Supplier: Apollo Scientific

α,α-Dimethoxytoluene