Sie suchten nach: Adh\\\\u00E4sionstester

Artikel-Nr: (BOSSBS-12448R-CY5)

Lieferant: Bioss

Beschreibung: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.

VE: 1 * 100 µl

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Artikel-Nr: (BOSSBS-12449R-CY5)

Lieferant: Bioss

Beschreibung: ADH6 (alcohol dehydrogenase 6), also known as ADH-5, is a 368 amino acid member of the class V zinc-containing alcohol dehydrogenase family. This family of enzymes functions to metabolize a wide variety of substrates such as retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. Localized to the cytoplasm and expressed in the stomach and liver, ADH6 catalyzes the reversible oxidation of alcohols to their corresponding aldehydes or ketones and is able to bind two zinc ions as cofactors. ADH6 contains a glucocorticoid response element upstream of its 5' UTR which is thought to be a steroid binding site, suggesting that expression of ADH6 may be under hormonal control. Multiple isoforms of ADH6 exist due to alternative splicing events.

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Artikel-Nr: (BOSSBS-12449R-A750)

Lieferant: Bioss

Beschreibung: ADH6 (alcohol dehydrogenase 6), also known as ADH-5, is a 368 amino acid member of the class V zinc-containing alcohol dehydrogenase family. This family of enzymes functions to metabolize a wide variety of substrates such as retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. localised to the cytoplasm and expressed in the stomach and liver, ADH6 catalyses the reversible oxidation of alcohols to their corresponding aldehydes or ketones and is able to bind two zinc ions as cofactors. ADH6 contains a glucocorticoid response element upstream of its 5' UTR which is thought to be a steroid binding site, suggesting that expression of ADH6 may be under hormonal control. Multiple isoforms of ADH6 exist due to alternative splicing events.

VE: 1 * 100 µl

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Artikel-Nr: (BOSSBS-12449R-A488)

Lieferant: Bioss

Beschreibung: ADH6 (alcohol dehydrogenase 6), also known as ADH-5, is a 368 amino acid member of the class V zinc-containing alcohol dehydrogenase family. This family of enzymes functions to metabolize a wide variety of substrates such as retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. Localized to the cytoplasm and expressed in the stomach and liver, ADH6 catalyzes the reversible oxidation of alcohols to their corresponding aldehydes or ketones and is able to bind two zinc ions as cofactors. ADH6 contains a glucocorticoid response element upstream of its 5' UTR which is thought to be a steroid binding site, suggesting that expression of ADH6 may be under hormonal control. Multiple isoforms of ADH6 exist due to alternative splicing events.

VE: 1 * 100 µl

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Artikel-Nr: (BOSSBS-12448R-CY7)

Lieferant: Bioss

Beschreibung: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.

VE: 1 * 100 µl

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Artikel-Nr: (BOSSBS-12449R-A555)

Lieferant: Bioss

Beschreibung: ADH6 (alcohol dehydrogenase 6), also known as ADH-5, is a 368 amino acid member of the class V zinc-containing alcohol dehydrogenase family. This family of enzymes functions to metabolize a wide variety of substrates such as retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. Localized to the cytoplasm and expressed in the stomach and liver, ADH6 catalyzes the reversible oxidation of alcohols to their corresponding aldehydes or ketones and is able to bind two zinc ions as cofactors. ADH6 contains a glucocorticoid response element upstream of its 5' UTR which is thought to be a steroid binding site, suggesting that expression of ADH6 may be under hormonal control. Multiple isoforms of ADH6 exist due to alternative splicing events.

VE: 1 * 100 µl

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Artikel-Nr: (BOSSBS-12449R-A647)

Lieferant: Bioss

Beschreibung: ADH6 (alcohol dehydrogenase 6), also known as ADH-5, is a 368 amino acid member of the class V zinc-containing alcohol dehydrogenase family. This family of enzymes functions to metabolize a wide variety of substrates such as retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. Localized to the cytoplasm and expressed in the stomach and liver, ADH6 catalyzes the reversible oxidation of alcohols to their corresponding aldehydes or ketones and is able to bind two zinc ions as cofactors. ADH6 contains a glucocorticoid response element upstream of its 5' UTR which is thought to be a steroid binding site, suggesting that expression of ADH6 may be under hormonal control. Multiple isoforms of ADH6 exist due to alternative splicing events.

VE: 1 * 100 µl

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Artikel-Nr: (BOSSBS-12449R-A350)

Lieferant: Bioss

Beschreibung: ADH6 (alcohol dehydrogenase 6), also known as ADH-5, is a 368 amino acid member of the class V zinc-containing alcohol dehydrogenase family. This family of enzymes functions to metabolize a wide variety of substrates such as retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. Localized to the cytoplasm and expressed in the stomach and liver, ADH6 catalyzes the reversible oxidation of alcohols to their corresponding aldehydes or ketones and is able to bind two zinc ions as cofactors. ADH6 contains a glucocorticoid response element upstream of its 5' UTR which is thought to be a steroid binding site, suggesting that expression of ADH6 may be under hormonal control. Multiple isoforms of ADH6 exist due to alternative splicing events.

VE: 1 * 100 µl

Sale!

Artikel-Nr: (BOSSBS-12449R-CY7)

Lieferant: Bioss

Beschreibung: ADH6 (alcohol dehydrogenase 6), also known as ADH-5, is a 368 amino acid member of the class V zinc-containing alcohol dehydrogenase family. This family of enzymes functions to metabolize a wide variety of substrates such as retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. Localized to the cytoplasm and expressed in the stomach and liver, ADH6 catalyzes the reversible oxidation of alcohols to their corresponding aldehydes or ketones and is able to bind two zinc ions as cofactors. ADH6 contains a glucocorticoid response element upstream of its 5' UTR which is thought to be a steroid binding site, suggesting that expression of ADH6 may be under hormonal control. Multiple isoforms of ADH6 exist due to alternative splicing events.

VE: 1 * 100 µl

Sale!

Artikel-Nr: (BOSSBS-12449R)

Lieferant: Bioss

Beschreibung: ADH6 (alcohol dehydrogenase 6), also known as ADH-5, is a 368 amino acid member of the class V zinc-containing alcohol dehydrogenase family. This family of enzymes functions to metabolize a wide variety of substrates such as retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. Localized to the cytoplasm and expressed in the stomach and liver, ADH6 catalyzes the reversible oxidation of alcohols to their corresponding aldehydes or ketones and is able to bind two zinc ions as cofactors. ADH6 contains a glucocorticoid response element upstream of its 5' UTR which is thought to be a steroid binding site, suggesting that expression of ADH6 may be under hormonal control. Multiple isoforms of ADH6 exist due to alternative splicing events.

VE: 1 * 100 µl

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Artikel-Nr: (BOSSBS-12448R)

Lieferant: Bioss

Beschreibung: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.

VE: 1 * 100 µl

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Artikel-Nr: (BOSSBS-12448R-A680)

Lieferant: Bioss

Beschreibung: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.

VE: 1 * 100 µl

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Artikel-Nr: (BOSSBS-12448R-CY3)

Lieferant: Bioss

Beschreibung: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.

VE: 1 * 100 µl

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Artikel-Nr: (BOSSBS-12448R-HRP)

Lieferant: Bioss

Beschreibung: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.

VE: 1 * 100 µl

Sale!

Artikel-Nr: (BOSSBS-12448R-A488)

Lieferant: Bioss

Beschreibung: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.

VE: 1 * 100 µl

Sale!

Artikel-Nr: (BOSSBS-12448R-A750)

Lieferant: Bioss

Beschreibung: The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.

VE: 1 * 100 µl

Sale!