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Supplier: Thermo Scientific
Description: Zinc peroxide (∼50% ZnO₂)
Supplier: ENZO LIFE SCIENCES
Description: SOD (Superoxide dismutase) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells, they are: EC SOD (extracellular SOD), Cu/Zn SOD (copper and zinc-containing SOD) and Mn SOD (manganese-containing SOD).

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Supplier: ENZO LIFE SCIENCES
Description: SOD (Superoxide dismutase) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells, they are: EC SOD (extracellular SOD), Cu/Zn SOD (copper and zinc-containing SOD) and Mn SOD (manganese-containing SOD).

New Product

Supplier: ENZO LIFE SCIENCES
Description: SOD (Superoxide dismutase) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells, they are: EC SOD (extracellular SOD), Cu/Zn SOD (copper and zinc-containing SOD) and Mn SOD (manganese-containing SOD).

New Product

Supplier: ENZO LIFE SCIENCES
Description: SOD (Superoxide dismutase) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells, they are: EC SOD (extracellular SOD), Cu/Zn SOD (copper and zinc-containing SOD) and Mn SOD (manganese-containing SOD).

New Product

Catalog Number: (ENZOADISOD101E)
Supplier: ENZO LIFE SCIENCES
Description: SOD (Superoxide dismutase) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells, they are: EC SOD (extracellular SOD), Cu/Zn SOD (copper and zinc-containing SOD) and Mn SOD (manganese-containing SOD).
UOM: 1 * 100 µG

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Catalog Number: (BOSSBS-12449R-FITC)
Supplier: Bioss
Description: 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12449R-A555)
Supplier: Bioss
Description: 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12449R-A350)
Supplier: Bioss
Description: 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12449R-A647)
Supplier: Bioss
Description: 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12449R-A750)
Supplier: Bioss
Description: 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12449R-A488)
Supplier: Bioss
Description: 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-10216R-A647)
Supplier: Bioss
Description: The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene. [provided by RefSeq, Jul 2008]
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-10216R-CY5)
Supplier: Bioss
Description: The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene. [provided by RefSeq, Jul 2008]
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-10239R-CY7)
Supplier: Bioss
Description: The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene. [provided by RefSeq, Jul 2008]
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-10216R-HRP)
Supplier: Bioss
Description: The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene. [provided by RefSeq, Jul 2008]
UOM: 1 * 100 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at eurega_services@eu.vwr.com
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
This product has been blocked by your organisation. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
Product(s) marked with this symbol are discontinued - sold till end of stock. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service on +353 1 8822222.
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