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Description: Glutathione reductase (GR) is a member of pyridine nucleotide- disulfideoxidoreductases, which includes the closely related enzymes thioredoxin reductase, lipoamide dehydrogenase, trypanothione reductase and mercuric ion reductase. GR is a cytoplasmic flavoenzyme widely distributed in aerobic organisms. The dimeric protein is composed of two identical subunits, each containing 1 FAD and 1 redox-active disulfide/dithiol as components of the catalytic apparatus. It plays a role in maintaining glutathione (GSH) in its reduced form by catalyzing the reduction of glutathione disulfide (GSSG): GSSG + NADPH + H+?2GSH + NADP+. In mosteukaryotic cells, GR maintains the ratio of [GSH]/[GSSG], and participates in several vital functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis.

Catalog Number: 10357-840

Supplier: Bioss

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Description: At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. GSTM2 is a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione.Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs.

Catalog Number: 10108-642

Supplier: Prosci

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Description: Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. GSTM3 is a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Mutations of this class mu gene have been linked with a slight increase in a number of cancers, likely due to exposure with environmental toxins.Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Mutations of this class mu gene have been linked with a slight increase in a number of cancers, likely due to exposure with environmental toxins. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Catalog Number: 10110-856

Supplier: Prosci

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Description: Glutathione reductase (GR) is a member of pyridine nucleotide- disulfideoxidoreductases, which includes the closely related enzymes thioredoxin reductase, lipoamide dehydrogenase, trypanothione reductase and mercuric ion reductase. GR is a cytoplasmic flavoenzyme widely distributed in aerobic organisms. The dimeric protein is composed of two identical subunits, each containing 1 FAD and 1 redox-active disulfide/dithiol as components of the catalytic apparatus. It plays a role in maintaining glutathione (GSH) in its reduced form by catalyzing the reduction of glutathione disulfide (GSSG): GSSG + NADPH + H+?2GSH + NADP+. In mosteukaryotic cells, GR maintains the ratio of [GSH]/[GSSG], and participates in several vital functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis.

Catalog Number: 10357-844

Supplier: Bioss

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Description: Glutathione reductase (GR) is a member of pyridine nucleotide- disulfideoxidoreductases, which includes the closely related enzymes thioredoxin reductase, lipoamide dehydrogenase, trypanothione reductase and mercuric ion reductase. GR is a cytoplasmic flavoenzyme widely distributed in aerobic organisms. The dimeric protein is composed of two identical subunits, each containing 1 FAD and 1 redox-active disulfide/dithiol as components of the catalytic apparatus. It plays a role in maintaining glutathione (GSH) in its reduced form by catalyzing the reduction of glutathione disulfide (GSSG): GSSG + NADPH + H+?2GSH + NADP+. In mosteukaryotic cells, GR maintains the ratio of [GSH]/[GSSG], and participates in several vital functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis.

Catalog Number: 10357-846

Supplier: Bioss

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Description: Glutathione S-transferases (GSTs) function to conjugate reduced glutathione to many exogenous and endogenous hydrophobic electrophiles. Although it shares the carboxy and amino-terminal glutathione S-transferase domains, GDAP1 is characterized as a GST-like protein because it contains an extended GST domain II and a predicted transmembrane domain, two characteristics which are unusual for GST family members. GDAP1 may function in a signal transduction pathway that is responsible for ganglioside-induced neurite differentiation and also may play a role in protecting myelin membranes from free-radical damage. Mutations in the gene encoding GDAP1 is the cause of many forms of Charcot-Marie-Tooth disease, a common inherited disorder of the peripheral nervous system that is characterized by reduced nerve conduction velocities, slow progressive distal muscle atrophy and absent deep tendon reflexes.

Catalog Number: 10266-180

Supplier: Bioss

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Description: Glutathione S-transferases (GSTs) function to conjugate reduced glutathione to many exogenous and endogenous hydrophobic electrophiles. Although it shares the carboxy and amino-terminal glutathione S-transferase domains, GDAP1 is characterized as a GST-like protein because it contains an extended GST domain II and a predicted transmembrane domain, two characteristics which are unusual for GST family members. GDAP1 may function in a signal transduction pathway that is responsible for ganglioside-induced neurite differentiation and also may play a role in protecting myelin membranes from free-radical damage. Mutations in the gene encoding GDAP1 is the cause of many forms of Charcot-Marie-Tooth disease, a common inherited disorder of the peripheral nervous system that is characterized by reduced nerve conduction velocities, slow progressive distal muscle atrophy and absent deep tendon reflexes.

Catalog Number: 10260-114

Supplier: Bioss

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Description: 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.

Catalog Number: 10282-046

Supplier: Bioss

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Description: See also G-4745, H-3996, the branched substrates H-2416, and L-2070, and the product families 'Glutathione-Related Peptides' and 'Ophthalmic Acid'.

Catalog Number: G-1970.0250BA

Supplier: Bachem Americas

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Description: 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.

Catalog Number: 10282-042

Supplier: Bioss

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Description: 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.

Catalog Number: 10282-044

Supplier: Bioss

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Description: Glutathione S-transferases (GSTs) function to conjugate reduced glutathione to many exogenous and endogenous hydrophobic electrophiles. Although it shares the carboxy and amino-terminal glutathione S-transferase domains, GDAP1 is characterized as a GST-like protein because it contains an extended GST domain II and a predicted transmembrane domain, two characteristics which are unusual for GST family members. GDAP1 may function in a signal transduction pathway that is responsible for ganglioside-induced neurite differentiation and also may play a role in protecting myelin membranes from free-radical damage. Mutations in the gene encoding GDAP1 is the cause of many forms of Charcot-Marie-Tooth disease, a common inherited disorder of the peripheral nervous system that is characterized by reduced nerve conduction velocities, slow progressive distal muscle atrophy and absent deep tendon reflexes.

Catalog Number: 10260-108

Supplier: Bioss

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Description: Glutathione S-transferases (GSTs) function to conjugate reduced glutathione to many exogenous and endogenous hydrophobic electrophiles. Although it shares the carboxy and amino-terminal glutathione S-transferase domains, GDAP1 is characterized as a GST-like protein because it contains an extended GST domain II and a predicted transmembrane domain, two characteristics which are unusual for GST family members. GDAP1 may function in a signal transduction pathway that is responsible for ganglioside-induced neurite differentiation and also may play a role in protecting myelin membranes from free-radical damage. Mutations in the gene encoding GDAP1 is the cause of many forms of Charcot-Marie-Tooth disease, a common inherited disorder of the peripheral nervous system that is characterized by reduced nerve conduction velocities, slow progressive distal muscle atrophy and absent deep tendon reflexes.

Catalog Number: 10260-112

Supplier: Bioss

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Description: Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. mutations of this class mu gene have been linked with an increase in a number of cancers, likely due to an increased susceptibility to environmental toxins and carcinogens. Multiple protein isoforms are encoded by transcript variants of this gene. (provided by RefSeq, Jul 2008).

Catalog Number: 77436-828

Supplier: Bioss

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Description: This gene encodes a member of the gamma-glutamyl transpeptidase (GGT) family, which are important in the metabolism of glutathione. The most ubiquitously expressed human GGT gene, GGT1, encodes a single transmembrane polypeptide that is post-translationally processed to form a heavy and a light chain. In contrast, the product of this gene only contains homology to the light chain region, and lacks a transmembrane domain. Multiple alternatively spliced variants, encoding the same protein, have been identified.

Catalog Number: 10296-808

Supplier: Bioss

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Description: This gene encodes a member of the gamma-glutamyl transpeptidase (GGT) family, which are important in the metabolism of glutathione. The most ubiquitously expressed human GGT gene, GGT1, encodes a single transmembrane polypeptide that is post-translationally processed to form a heavy and a light chain. In contrast, the product of this gene only contains homology to the light chain region, and lacks a transmembrane domain. Multiple alternatively spliced variants, encoding the same protein, have been identified.

Catalog Number: 10296-806

Supplier: Bioss

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