464 Results for: "Redox-"

Supplier: Bioss

This multifunctional protein catalyses the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307).

Supplier: Thermo Orion

The metallic redox/ORP electrodes can be used to make direct measurements of redox potentials or to perform potentiometric titrations. The double platinum Orion™ combination electrode is designed for performing accurate Karl Fischer titrations.

Supplier: Bioss

Transcription factor involved in the induction of oxygen regulated genes. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation requires recruitment of transcriptional coactivators such as CREBPB and probably EP3. Interaction with redox regulatory protein APEX seems to activate CTAD (By similarity).

Supplier: Bioss

Transcription factor involved in the induction of oxygen regulated genes. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation requires recruitment of transcriptional coactivators such as CREBPB and probably EP3. Interaction with redox regulatory protein APEX seems to activate CTAD (By similarity).

Supplier: Bioss

Transcription factor involved in the induction of oxygen regulated genes. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation requires recruitment of transcriptional coactivators such as CREBPB and probably EP3. Interaction with redox regulatory protein APEX seems to activate CTAD (By similarity).

Supplier: Bioss

Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.

Supplier: Bioss

Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell-surface expression of HRH3. Has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. Could also promote endothelial cell proliferation and regulate endothelial morphogenesis.Tissue specificity: Detected in epithelial cells from colon, esophagus and kidney (at protein level). Expression is prominent in heart, kidney, placenta and skeletal muscle.

Supplier: VWR Collection

User friendly instrument distinguished by a large a 12,7 cm colour graphic touch screen. Can be used for accurate measurements of pH, mV, Redox potential (ORP), conductivity, salinity, TDS, resistivity and temperature. This pH meter enables simultaneous measurements displaying and storing of three functions (pH, conductivity and temperature).

Supplier: Bioss

This gene encodes an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), or NADH:ubiquinone oxidoreductase, the first multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I plays a vital role in cellular ATP production, the primary source of energy for many crucial processes in living cells. It removes electrons from NADH and passes them by a series of different protein-coupled redox centers to the electron acceptor ubiquinone. In well-coupled mitochondria, the electron flux leads to ATP generation via the building of a proton gradient across the inner membrane. Complex I is composed of at least 41 subunits, of which 7 are encoded by the mitochondrial genome and the remainder by nuclear genes. [provided by RefSeq, Jul 2008].

Supplier: Bioss

This gene encodes an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), or NADH:ubiquinone oxidoreductase, the first multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I plays a vital role in cellular ATP production, the primary source of energy for many crucial processes in living cells. It removes electrons from NADH and passes them by a series of different protein-coupled redox centers to the electron acceptor ubiquinone. In well-coupled mitochondria, the electron flux leads to ATP generation via the building of a proton gradient across the inner membrane. Complex I is composed of at least 41 subunits, of which 7 are encoded by the mitochondrial genome and the remainder by nuclear genes. [provided by RefSeq, Jul 2008].

Supplier: Hach

sensION+ 5057 is a combination platinum ORP electrode with a glass body and refillable liquid-electrolyte reference. It is dedicated for use with Hach sensION+ labpratory pH (mV) meters.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

This gene encodes an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), or NADH:ubiquinone oxidoreductase, the first multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I plays a vital role in cellular ATP production, the primary source of energy for many crucial processes in living cells. It removes electrons from NADH and passes them by a series of different protein-coupled redox centers to the electron acceptor ubiquinone. In well-coupled mitochondria, the electron flux leads to ATP generation via the building of a proton gradient across the inner membrane. Complex I is composed of at least 41 subunits, of which 7 are encoded by the mitochondrial genome and the remainder by nuclear genes. [provided by RefSeq, Jul 2008].

Supplier: Bioss

This gene encodes an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), or NADH:ubiquinone oxidoreductase, the first multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I plays a vital role in cellular ATP production, the primary source of energy for many crucial processes in living cells. It removes electrons from NADH and passes them by a series of different protein-coupled redox centers to the electron acceptor ubiquinone. In well-coupled mitochondria, the electron flux leads to ATP generation via the building of a proton gradient across the inner membrane. Complex I is composed of at least 41 subunits, of which 7 are encoded by the mitochondrial genome and the remainder by nuclear genes. [provided by RefSeq, Jul 2008].

Supplier: Bioss

Transcription factor involved in the induction of oxygen regulated genes. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation requires recruitment of transcriptional coactivators such as CREBPB and probably EP3. Interaction with redox regulatory protein APEX seems to activate CTAD (By similarity).

Supplier: Thermo Orion

Use the Orion Star T920 redox titrator for dedicated redox titrations including sulphite/SO₂ and reducing sugar in juice and wine, ascorbic acid (vitamin C) and peroxide value in food products, dissolved oxygen in wastewater by Winkler titration and organic matter in soil.

Supplier: Bioss

Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.

Supplier: Bioss

Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell-surface expression of HRH3. Has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. Could also promote endothelial cell proliferation and regulate endothelial morphogenesis.Tissue specificity: Detected in epithelial cells from colon, esophagus and kidney (at protein level). Expression is prominent in heart, kidney, placenta and skeletal muscle.

Supplier: Agrisera

Trxf1/2 (Thioredoxin F1/F2, chloroplastic) involved in the redox regulation of enzymes of Calvin-Benson cycle and oxidative pentose phosphate pathway. Alternative names: Thioredoxin F1, F2 AtTrxf1, AtTrxf2,Trxf1/2 (Thioredoxin F1/F2, chloroplastic) involved in the redox regulation of enzymes of Calvin-Benson cycle and oxidative pentose phosphate pathway. Alternative names: Thioredoxin F1, F2 AtTrxf1, AtTrxf2

Supplier: Bioss

This multifunctional protein catalyses the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307).

Supplier: Bioss

This multifunctional protein catalyses the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307).

Supplier: AAT BIOQUEST

Methylene Blue (MB) is widely used as a redox indicator in nucleic acid research.

Supplier: AAT BIOQUEST

Methylene Blue (MB) is widely used as a redox indicator in nucleic acid research.

Supplier: Bioss

This multifunctional protein catalyses the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307).

Supplier: Honeywell Chemicals

Ferroin (1,10-phenanthrolineferrous sulphate complex) solution Reag. Ph. Eur. redox indicator E0 (H2SO4 1 mol/l) = +1,06 volt, Fluka™

Supplier: Bioss

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.

Supplier: Bioss

This gene encodes an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), or NADH:ubiquinone oxidoreductase, the first multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I plays a vital role in cellular ATP production, the primary source of energy for many crucial processes in living cells. It removes electrons from NADH and passes them by a series of different protein-coupled redox centers to the electron acceptor ubiquinone. In well-coupled mitochondria, the electron flux leads to ATP generation via the building of a proton gradient across the inner membrane. Complex I is composed of at least 41 subunits, of which 7 are encoded by the mitochondrial genome and the remainder by nuclear genes. [provided by RefSeq, Jul 2008].

Supplier: AAT BIOQUEST

The monitoring of reduced and oxidised glutathione (GSH) in biological samples is essential for evaluating the redox and detoxification status of cells and tissues in relation to the protective role of glutathione against oxidative and free-radical-mediated cell injury.