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: 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 centres 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.

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 centres 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.

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 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: Honeywell Chemicals

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

Supplier: Hach

sensION+ 5055 is a combination platinum ORP electrode with a polycarbonate body and non refillable gel-electrolyte reference. It is dedicated for use with Hach sensION+ portable pH (mV) meters.

Supplier: AAT BIOQUEST

Resazurin is a non-toxic, water-soluble and redox-sensitive dye that changes from its blue/non-fluorescent state to pink/highly-fluorescent upon reduction to resorufin by many biological processes.

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: WTW

This two-channel instrument is ideal for precision measurements of pH, ISE or Redox and automatic documentation acc. to GLP/ AQA as required by accredited laboratories. The high resolution measurements can be controlled conveniently and easily via a graphical user interface.

Supplier: AAT BIOQUEST

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

Supplier: Mettler - Toledo

Electrode, pH, LE series, Redox electrode LE501, refillable, pH: -, 0...+80 °C, Glass, Diaphr.: Ceramic, Electrolyte: KCl 3 mol/l, Ø×L: 12×120 mm, BNC, 1 m cable, For: Dirty solutions, water treatments

Supplier: Bioss

Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 4 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP3. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.

Supplier: Bioss

Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 4 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP3. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.

Supplier: AAT BIOQUEST

Protein thiols are very important to protein structure, protein function and biological system redox environment.

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

Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 4 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP3. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.

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

The subcellular detection and localization of GSH is important in understanding the modulation of redox status, the effect of drugs, and the mechanisms of detoxification.

Supplier: Hach

The Radiometer Analytical electrode range features single, double, and combined metal electrodes with platinum, silver, gold, antimony, mercury and glassy carbon sensing elements. This variety of designs can be used for redox measurements, redox titrations, potentiometric techniques, and imposed current potentiometric titration.

Supplier: CUSTOM MADE CHEMICALS LAB

It can be used as a redox titrant in iodometry for TMAR chlorine determination according to SERES. It is an inorganic compound with an excellent shelf life.

Supplier: Bioss

The single-stranded-DNA-binding proteins (SSBs) are essential for DNA function in prokaryotic and eukaryotic cells, mitochondria, phages and viruses. Replication protein A (RPA), a highly conserved eukaryotic protein, is a heterotrimeric SSB. RPA plays an important role in DNA replication, recombination and repair. The binding of human RPA (hRPA) to DNA involves molecular polarity in which initial hRPA binding occurs on the 5' side of an ssDNA substrate and then extends in the 3' direction to create a stably bound hRPA. RPA is a major damage-recognition protein involved in the early stages of nucleotide excision repair. It can also play a role in telomere maintenance. The RPA 70 kDa subunit binds to ssDNA and mediates interactions with many cellular and viral proteins. The DNA binding domain lies in the middle of RPA 70 kDa subunit and comprises two structurally homologous subdomains oriented in tandem. RPA contains a conserved four cysteine-type zinc-finger motif, which mediates the transition of RPA-ssDNA interaction to a stable RPA-ssDNA complex in a redox-dependent manner.

Supplier: AAT BIOQUEST

Catalase is a common antioxidant heme-containing redox enzyme found in nearly all living organisms that are exposed to oxygen.

Supplier: ProSci Inc.

The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP-ribosylation, histone deacetylation, and in some Ca (2+) signaling pathways. NMNAT (EC 2.7.7.1) is a central enzyme in NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD.The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP-ribosylation, histone deacetylation, and in some Ca (2+) signaling pathways. NMNAT (EC 2.7.7.1) is a central enzyme in NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD (Zhang et al., 2003 [PubMed 12574164]).

Supplier: Bioss

The single-stranded-DNA-binding proteins (SSBs) are essential for DNA function in prokaryotic and eukaryotic cells, mitochondria, phages and viruses. Replication protein A (RPA), a highly conserved eukaryotic protein, is a heterotrimeric SSB. RPA plays an important role in DNA replication, recombination and repair. The binding of human RPA (hRPA) to DNA involves molecular polarity in which initial hRPA binding occurs on the 5' side of an ssDNA substrate and then extends in the 3' direction to create a stably bound hRPA. RPA is a major damage-recognition protein involved in the early stages of nucleotide excision repair. It can also play a role in telomere maintenance. The RPA 70 kDa subunit binds to ssDNA and mediates interactions with many cellular and viral proteins. The DNA binding domain lies in the middle of RPA 70 kDa subunit and comprises two structurally homologous subdomains oriented in tandem. RPA contains a conserved four cysteine-type zinc-finger motif, which mediates the transition of RPA-ssDNA interaction to a stable RPA-ssDNA complex in a redox-dependent manner.

Supplier: Bioss

The single-stranded-DNA-binding proteins (SSBs) are essential for DNA function in prokaryotic and eukaryotic cells, mitochondria, phages and viruses. Replication protein A (RPA), a highly conserved eukaryotic protein, is a heterotrimeric SSB. RPA plays an important role in DNA replication, recombination and repair. The binding of human RPA (hRPA) to DNA involves molecular polarity in which initial hRPA binding occurs on the 5' side of an ssDNA substrate and then extends in the 3' direction to create a stably bound hRPA. RPA is a major damage-recognition protein involved in the early stages of nucleotide excision repair. It can also play a role in telomere maintenance. The RPA 70 kDa subunit binds to ssDNA and mediates interactions with many cellular and viral proteins. The DNA binding domain lies in the middle of RPA 70 kDa subunit and comprises two structurally homologous subdomains oriented in tandem. RPA contains a conserved four cysteine-type zinc-finger motif, which mediates the transition of RPA-ssDNA interaction to a stable RPA-ssDNA complex in a redox-dependent manner.

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

The single-stranded-DNA-binding proteins (SSBs) are essential for DNA function in prokaryotic and eukaryotic cells, mitochondria, phages and viruses. Replication protein A (RPA), a highly conserved eukaryotic protein, is a heterotrimeric SSB. RPA plays an important role in DNA replication, recombination and repair. The binding of human RPA (hRPA) to DNA involves molecular polarity in which initial hRPA binding occurs on the 5' side of an ssDNA substrate and then extends in the 3' direction to create a stably bound hRPA. RPA is a major damage-recognition protein involved in the early stages of nucleotide excision repair. It can also play a role in telomere maintenance. The RPA 70 kDa subunit binds to ssDNA and mediates interactions with many cellular and viral proteins. The DNA binding domain lies in the middle of RPA 70 kDa subunit and comprises two structurally homologous subdomains oriented in tandem. RPA contains a conserved four cysteine-type zinc-finger motif, which mediates the transition of RPA-ssDNA interaction to a stable RPA-ssDNA complex in a redox-dependent manner.