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Numéro de catalogue: (AATB22280)
Fournisseur: AAT BIOQUEST
Description: 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.
UOM: 1 * 500 Tests


Numéro de catalogue: (BOSSBS-1476R-CY5)
Fournisseur: Bioss
Description: 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).
UOM: 1 * 100 µl


Fournisseur: Hach
Description: 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.

Fournisseur: Honeywell Chemicals
Description: Ferroïne (Phénanthroline-1,10-fer(II) sulfate) solution Reag. Ph. Eur. indicateur redox E0 (H2SO4 1 mol/l) = +1,06 volt, Fluka™

Numéro de catalogue: (AATB5529)
Fournisseur: AAT BIOQUEST
Description: Protein thiols are very important to protein structure, protein function and biological system redox environment.
UOM: 1 * 2 Tests


Numéro de catalogue: (AATB11306)
Fournisseur: AAT BIOQUEST
Description: Catalase is a common antioxidant heme-containing redox enzyme found in nearly all living organisms that are exposed to oxygen.
UOM: 1 * 200 Tests


Numéro de catalogue: (AATB15700)
Fournisseur: AAT BIOQUEST
Description: 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.
UOM: 1 * 100 mg


Fournisseur: Honeywell Chemicals
Description: Ferroïne (Phénanthroline-1,10-fer(II) sulfate) 0.025 M en solution aqueuse indicateur redox, Fluka™
Fournisseur: WTW
Description: Cet instrument à deux canaux est idéal pour effectuer des mesures précises de pH, ISE ou d'oxydoréduction, et pour générer automatiquement des données conformes aux BPL/AQA, requises par les laboratoires accrédités. Les mesures haute résolution peuvent être contrôlées facilement grâce à l'interface utilisateur graphique.

Numéro de catalogue: (PRSI30-467)
Fournisseur: ProSci Inc.
Description: 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]).
UOM: 1 * 1 EA


Numéro de catalogue: (BOSSBS-11233R-CY5)
Fournisseur: Bioss
Description: 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.
UOM: 1 * 100 µl


Numéro de catalogue: (CMPLZ15321110.1L)
Fournisseur: CUSTOM MADE CHEMICALS LAB
Description: 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.
UOM: 1 * 1 L


Numéro de catalogue: (BOSSBS-1476R-HRP)
Fournisseur: Bioss
Description: 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).
UOM: 1 * 100 µl


Fournisseur: Mettler - Toledo
Description: Électrode, pH, LE series, Électrode d'oxydoréduction LE501, rechargeable, pH: -, 0...+80 °C, Verre, Membrane: Ceramic, Électrolyte: KCl 3 mol/l, Ø×L: 12×120 mm, BNC, câble d'un mètre, Pour: Solutions chargées, traitements de l'eau

Numéro de catalogue: (BOSSBS-11233R-CY3)
Fournisseur: Bioss
Description: 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.
UOM: 1 * 100 µl


Fournisseur: MP Biomedicals
Description: Safranine O is a redox and adsorption indicator.

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