Votre recherche pour: \\u00C9lectrodes+redox

Numéro de catalogue: (T3134-25G)

Fournisseur: SIGMA ALDRICH MICROSCOPY

Description: N,N,N′,N′-Tetramethyl-p-phenylenediamine dihydrochloride (TMPD) is a redox mediator used in the oxidase test for detecting bacterial cytochrome c oxidases. TMPD is commonly used to perform the oxidase test for the colorimetric identification of pathogenic and non-pathogenic bacteria.

UOM: 1 * 25 g

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Numéro de catalogue: (BOSSBS-11439R-A750)

Fournisseur: Bioss

Description: May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H₂O₂ generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H₂O₂ generation.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-11439R-A488)

Fournisseur: Bioss

Description: May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H(2)O(2) generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H(2)O(2) generation.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-6845R-HRP)

Fournisseur: Bioss

Description: Calcium-dependent NADPH oxidase that generates superoxide. Also functions as a calcium-dependent proton channel and may regulate redox-dependent processes in lymphocytes and spermatozoa. May play a role in cell growth and apoptosis.

UOM: 1 * 100 µl

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Fournisseur: SELENOZYME

Description: The TrxR enzyme in C. elegans is the single selenoprotein in this organism, exerting a wide range of functions in redox control and for antioxidant systems. It is also together with glutathione reductase essential for the molting process.
We provide the main isoform of the C. elegans TrxR enzyme with more than 90% Sec contents and more than 95% purity in aliquots at amounts from 5 to 50 units.

Fournisseur: Cole-Parmer

Description: 200 mV redox standard

Numéro de catalogue: (BOSSBS-5150R-A680)

Fournisseur: Bioss

Description: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs).

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5150R-FITC)

Fournisseur: Bioss

Description: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs).

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-4256R-A488)

Fournisseur: Bioss

Description: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-4256R-A750)

Fournisseur: Bioss

Description: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centres can be oxidised to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidised Trx is catalysed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

UOM: 1 * 100 µl

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Fournisseur: Thermo Fisher Scientific

Description: Disodium terephthalate and its various derivatives are synthesized via simple acid-base chemistry for anode materials in Na ion batteries. They show excellent electrochemical performance, including little capacity fading over 90 cycles, ideal redox potential, and excellent rate performance, making them promising candidates for Na ion batteries.

MSMD Certificats

Fournisseur: VWR Collection

Description: Instruments simples et compacts conçus pour délivrer des résultats rapides et précis dans un format de type stylo économique. Idéaux pour l'agriculture, l'apprentissage, le lavage des fruits et légumes, les piscines, les eaux usées, le blanchiment de la pâte et l'aquaculture.

Numéro de catalogue: (BOSSBS-4256R-CY5.5)

Fournisseur: Bioss

Description: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-4256R-CY7)

Fournisseur: Bioss

Description: Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-3875R-A647)

Fournisseur: Bioss

Description: Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-3875R-HRP)

Fournisseur: Bioss

Description: Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).

UOM: 1 * 100 µl

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