Votre recherche pour: \\\\u00C9lectrodes+redox

Fournisseur: Thermo Fisher Scientific

Description: Diphénylamine 99+%, très pur qualité Indicateur, indicateur redox

MSMD

Numéro de catalogue: (87702.180)

Fournisseur: VWR Chemicals

Description: Ferroïne (Phénanthroline-1,10-fer(II) sulfate) 0.025 mol/l en solution aqueuse Reag. Ph. Eur. 1038100 indicateur redox

UOM: 1 * 100 mL

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Fournisseur: ENZO LIFE SCIENCES

Description: Screen-Well™ REDOX library contains 84 compounds with defined prooxidant or antioxidant activity.

Fournisseur: SIGMA ALDRICH MICROSCOPY

Description: Indophenol is used in hair dyes, redox materials, lubricants, liquid crystal displays, biosensor and fuel cells. It is toxic to fishes and is implicated in environmental pollution. Indophenol method is common for the determination of ammonia. The reaction gives a blue product, which is measured spectrophotometrically.

Numéro de catalogue: (BOSSBS-11277R-A350)

Fournisseur: Bioss

Description: DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-7518R-CY7)

Fournisseur: Bioss

Description: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play role in redox homeostasis.

UOM: 1 * 100 µl

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Numéro de catalogue: (ENZOADISPP8921)

Fournisseur: ENZO LIFE SCIENCES

Description: Thioredoxin (Trx) is a redox protein of approximately 12 kDa. Its primary domain is conserved across a number of Trx family members and contains a conserved catalytic site Cys-Gly-Pro-Cys. It is ubiquitous and found in many organisms from bacteria to mammals. Trx has been shown to function in cell proliferation, redox signaling and inhibition of apoptosis.

UOM: 1 * 1 mg

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Numéro de catalogue: (662-1787)

Fournisseur: VWR Collection

Description: Avec câble de 1 m fixé.

UOM: 1 * 1 ST

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Fournisseur: Cayman Chemical

Description: MitoPQ is comprised of a triphenylphosphonium lipophilic cation conjugated to the redox cycler paraquat. Driven by membrane potential, it accumulates selectively in the mitochondrial matrix where it produces superoxide by redox cycling at the flavin site of complex I. Thus, MitoPQ selectively increases superoxide production within mitochondria and can be used as a tool either in cells or in vivo to investigate the role of mitochondrial superoxide in pathology and redox signaling.

Fournisseur: Thermo Fisher Scientific

Description: Sodium diphénylaminesulfonate-4, pur qualité Indicateur, indicateur redox

MSMD

Numéro de catalogue: (BOSSBS-11277R-CY7)

Fournisseur: Bioss

Description: DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-11277R-HRP)

Fournisseur: Bioss

Description: DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

UOM: 1 * 100 µl

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Fournisseur: Apollo Scientific

Description: Redox indicator.

Numéro de catalogue: (BOSSBS-11277R-A750)

Fournisseur: Bioss

Description: DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen Signalling.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-11277R-A555)

Fournisseur: Bioss

Description: DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-1874R-A680)

Fournisseur: Bioss

Description: Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol.

UOM: 1 * 100 µl

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