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Description: Diphénylamine 99+%, très pur qualité Indicateur, indicateur redox
Numéro de catalogue: ACRO221921000
UOM: 1 * 100 g
Fournisseur: Thermo Fisher Scientific

MSMD


Description: Phenolphthalin ≥98.0% (par HPLC, analyse par titration) indicateur redox
Numéro de catalogue: TCIAP0095-500G
UOM: 1 * 500 g
Fournisseur: TCI


Description: Screen-Well™ REDOX library contains 84 compounds with defined prooxidant or antioxidant activity.
Numéro de catalogue: ENZOBML28350500
UOM: 1 * 1 SET
Fournisseur: ENZO LIFE SCIENCES


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: I5763-5G
UOM: 1 * 5 g
Fournisseur: SIGMA ALDRICH MICROSCOPY


Description: Avec câble de 1 m fixé.
Numéro de catalogue: 662-1787
UOM: 1 * 1 ST
Fournisseur: VWR Collection


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.
Numéro de catalogue: ENZOADISPP8921
UOM: 1 * 1 mg
Fournisseur: ENZO LIFE SCIENCES


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.
Numéro de catalogue: BOSSBS-11277R-A350
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play role in redox homeostasis.
Numéro de catalogue: BOSSBS-7518R-CY7
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Sodium diphénylaminesulfonate-4, pur qualité Indicateur, indicateur redox
Numéro de catalogue: ACRO222220250
UOM: 1 * 25 g
Fournisseur: Thermo Fisher Scientific

MSMD


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.
Numéro de catalogue: BOSSBS-11277R-CY7
UOM: 1 * 100 µl
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.
Numéro de catalogue: BOSSBS-11277R-HRP
UOM: 1 * 100 µl
Fournisseur: Bioss


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.
Numéro de catalogue: CAYM18808-25
UOM: 1 * 25 mg
Fournisseur: Cayman Chemical


Description: Technologie de capteur haute qualité amélioré associée aux éléments électroniques de mesure les plus modernes. Les électrodes sont dotées d'un raccord de connexion qui peut être connecté à un câble IDS ou à un module sans fil.
Numéro de catalogue: 662-1721
UOM: 1 * 1 ST
Fournisseur: WTW


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.
Numéro de catalogue: BOSSBS-11277R-A750
UOM: 1 * 100 µl
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.
Numéro de catalogue: BOSSBS-11277R-A555
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Plays a role as a glutathione (GSH)-dependent antioxidant. May be involved in a redox-related process. May play a role in the myopathies of selenium deficiency.
Numéro de catalogue: BOSSBS-0495R-A680
UOM: 1 * 100 µl
Fournisseur: Bioss


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