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Citas y referencias (315)
Invitrogen™
Rodamina B Lissamine™ 1,2-dihexadecanoil-sn-glicero-3-fosfoetanolamina, sal de trietilamonio (rodamina DHPE)
El fosfolípido, rodamina DHPE se etiqueta en el grupo funcional con el fluoróforo rojo-fluorescente de la rodamina B con unosMás información
| Número de catálogo | Cantidad |
|---|---|
| L1392 | 5 mg |
Número de catálogo L1392
Precio (MXN)
-
Cantidad:
5 mg
El fosfolípido, rodamina DHPE se etiqueta en el grupo funcional con el fluoróforo rojo-fluorescente de la rodamina B con unos niveles máximos de excitación/emisión de ∼560/580 nm.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Almacenamiento recomendadoAlmacenar en el congelador (de – 5 a – 30 °C) y proteger de la luz.
Forma físicaSolid
Línea de productosLissamine
Cantidad5 mg
Unit SizeEach
Citations & References (315)
Citations & References
Abstract
Journal:
PubMed ID:18198177
Poly(aspartic acid)-dependent fusion of liposomes bearing the quaternary ammonium detergent [[[(1,1,3,3-tetramethylbutyl)cresoxy]ethoxy]ethyl] dimethylbenzylammonium hydroxide.
Journal:Biochemistry
PubMed ID:3349055
Addition of the quaternary ammonium detergent [[[(1,1,3,3-tetramethylbutyl)cresoxy]ethoxy]ethyl] dimethylbenzylammonium hydroxide (DEBDA[OH]) and the fluorescent probes N-(7-nitro-2-1,3-benzoxadiazol-4-yl)phosphatidylethanolamine and N-(lissamine rhodamine B sulfonyl)phosphatidylethanolamine (N-NBD-PE and N-Rh-PE, respectively) to liposomes composed of phosphatidylcholine (PC) and cholesterol (chol) resulted in the formation of fluorescently labeled liposomes bearing DEBDA[OH]. Incubation of the anionic polymer poly(aspartic acid)
Use of resonance energy transfer to study the kinetics of amphiphile transfer between vesicles.
Journal:Biochemistry
PubMed ID:7082641
Topography of the hydrophilic helices of membrane-inserted diphtheria toxin T domain: TH1-TH3 as a hydrophilic tether.
Journal:Biochemistry
PubMed ID:16800637
'After low pH-triggered membrane insertion, the T domain of diphtheria toxin helps translocate the catalytic domain of the toxin across membranes. In this study, the hydrophilic N-terminal helices of the T domain (TH1-TH3) were studied. The conformation triggered by exposure to low pH and changes in topography upon membrane insertion
Immunochemical analysis shows all three domains of diphtheria toxin penetrate across model membranes.
Journal:J Biol Chem
PubMed ID:7499201
'Diphtheria toxin undergoes membrane insertion and translocation across membranes when exposed to low pH. In this study, the translocation of the toxin has been investigated by the binding of antibodies to two preparations of model membrane-inserted toxin. In one preparation, toxin was added externally to model membrane vesicles and then