Los bioconjugados hechos con la eosina-5-maleimida reactiva al tiol pueden usarse como sondas fosforescentes o como fotosensibilizadores. Con su altoMás información
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Número de catálogo
Cantidad
E118
25 mg
Número de catálogo E118
Precio (MXN)
-
Cantidad:
25 mg
Los bioconjugados hechos con la eosina-5-maleimida reactiva al tiol pueden usarse como sondas fosforescentes o como fotosensibilizadores. Con su alto rendimiento cuántico (∼0,57) para la generación de oxígeno singlete, la eosina y sus conjugados pueden utilizarse como fotooxidantes eficaces de diaminobenzidina (DAB) en estudios de microscopía electrónica de alta resolución y en aplicaciones correlacionadas de fluorescencia y microscopía electrónica.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Reactividad químicaTiol
Etiqueta o tinteEosina
Tipo de productoMaleimida
Cantidad25 mg
Fracción reactivaMaleimida
Condiciones de envíoTemperatura ambiente
Tipo de etiquetaColorantes clásicos
Unit SizeEach
Contenido y almacenamiento
Almacenar en el congelador (de – 5 a – 30 °C) y proteger de la luz.
Citations & References (132)
Citations & References
Abstract
Oligomeric state of human erythrocyte band 3 measured by fluorescence resonance energy homotransfer.
Authors:Blackman SM, Piston DW, Beth AH
Journal:Biophys J
PubMed ID:9675213
The oligomeric state of the erythrocyte anion exchange protein, band 3, has been assayed by resonance energy homotransfer. Homotransfer between oligomeric subunits, labeled with eosin-5-maleimide at Lys430 in the transmembrane domain, has been demonstrated by steady-state and time-resolved fluorescence spectroscopy, and is readily observed by its depolarization of the eosin ... More
Spectroscopic and kinetic characterization of eosin-5-maleimide.
Authors:Schopfer LM, Salhany JM
Journal:Anal Biochem
PubMed ID:9514795
Eosin-5-maleimide (EM) is an increasingly important and widely used probe in the study of membrane protein structure and function. Yet little is known about its spectral properties in hydrophobic and hydrophilic environments. Furthermore, EM is hydrolyzed faster than the traditional N-ethylmaleimide. To offer a more solid foundation for the use ... More
Transfer of band 3, the erythrocyte anion transporter, between phospholipid vesicles and cells.
Authors:Newton AC, Cook SL, Huestis WH
Journal:Biochemistry
PubMed ID:6661430
Band 3, the anion transport protein of human erythrocyte membranes, can be transferred from cells to liposomes and from liposomes back to cell membranes, retaining function and native orientation. After incubation with cells, sonicated phosphatidylcholine vesicles bind a transmembrane protein that comigrates with band 3 on sodium dodecyl sulfate-polyacrylamide gels. ... More
Structural and functional characterization of band 3 from Southeast Asian ovalocytes.
Authors:Moriyama R, Ideguchi H, Lombardo CR, Van Dort HM, Low PS
Journal:J Biol Chem
PubMed ID:1464593
'To determine why deletion of the nine amino acids joining the membrane and cytoplasmic domains of band 3 from Southeast Asian ovalocytes (SAO) renders the erythrocytes rigid, we compared the structural and functional properties of SAO and normal band 3. Calorimetric data, inhibitor binding studies, and anion transport assays all ... More
Loss of rotational mobility of band 3 proteins in human erythrocyte membranes induced by antibodies to glycophorin A.
Authors:Che A, Cherry RJ
Journal:Biophys J
PubMed ID:7612830
'The effect of antibodies to glycophorin A on the rotational diffusion of band 3 in human erythrocyte membranes was investigated by transient dichrosim. Three antibodies that recognize different epitopes on the exofacial domain of glycophorin A all strongly reduce the rotational mobility of band 3. The effect is at most ... More