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Citations & References (132)
Invitrogen™
Eosin-5-Maleimide
Bioconjugates made with the thiol-reactive eosin-5-maleimide can be used as phosphorescent probes or as photosensitizers. With its high quantum yieldRead more
| Catalog Number | Quantity |
|---|---|
| E118 | 25 mg |
Catalog number E118
Price (TWD)
16,380.00
Online offer
Ends: 31-Dec-2025
23,400.00Save 7,020.00 (30%)
Each
Quantity:
25 mg
Price (TWD)
16,380.00
Online offer
Ends: 31-Dec-2025
23,400.00Save 7,020.00 (30%)
Each
Bioconjugates made with the thiol-reactive eosin-5-maleimide can be used as phosphorescent probes or as photosensitizers. With its high quantum yield (∼0.57) for singlet oxygen generation, eosin and its conjugates can be used as effective photooxidizers of diaminobenzidine (DAB) in high-resolution electron microscopy studies and in correlated fluorescence and electron microscopy applications.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Chemical ReactivityThiol
Label or DyeEosin
Product TypeMaleimide
Quantity25 mg
Reactive MoietyMaleimide
Shipping ConditionRoom Temperature
Label TypeClassic Dyes
Unit SizeEach
Contents & Storage
Store in freezer (-5 to -30°C) and protect from light.
Citations & References (132)
Citations & References
Abstract
Oligomeric state of human erythrocyte band 3 measured by fluorescence resonance energy homotransfer.
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
Spectroscopic and kinetic characterization of eosin-5-maleimide.
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
Transfer of band 3, the erythrocyte anion transporter, between phospholipid vesicles and cells.
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.
Structural and functional characterization of band 3 from Southeast Asian ovalocytes.
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
Loss of rotational mobility of band 3 proteins in human erythrocyte membranes induced by antibodies to glycophorin A.
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