Citations & References (132)

Invitrogen™

Eosin-5-Maleimide

eosin-5-maleimide

Catalog Number	Quantity
E118	25 mg

Catalog number E118

Price (USD)

632.00

Quantity:

25 mg

Price (USD)

632.00

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.

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

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