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引用和文献 (132)
Invitrogen™
曙红-5-马来酰亚胺
通过硫醇反应性曙红-5-马来酰亚胺生成的生物偶联物可用作磷光探针或光敏剂。具有高量子得率 (∼0.57)，适用于单线态氧生成，曙红及其偶联物可作为高分辨率电子显微镜研究和相关荧光和电子显微镜检查应用中二氨基联苯胺 (DAB) 的有效光氧化剂。了解更多信息
| 货号 | 数量 |
|---|---|
| E118 | 25 mg |
货号 E118
价格（CNY)
7,589.00
Each
数量:
25 mg
价格（CNY)
7,589.00
Each
通过硫醇反应性曙红-5-马来酰亚胺生成的生物偶联物可用作磷光探针或光敏剂。具有高量子得率 (∼0.57)，适用于单线态氧生成，曙红及其偶联物可作为高分辨率电子显微镜研究和相关荧光和电子显微镜检查应用中二氨基联苯胺 (DAB) 的有效光氧化剂。
仅供科研使用。不可用于诊断程序。
规格
化学反应性硫醇
标签或染料曙红
产品类型马来酰亚胺
数量25 mg
反应一部分马来酰亚胺
运输条件室温
标签类型经典染料
Unit SizeEach
内容与储存
储存在冰箱(-5 至 -30°C)中并避光。
引用和文献 (132)
引用和文献
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