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引用和文献 (25)
Invitrogen™
BODIPY™ FL 碘乙酰胺（BODIPY™ FL C1-IA，N-(4,4-二氟-5,7-二甲基-4-硼杂-3a,4a-二氮杂-s-引达省-3-丙酸)碘乙酰胺）
硫醇反应性 BODIPY™ FL 碘乙酰胺可用于生成绿色荧光生物偶联物。电子中性 BODIPY™ FL 染料具有绿色荧光 BODIPY™ 染料中极佳荧光素样光谱了解更多信息
| 货号 | 数量 |
|---|---|
| D6003 | 5 mg |
货号 D6003
价格（CNY)
6,775.00
Each
数量:
5 mg
价格（CNY)
6,775.00
Each
硫醇反应性 BODIPY™ FL 碘乙酰胺可用于生成绿色荧光生物偶联物。电子中性 BODIPY™ FL 染料具有绿色荧光 BODIPY™ 染料中极佳荧光素样光谱。
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BODIPY™ FL
产品类型FL 碘乙酰胺
数量5 mg
反应一部分烷基卤化物、碘乙酰胺
运输条件室温
标签类型BODIPY 染料
产品线BODIPY
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 (25)
引用和文献
Abstract
Membrane translocation of charged residues at the tips of hydrophobic helices in the T domain of diphtheria toxin.
Journal:Biochemistry
PubMed ID:9893993
'The low pH triggered membrane insertion of the T domain of diphtheria toxin is a critical step in the translocation of the C domain of the toxin across membranes in vivo. We previously established that the T domain can interact with membranes in two distinct conformations, one in which the
Topography of diphtheria toxin A chain inserted into lipid vesicles.
Journal:Biochemistry
PubMed ID:15697244
'The membrane-inserting T domain of diphtheria toxin aids the low-pH-triggered translocation of the catalytic A chain of the toxin across endosomal membranes. To evaluate the role of the isolated A chain in translocation, the topography of isolated A chain inserted into model membrane vesicles was investigated using a mixture either
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
Cellular uptake of aminoglycosides, guanidinoglycosides, and poly-arginine.
Journal:J Am Chem Soc
PubMed ID:14531657
The use of site-directed fluorophore labeling and donor-donor energy migration to investigate solution structure and dynamics in proteins.
Journal:Proc Natl Acad Sci U S A
PubMed ID:10535947
'The use of molecular genetics for introducing fluorescent molecules enables the use of donor-donor energy migration to determine intramolecular distances in a variety of proteins. This approach can be applied to examine the overall molecular dimensions of proteins and to investigate structural changes upon interactions with specific target molecules. In