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Citations & References (25)
Invitrogen™
BODIPY™ FL Iodoacetamide (BODIPY™ FL C1-IA, N-(4,4-Difluoro-5,7-Dimethyl-4-Bora-3a,4a-Diaza-s-Indacene-3-yl)Methyl)Iodoacetamide)
The thiol-reactive BODIPY™ FL iodoacetamide can be used to create green-fluorescent bioconjugates. The electronically neutral BODIPY™ FL dye has theRead more
| Catalog Number | Quantity |
|---|---|
| D6003 | 5 mg |
Catalog number D6003
Price (USD)
-
Quantity:
5 mg
The thiol-reactive BODIPY™ FL iodoacetamide can be used to create green-fluorescent bioconjugates. The electronically neutral BODIPY™ FL dye has the most fluorescein-like spectra of the green-fluorescent BODIPY™ dyes.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Chemical ReactivityThiol
Label or DyeBODIPY™ FL
Product TypeFL Iodoacetamide
Quantity5 mg
Reactive MoietyAlkyl Halide, Iodoacetamide
Shipping ConditionRoom Temperature
Label TypeBODIPY Dyes
Product LineBODIPY
Unit SizeEach
Contents & Storage
Store in freezer (-5 to -30°C) and protect from light.
Citations & References (25)
Citations & References
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