Colorant FM™ 4-64 (dibromure de N-(3-triéthylammoniumpropyl)-4-(6-(4-(diéthylamino) phényl) hexatriényl) pyridinium)
Colorant FM&trade; 4-64 (dibromure de <i>N</i>-(3-triéthylammoniumpropyl)-4-(6-(4-(diéthylamino) phényl) hexatriényl) pyridinium)
Citations et références (329)
Invitrogen™

Colorant FM™ 4-64 (dibromure de N-(3-triéthylammoniumpropyl)-4-(6-(4-(diéthylamino) phényl) hexatriényl) pyridinium)

D’après les expériences, le colorant styryle FM 4-64 colore sélectivement les membranes vacuolaires d’une fluorescence rouge (maxima d’excitation / émissionAfficher plus
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RéférenceQuantité
T31661mg
T1332010 x 100 μg
Référence T3166
Prix (EUR)
578,68
Special offer
Online exclusive
termine: 15-Feb-2026
808,00
Économisez 229,32 (28%)
1 mg
Ajouter au panier
Quantité:
1mg
Prix (EUR)
578,68
Special offer
Online exclusive
termine: 15-Feb-2026
808,00
Économisez 229,32 (28%)
1 mg
Ajouter au panier
D’après les expériences, le colorant styryle FM 4-64 colore sélectivement les membranes vacuolaires d’une fluorescence rouge (maxima d’excitation / émission de ∼ 515 / 640 nm). Ce colorant lipophile est un outil important pour la visualisation de la morphologie et de la dynamique des organites vacuolaires, pour l’étude de la voie endocytaire et pour l’analyse et la caractérisation des mutants de l’endocytose de levure. Le colorant FM 4-64 est également disponible dans un emballage spécial avec 10 flacons de 100 μg chacun (T-13320).
Usage exclusivement réservé à la recherche. Ne pas utiliser pour des procédures de diagnostic.
Spécifications
CouleurRouge
Méthode de détectionFluorescence
À utiliser avec (équipement)Microscope à fluorescence
Gamme de produitsFM
Quantité1mg
Conditions d’expéditionTempérature ambiante
Type d’étiquetteFluorescent Dye
Type de produitColorant
SubCellular LocalizationMembrane plasmique
Unit Size1 mg
Contenu et stockage
Stocker à température ambiante et à l'abri de lalumière.

Foire aux questions (FAQ)

I want to study endosomes trafficking using FM 4-64. Will the label be retained after fixation? And can I label already-fixed cells?

No. For that you would need the FM 4-64FX version. The non-FX version will not be retained upon fixation, leading to loss of much of the stain and an increase in background. The FX version will be retained using an aldehyde-based fixative. Cells that are already fixed will be stained throughout the cell and the signal will not be localized; it is recommended to stain live cells and then fix.

Find additional tips, troubleshooting help, and resources within our Cell Analysis Support Center.

I want to study endosome trafficking using FM 4-64 dye. Will the label be retained after fixation? And can I label cells that have already been fixed?

No. For that, you would need the FM 4-64FX version. The non-FX version will be lost, leading to loss of much of the specific label and a vast increase in background labeling. The FX version will be fixed in place with formaldehyde. Cells that have been fixed already will not label correctly, so you will need to label the cells live and then fix.

Find additional tips, troubleshooting help, and resources within our Cell Analysis Support Center.

Citations et références (329)

Citations et références
Abstract
Apg9p/Cvt7p is an integral membrane protein required for transport vesicle formation in the Cvt and autophagy pathways.
Authors:Noda T,Kim J,Huang WP,Baba M,Tokunaga C,Ohsumi Y,Klionsky DJ
Journal:The Journal of cell biology
PubMed ID:10662773
In nutrient-rich, vegetative conditions, the yeast Saccharomyces cerevisiae transports a resident protease, aminopeptidase I (API), to the vacuole by the cytoplasm to vacuole targeting (Cvt) pathway, thus contributing to the degradative capacity of this organelle. When cells subsequently encounter starvation conditions, the machinery that recruited precursor API (prAPI) also sequesters ... More
Glutamate induces the rapid formation of spine head protrusions in hippocampal slice cultures.
Authors:Richards DA,Mateos JM,Hugel S,de Paola V,Caroni P,Gähwiler BH,McKinney RA
Journal:Proceedings of the National Academy of Sciences of the United States of America
PubMed ID:15831587
Synaptic plasticity at neuronal connections has been well characterized functionally by using electrophysiological approaches, but the structural basis for this phenomenon remains controversial. We have studied the dynamic interactions between presynaptic and postsynaptic structures labeled with FM 4-64 and a membrane-targeted GFP, respectively, in hippocampal slices. Under conditions of reduced ... More
Fab1p is essential for PtdIns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis.
Authors:Gary JD,Wurmser AE,Bonangelino CJ,Weisman LS,Emr SD
Journal:The Journal of cell biology
PubMed ID:9763421
The Saccharomyces cerevisiae FAB1 gene encodes a 257-kD protein that contains a cysteine-rich RING-FYVE domain at its NH2-terminus and a kinase domain at its COOH terminus. Based on its sequence, Fab1p was initially proposed to function as a phosphatidylinositol 4-phosphate (PtdIns(4)P) 5-kinase (). Additional sequence analysis of the Fab1p kinase ... More
Slow spontaneous secretion from single large dense-core vesicles monitored in neuroendocrine cells.
Authors:Stenovec M, Kreft M, Poberaj I, Betz WJ, Zorec R
Journal:FASEB J
PubMed ID:15180959
Hormones are released from cells by passing through an exocytotic pore that forms after vesicle and plasma membrane fusion. In stimulated exocytosis vesicle content is discharged swiftly. Although rapid vesicle discharge has also been proposed to mediate basal secretion, this has not been studied directly. We investigated basal hormone release ... More
Traffic-independent function of the Sar1p/COPII machinery in proteasomal sorting of the cystic fibrosis transmembrane conductance regulator.
Authors:Fu L, Sztul E
Journal:J Cell Biol
PubMed ID:12538638
'Newly synthesized proteins that do not fold correctly in the ER are targeted for ER-associated protein degradation (ERAD) through distinct sorting mechanisms; soluble ERAD substrates require ER-Golgi transport and retrieval for degradation, whereas transmembrane ERAD substrates are retained in the ER. Retained transmembrane proteins are often sequestered into specialized ER ... More
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