Phalloidin Labeling Probes
Phalloidin Labeling Probes
Citas y referencias (25)
Invitrogen™

Phalloidin Labeling Probes

Achieve precise and reliable F-actin staining with fluorescent and biotinylated phalloidins. Phalloidin conjugates are widely used in imaging applications to selectively label F-actin in a variety of sample types including fixed and permeabilized cells, tissue sections, and cell-free experiments.
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Número de catálogoColorIntervalo de longitud de onda de excitaciónTipo de colorante
A22281Azul346⁄442Alexa Fluor™ 350
A30104Violeta405/450Alexa Fluor™ Plus 405
A12379Verde495⁄518Alexa Fluor™ 488
F432Verde496⁄516FITC (fluoresceína)
R415Rojo anaranjado540⁄565TRITC (isotiocianato de tetrametilrodamina)
A22283Naranja556⁄570Alexa Fluor™ 546
A34055Naranja555⁄565Alexa Fluor™ 555
A30106Naranja555/565 nmAlexa Fluor Plus 555
B3475Rojo558⁄569BODIPY™
A12380Rojo anaranjado578⁄600Alexa Fluor™ 568
A12381Rojo581⁄609Alexa Fluor™ 594
T7471Rojo591⁄608Texas Red™
A22284Rojo lejano632⁄647Alexa Fluor™ 633
A34054Rojo lejano633⁄647Alexa Fluor™ 635
A22287Rojo lejano650⁄668Alexa Fluor™ 647
A30107Rojo lejano650/668 nmAlexa Fluor Plus 647
A22286Infrarrojo cercano679⁄702Alexa Fluor™ 680
A30105Infrarrojo cercano758/784Alexa Fluor™ Plus 750
P3457NingunoNingunoFaloidina (sin marcar)
Número de catálogo A22281
Precio (USD)
1.013,10
Each
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Color:
Azul
Intervalo de longitud de onda de excitación:
346⁄442
Tipo de colorante:
Alexa Fluor™ 350
Precio (USD)
1.013,10
Each
Añadir al carro de la compra
Fluorescent and biotinylated phalloidins are water soluble and bind to filamentous actin (F-actin) with nanomolar affinity, making them convenient probes for labeling, identifying, and quantifying F-actin in cryopreserved tissue sections, fixed and permeabilized cells, and cell-free experiments. Phalloidin conjugates bind similarly to actin from various species, including plants and animals, enabling staining of the cytoskeleton in a wide range of samples.

A variety of phalloidin conjugates for filamentous (F-actin) staining are available, including fluorescent Alexa Fluor and Alexa Fluor Plus phalloidins, along with phalloidins conjugated to classic fluorescent dyes such as BODIPY, fluorescein, and rhodamine. Phalloidin staining is spectrally compatible with other fluorescent stains used in cellular analyses such as GFP/RFP, Qdot nanocrystals, and other Alexa Fluor conjugates and antibodies. Biotin‐XX Phalloidin can be used to visualize actin filaments via fluorescent streptavidin tags or standard enzyme-mediated avidin/streptavidin techniques such as in electron microscopy. Unlabeled phalloidin is available for use as a control in blocking F‐actin staining or in promoting polymerization.

Phalloidin conjugates bind to both large and small actin filaments with similar affinity in a 1:1 stoichiometry between phallotoxin and actin subunits. They do not bind G-actin monomers.

Alexa Fluor and Alexa Fluor Plus phalloidin conjugates for F-actin staining

Fluorescent Alexa Fluor dye conjugates of phalloidin are popular F-actin stains, offering color choices across the full spectral range. These phalloidin conjugates provide researchers with fluorescent probes that are superior in brightness and photostability compared to other spectrally similar conjugates.

Alexa Fluor Plus Phalloidin conjugates retain the same specificity for actin but offer 3-5 times greater sensitivity and brightness compared to the corresponding Alexa Fluor Phalloidin conjugate. This increased brightness is beneficial for challenging F-actin imaging, such as the super‐resolution microscopy methods SIM and STORM, and for reliable staining of actin stress fibers.

Features of phalloidin probes

  • High specificity—binds selectively to F-actin, which allows for precise labeling of actin filaments in fixed cells and cryopreserved tissues
  • Strong affinity—nanomolar binding affinity for F-actin, which ensures stable and reliable actin staining
  • Extensive fluorescent conjugate options—over twenty conjugated varieties of phalloidin
  • Compatibility with fixed samples—typically used with fixed cells and tissues, making them suitable for actin staining in detailed structural studies, immunofluorescence staining, and IHC applications
  • Multiplexing capability—the wide availability of phalloidin conjugates enables their use in combination with other fluorescent probes and antibodies for multiplex imaging. Biotinylated phalloidin can be made use of in downstream streptavidin steps.
  • Quantitative analysis—can be used for quantitative analysis of F-actin distribution and density within cells, aiding in the study of cytoskeletal dynamics. The unlabeled phalloidin can be titrated as a control.
  • Ease of use—staining is straightforward and quick
  • Excellent stability—exhibit good photostability, which is essential for prolonged imaging sessions and time-lapse studies
  • Wide applicability—used for a range of applications, including studying cell morphology, motility, and the effects of drugs on the actin cytoskeleton

Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.

Especificaciones
ColorAzul
Tipo de coloranteAlexa Fluor™ 350
Intervalo de longitud de onda de excitación346⁄442
Para utilizar con (equipo)Fluorescence Microscope, Flow Cytometer, Confocal Microscope, Compatible with DAPI filter set
Línea de productosAlexa Fluor
Cantidad300 Units
Condiciones de envíoTemperatura ambiente
Tipo de etiquetaColorantes Alexa Fluor
Tipo de productoFaloidina
SubCellular LocalizationActina, citoesqueleto, Cytoskeleton
Unit SizeEach
Contenido y almacenamiento
Almacenar en el congelador de -5 °C a -30 °C y proteger de la luz.

Preguntas frecuentes

Can I combine Click-iT or Click-iT Plus reactions with phalloidin conjugates used for actin staining?

We do not recommend using phalloidin conjugates for staining actin in combination with traditional Click-iT or Click-iT Plus reactions since phalloidin is extremely sensitive to the presence of copper.

For staining actin in combination with traditional Click-iT or Click-iT Plus reactions, we recommend using anti-α-actin antibodies for staining actin in the cytoskeleton. You can find a list of our actin antibodies here.

Another option would be to use the Click-iT Plus Alexa Fluor Picolyl Azide Toolkit (Cat. Nos. C10641, C10642, C10643). These Click-iT Plus toolkits provide Copper and Copper protectant separately which makes it easier to titrate the copper concentration to obtain optimal labeling with minimal copper-mediated damage. You may need to optimize the click reaction with the lowest possible concentration of copper and then perform the phalloidin staining.

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

I'm trying to label my paraffin sections for F-actin with a phalloidin conjugate, but I'm not seeing any signal. Why?

When cells and tissues are treated with solvents such as xylene or acetone (for example during deparaffinization of tissue sections), it affects the F-actin in a way that prevents phalloidins from binding. Phalloidin may be used with cryosections, which are not typically washed with organic solvents, or anti-actin antibodies may be used.

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

Citations & References (25)

Citations & References
Abstract
Grp1-associated scaffold protein (GRASP) is a regulator of the ADP ribosylation factor 6 (Arf6)-dependent membrane trafficking pathway.
Authors:Venkataraman A, Nevrivy DJ, Filtz TM, Leid M,
Journal:Cell Biol Int
PubMed ID:22931251
GRASP interacts with Grp1 (general receptor for phosphoinositides 1; cytohesin 3), which catalyses nucleotide exchange on and activation of Arf6 (ADP-ribosylation factor-6). Arf6 is a low-molecular-mass GTPase that regulates key aspects of endocytic recycling pathways. Overexpressed GRASP accumulated in the juxtanuclear ERC (endocytic recycling compartment). GRASP co-localized with a constitutively ... More
A small-molecule approach to studying invasive mechanisms of Toxoplasma gondii.
Authors:Carey KL, Westwood NJ, Mitchison TJ, Ward GE
Journal:Proc Natl Acad Sci U S A
PubMed ID:15123807
'Toxoplasma gondii is the most common protozoan parasite of humans. Infection with T. gondii can lead to life-threatening disease as a result of repeated cycles of host cell invasion, parasite replication, and host cell lysis. Relatively little is known about the invasive mechanisms of T. gondii and related parasites within ... More
Polar localization of virulence-related Esx-1 secretion in mycobacteria.
Authors:Carlsson F, Joshi SA, Rangell L, Brown EJ,
Journal:PLoS Pathog
PubMed ID:19180234
'The Esx-1 (type VII) secretion system is critical for virulence of both Mycobacterium tuberculosis and Mycobacterium marinum, and is highly conserved between the two species. Despite its importance, there has been no direct visualization of Esx-1 secretion until now. In M. marinum, we show that secretion of Mh3864, a novel ... More
Focal adhesion size controls tension-dependent recruitment of alpha-smooth muscle actin to stress fibers.
Authors:Goffin JM, Pittet P, Csucs G, Lussi JW, Meister JJ, Hinz B
Journal:J Cell Biol
PubMed ID:16401722
'Expression of alpha-smooth muscle actin (alpha-SMA) renders fibroblasts highly contractile and hallmarks myofibroblast differentiation. We identify alpha-SMA as a mechanosensitive protein that is recruited to stress fibers under high tension. Generation of this threshold tension requires the anchoring of stress fibers at sites of 8-30-microm-long "supermature" focal adhesions (suFAs), which ... More
Restriction of receptor movement alters cellular response: physical force sensing by EphA2.
Authors:Salaita K, Nair PM, Petit RS, Neve RM, Das D, Gray JW, Groves JT,
Journal:Science
PubMed ID:20223987
'Activation of the EphA2 receptor tyrosine kinase by ephrin-A1 ligands presented on apposed cell surfaces plays important roles in development and exhibits poorly understood functional alterations in cancer. We reconstituted this intermembrane signaling geometry between live EphA2-expressing human breast cancer cells and supported membranes displaying laterally mobile ephrin-A1. Receptor-ligand binding, ... More
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