Phalloidin Labeling Probes
Phalloidin Labeling Probes
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
T7471Rojo591⁄608Texas Red™
A22281Azul346⁄442Alexa Fluor™ 350
A30104Violeta405/450Alexa Fluor™ Plus 405
A12379Verde495⁄518Alexa Fluor™ 488
O7466Verde496⁄520Oregon Green™ 488
F432Verde496⁄516FITC (fluoresceína)
A22282Amarillo531⁄554Alexa Fluor™ 532
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
A22284Rojo lejano632⁄647Alexa Fluor™ 633
A34054Rojo lejano633⁄647Alexa Fluor™ 635
A22287Rojo lejano650⁄668Alexa Fluor™ 647
A30107Rojo lejano650/668 nmAlexa Fluor Plus 647
A22285Infrarrojo cercano663⁄690Alexa Fluor™ 660
A22286Infrarrojo cercano679⁄702Alexa Fluor™ 680
A30105Infrarrojo cercano758/784Alexa Fluor™ Plus 750
B7474NingunoNingunoBiotin-XX
P3457NingunoNingunoFaloidina (sin marcar)
Número de catálogo T7471
Precio (MXN)
-
Color:
Rojo
Intervalo de longitud de onda de excitación:
591⁄608
Tipo de colorante:
Texas Red™
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
ColorRojo
Tipo de coloranteTexas Red™
Intervalo de longitud de onda de excitación591⁄608
Para utilizar con (equipo)Fluorescence Microscope, Flow Cytometer, Confocal Microscope, Compatible with Texas Red filter set
Línea de productosTexas Red
Cantidad300 Units
Condiciones de envíoTemperatura ambiente
Tipo de etiquetaColorantes clásicos
Tipo de productoFaloidina
SubCellular LocalizationActina, citoesqueleto, Cytoskeleton
Unit Size300 units
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 (130)

Citations & References
Abstract
I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure.
Authors:Linke WA, Rudy DE, Centner T, Gautel M, Witt C, Labeit S, Gregorio CC
Journal:J Cell Biol
PubMed ID:10444071
'In cardiac muscle, the giant protein titin exists in different length isoforms expressed in the molecule''s I-band region. Both isoforms, termed N2-A and N2-B, comprise stretches of Ig-like modules separated by the PEVK domain. Central I-band titin also contains isoform-specific Ig-motifs and nonmodular sequences, notably a longer insertion in N2-B. ... More
Tyrosine phosphorylation of paxillin alpha is involved in temporospatial regulation of paxillin-containing focal adhesion formation and F-actin organization in motile cells.
Authors:Nakamura K, Yano H, Uchida H, Hashimoto S, Schaefer E, Sabe H
Journal:J Biol Chem
PubMed ID:10823820
'Temporal and spatial regulation of actin-based cytoskeletal organization and focal adhesion formation play an essential role in cell migration. Here, we show that tyrosine phosphorylation of a focal adhesion protein, paxillin, crucially participates in these regulations. We found that tyrosine phosphorylation of paxillin was a prominent event upon integrin activation ... More
Signaling complexes of the FERM domain-containing protein GRSP1 bound to ARF exchange factor GRP1.
Authors:Klarlund JK, Holik J, Chawla A, Park JG, Buxton J, Czech MP
Journal:J Biol Chem
PubMed ID:11445584
'GRP1 is a member of a family of proteins that contain a coiled-coil region, a Sec7 homology domain with guanosine nucleotide exchange activity for the ARF GTP-binding proteins, and a pleckstrin homology domain at the C terminus. The pleckstrin homology domain of GRP1 binds phosphatidylinositol (3,4,5) trisphosphate and mediates the ... More
Localized suppression of RhoA activity by Tyr31/118-phosphorylated paxillin in cell adhesion and migration.
Authors:Tsubouchi A, Sakakura J, Yagi R, Mazaki Y, Schaefer E, Yano H, Sabe H
Journal:J Cell Biol
PubMed ID:12446743
'RhoA activity is transiently inhibited at the initial phase of integrin engagement, when Cdc42- and/or Rac1-mediated membrane spreading and ruffling predominantly occur. Paxillin, an integrin-assembly protein, has four major tyrosine phosphorylation sites, and the phosphorylation of Tyr31 and Tyr118 correlates with cell adhesion and migration. We found that mutation of ... More
Transformation activity of Cdc42 requires a region unique to Rho-related proteins.
Authors:Wu WJ, Lin R, Cerione RA, Manor D
Journal:J Biol Chem
PubMed ID:9642217
'The Rho subfamily GTP-binding protein Cdc42 mediates actin cytoskeletal rearrangements and cell cycle progression and is essential for Ras transformation. Expression of a Cdc42 mutant (Cdc42(F28L)) that undergoes spontaneous activation (guanine nucleotide exchange) results in transformation of NIH3T3 fibroblasts. In this report, we show that deletion of residues 120-139 from ... More