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 do catálogoColorExcitation Wavelength RangeDye Type
A22281Blue346/442 nmAlexa Fluor™ 350
A30104Violet405/450 nmAlexa Fluor™ Plus 405
A12379Green495/518 nmAlexa Fluor™ 488
O7466Green496/520 nmOregon Green™ 488
F432Green496/516 nmFITC (Fluorescein)
A22282Yellow531/554 nmAlexa Fluor™ 532
R415Red-orange540/565 nmTRITC
A22283Orange556/570 nmAlexa Fluor™ 546
A34055Orange555/565 nmAlexa Fluor™ 555
A30106Orange555/565 nmAlexa Fluor Plus 555
B3475Red558/569 nmBODIPY™
A12380Orange-red578/600 nmAlexa Fluor™ 568
A12381Red581/609 nmAlexa Fluor™ 594
T7471Red591/608 nmTexas Red™
A22284Far-red632/647 nmAlexa Fluor™ 633
A34054Far-red633/647 nmAlexa Fluor™ 635
A22287Far-red650/668 nmAlexa Fluor™ 647
A30107Far-red650/668 nmAlexa Fluor Plus 647
A22285Near-infrared663/690 nmAlexa Fluor™ 660
A22286Near-infrared679/702 nmAlexa Fluor™ 680
A30105Near-infrared758/784 nmAlexa Fluor™ Plus 750
B7474NoneNoneBiotin-XX
P3457NoneNonePhalloidin (unlabeled)
Número do catálogo A22281
Preço (BRL)
5.020,01
Each
Color:
Blue
Excitation Wavelength Range:
346/442 nm
Dye Type:
Alexa Fluor™ 350
Preço (BRL)
5.020,01
Each
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
For Research Use Only. Not for use in diagnostic procedures.
Especificações
ColorBlue
Dye TypeAlexa Fluor™ 350
Excitation Wavelength Range346/442 nm
For Use With (Equipment)Fluorescence Microscope, Flow Cytometer, Confocal Microscope, Compatible with DAPI filter set
Product LineAlexa Fluor
Quantity300 Units
Shipping ConditionRoom Temperature
Label TypeAlexa Fluor Dyes
Product TypePhalloidin
Sub Cellular LocalizationActin, Cytoskeleton
Unit SizeEach
Conteúdo e armazenamento
Store in freezer -5°C to -30°C and protect from light.

Frequently asked questions (FAQs)

Do you offer alternative package sizes for phalloidin or ReadyProbes reagents?

Alternative package sizes may be available through a custom request process. Contact Thermo Fisher Scientific customer support or your sales representative to discuss available options for the specific reagent and quantity needed.

Can I use conjugated phalloidin label probes on organoids?

Yes. Conjugated phalloidin labeling probes can be used with organoids when F-actin is accessible after fixation and permeabilization. Because organoids are thicker than monolayer cell cultures, protocol optimization may be needed, including permeabilization conditions, probe incubation time, and probe concentration.

Are conjugated phalloidin reagents antibodies?

No, Phalloidin is not an antibody. It is a bicyclic peptide toxin originally isolated from the Amanita phalloides mushroom and is used to bind and label F-actin in fixed and permeabilized samples.

Can I use methanol instead of DMSO to reconstitute the conjugated phalloidins from the lyophilized solids?

Yes, methanol can be used to reconstitute fluorescent phalloidin, but it creates a less concentrated stock solution than DMSO. Dissolve the vial contents in 1.5 mL of methanol to yield a 40X stock solution at a concentration of 200 assays/mL, which is equivalent to approximately 6.6 µM. One unit/assay of fluorescent phalloidins is equivalent to 5 µL of the methanolic stock solution. Methanol may be used as a stock-solution solvent, but methanol-containing fixatives are not recommended because they can disrupt F-actin.

How do I reconstitute fluorescent conjugated phalloidin probes to make a stock solution?

For fluorescent phalloidin label probes, prepare a DMSO stock solution by dissolving the vial contents in 150 µL anhydrous DMSO to make a 400X stock, with a concentration of approximately 66 µM or 2,000 assays per mL. Store between -25°C and -5°C, protected from light. One unit/assay of fluorescent phalloidins is equivalent to 0.5 µL of the DMSO stock solution.

Citações e referências (25)

Citações e referências
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