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Citations & References (130)
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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| Catalog Number | Color | Excitation Wavelength Range | Dye Type |
|---|---|---|---|
| T7471 | Red | 591/608 nm | Texas Red™ |
| A22281 | Blue | 346/442 nm | Alexa Fluor™ 350 |
| A30104 | Violet | 405/450 nm | Alexa Fluor™ Plus 405 |
| A12379 | Green | 495/518 nm | Alexa Fluor™ 488 |
| O7466 | Green | 496/520 nm | Oregon Green™ 488 |
| F432 | Green | 496/516 nm | FITC (Fluorescein) |
| A22282 | Yellow | 531/554 nm | Alexa Fluor™ 532 |
| R415 | Red-orange | 540/565 nm | TRITC |
| A22283 | Orange | 556/570 nm | Alexa Fluor™ 546 |
| A34055 | Orange | 555/565 nm | Alexa Fluor™ 555 |
| A30106 | Orange | 555/565 nm | Alexa Fluor Plus 555 |
| B3475 | Red | 558/569 nm | BODIPY™ |
| A12380 | Orange-red | 578/600 nm | Alexa Fluor™ 568 |
| A12381 | Red | 581/609 nm | Alexa Fluor™ 594 |
| A22284 | Far-red | 632/647 nm | Alexa Fluor™ 633 |
| A34054 | Far-red | 633/647 nm | Alexa Fluor™ 635 |
| A22287 | Far-red | 650/668 nm | Alexa Fluor™ 647 |
| A30107 | Far-red | 650/668 nm | Alexa Fluor Plus 647 |
| A22285 | Near-infrared | 663/690 nm | Alexa Fluor™ 660 |
| A22286 | Near-infrared | 679/702 nm | Alexa Fluor™ 680 |
| A30105 | Near-infrared | 758/784 nm | Alexa Fluor™ Plus 750 |
| B7474 | None | None | Biotin-XX |
| P3457 | None | None | Phalloidin (unlabeled) |
Catalog number T7471
Price (EUR)
803,65
Offre exceptionnelle en ligne
856,00Save 52,35 (6%)
300 units
Color:
Red
Excitation Wavelength Range:
591/608 nm
Dye Type:
Texas Red™
Price (EUR)
803,65
Offre exceptionnelle en ligne
856,00Save 52,35 (6%)
300 units
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.
Specifications
ColorRed
Dye TypeTexas Red™
Excitation Wavelength Range591/608 nm
For Use With (Equipment)Fluorescence Microscope, Flow Cytometer, Confocal Microscope, Compatible with Texas Red filter set
Product LineTexas Red
Quantity300 Units
Shipping ConditionRoom Temperature
Label TypeClassic Dyes
Product TypePhalloidin
SubCellular LocalizationActin, Cytoskeleton
Unit Size300 units
Contents & Storage
Store in freezer -5°C to -30°C and protect from light.
Frequently asked questions (FAQs)
Can I combine Click-iT or Click-iT Plus reactions with phalloidin conjugates used for actin staining?
I'm trying to label my paraffin sections for F-actin with a phalloidin conjugate, but I'm not seeing any signal. Why?
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.
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.
Tyrosine phosphorylation of paxillin alpha is involved in temporospatial regulation of paxillin-containing focal adhesion formation and F-actin organization in motile cells.
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
Signaling complexes of the FERM domain-containing protein GRSP1 bound to ARF exchange factor GRP1.
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
Localized suppression of RhoA activity by Tyr31/118-phosphorylated paxillin in cell adhesion and migration.
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
Transformation activity of Cdc42 requires a region unique to Rho-related proteins.
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