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| Product Name | Fluor 532 Phalloidin |
| Catalog No. | RESK-0575 |
| Description | Fluor 532 Phalloidin is a conjugate of phalloidin and the Fluor 532 fluorophore that emits bright, photostable orange fluorescence (Ex/Em 543/563 nm). Phalloidin is a cyclic heptapeptide toxin derived from the death cap mushroom Amanita phalloides. It binds filamentous actin (F-actin) selectively with high affinity (Kd = 20 nM) and does not bind monomeric actin (G-actin), making it a standard probe for labeling F-actin in tissue sections, cell cultures, and cell-free systems for qualitative and quantitative analysis. Phalloidin derivatives bind large and small actin filaments with similar affinity in muscle and non-muscle cells of both animal and plant origin, at a stoichiometry of approximately one phalloidin molecule per actin subunit. Nonspecific binding is negligible, providing excellent contrast between stained and unstained regions, so phalloidin conjugates are an ideal alternative to actin antibodies. Phalloidin derivatives are very small (approximately 12-15 Å in diameter, molecular weight |
| Intended Use | For qualitative and quantitative detection of F-actin (filamentous actin) in tissue sections, cell cultures, and cell-free systems. For research use only. |
| Principle / Technology | Phalloidin is a cyclic heptapeptide toxin from Amanita phalloides that selectively binds F-actin with high affinity (Kd = 20 nM) at approximately one phalloidin molecule per actin subunit, without binding monomeric G-actin. Binding stabilizes microfilaments by preventing depolymerization, disrupting the polymerization-depolymerization equilibrium and lowering the critical concentration of actin polymerization to <1 μg/mL; it also inhibits the ATP hydrolysis activity of F-actin. Covalent conjugation to the Fluor 532 fluorophore converts this selective binding into a bright, photostable orange fluorescent signal for cytoskeletal visualization. |
| Detection Method | Fluorescence detection (fluorescence microscopy / fluorescence imaging); excitation/emission maxima 543/563 nm (orange fluorescence). |
| Sample Type | Tissue sections, cell cultures, and cell-free preparations; suitable for muscle and non-muscle cells of animal and plant origin (no species dependence). |
| Performance Range / Specifications | Molecular weight: ~1800 Da Excitation/emission maxima (Ex/Em): 543/563 nm Solubility: soluble in DMSO Supplied at 1 mg/mL; 300 T size (30 μL per vial). |
| Specificity | Selectively binds filamentous actin (F-actin) with high affinity (Kd = 20 nM); does not bind monomeric actin (G-actin). Binds large and small filaments with similar affinity at a stoichiometry of approximately one phalloidin molecule per actin subunit. Nonspecific binding is negligible, giving clearly defined stained and unstained regions. Binding shows no species dependence. |
| Components / Formulation | Fluor 532 Phalloidin supplied as a stock solution at 1 mg/mL in DMSO; 30 μL per vial (300 tests). |
| Storage Conditions | Store at -25 to -15 °C. |
| Shelf Life | 1 year when stored at -25 to -15 °C. |
| Package Specifications | 300 T (30 μL per vial, 1 mg/mL). |
| Product Form | Liquid stock solution in DMSO. |
| Concentration | 1 mg/mL |
| Molecular Weight | ~1800 Da |
| Source / Origin | The phalloidin moiety is a cyclic heptapeptide toxin derived from the death cap mushroom Amanita phalloides. |
| Shipping Conditions | Shipped on ice packs. |
| Expiration Date / Stability | Stable for 1 year when stored at -25 to -15 °C. |
| Regulatory / Compliance | For research use only. |
| Compatibility | Fully compatible with other fluorescent labels used in cell analysis, including fluorescent proteins, semiconductor nanocrystal labels, and other Fluor dye conjugates (including Fluor-conjugated secondary antibodies). F-actin bound by this product retains many native actin biological properties. Binding is species-independent. |
| Application Notes / Precautions | Phalloidin derivatives are very small (approximately 12-15 Å in diameter, molecular weight <2000 Daltons), so most physiological properties of actin are preserved after labeling: labeled filaments still interact with actin-binding proteins such as myosin, tropomyosin, and DNase I; phalloidin-labeled filaments can still penetrate solid-phase myosin matrices; and glycerol-extracted muscle fibers remain contractile after labeling. Because phalloidin binding lowers the critical concentration of actin polymerization to <1 μg/mL, this product can also be used as an actin polymerization-promoting agent; phalloidin additionally inhibits the ATP hydrolysis activity of F-actin. The high staining specificity and contrast make this conjugate a superior alternative to actin antibodies for F-actin visualization. |
| Recognition Site | Filamentous actin (F-actin); does not bind monomeric actin (G-actin). |
For research use only, not for clinical use.
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