Actin Inhibitors
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $260.00 $799.00 | 36 | |
Latrunculin A, derived from the marine sponge Latrunculia magnifica, is a potent actin polymerization inhibitor that disrupts cytoskeletal dynamics. It binds to G-actin, preventing its assembly into F-actin filaments, thereby altering cellular morphology and motility. This compound exhibits unique kinetics, with a rapid onset of action that leads to significant changes in cell shape and function. Its specificity for actin highlights its role in modulating cellular architecture and signaling pathways. | ||||||
Phalloidin Amine | sc-397330 | 100 µg | $236.00 | 1 | ||
Phalloidin Amine is a cyclic peptide that selectively binds to F-actin, stabilizing filamentous structures and preventing depolymerization. This interaction enhances the integrity of the cytoskeleton, influencing cellular shape and mechanical properties. Its affinity for actin is characterized by a unique binding mechanism that promotes filament stability, thereby affecting cellular processes such as motility and division. The compound's distinct structural features contribute to its role in actin dynamics. | ||||||
Latrunculin B | 76343-94-7 | sc-203318 | 1 mg | $229.00 | 29 | |
Latrunculin B is a potent actin-disrupting agent that sequesters monomeric G-actin, inhibiting its polymerization into filamentous structures. This selective binding alters the equilibrium between G-actin and F-actin, leading to a rapid decrease in filamentous actin pools. The compound's unique interaction with actin monomers disrupts cytoskeletal organization, impacting cellular processes like shape maintenance and motility. Its kinetic profile reveals a fast onset of action, making it a critical tool for studying actin dynamics. | ||||||
Swinholide A, Theonella swinhoei | 95927-67-6 | sc-205914 | 10 µg | $135.00 | ||
Swinholide A, derived from Theonella swinhoei, exhibits a unique mechanism of action on actin by promoting the disassembly of filamentous structures. It binds to specific sites on F-actin, destabilizing the polymer and facilitating depolymerization. This compound influences actin dynamics through its distinct interaction with the cytoskeletal network, leading to altered cellular morphology and motility. Its rapid kinetics enable swift modulation of actin filament integrity, providing insights into cytoskeletal regulation. | ||||||