Phalloidin | Actin-binding agent

Phalloidin chemical structure

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Phalloidin (17466-45-4) is a bicyclic heptapeptide that binds to filamentous actin, promoting and stabilizing polymerization.1,2 Reverses actin destabilization by cytochalasin B2, and modifies branch formation / deformation mediated by Arp2/3 complex3. Immobilized phalloidin can be used for biochemical isolation of F-actin and F-actin binding proteins.4

References/Citations:

  1. Coluccio and Tilney (1984), Phalloidin enhances actin assembly by preventing monomer dissociation; J. Cell Biol. 99 529
  2. Cooper. (1987), Effects of cytochalasin and phalloidin on actin; J. Cell Biol. 105 1473
  3. Mahaffy et al. (2006), Kinetics of the formation and dissociation of actin filament branches mediated by Arp2/3 complex; Biophys. J. 91 3519
  4. Samwer et al. (2013), The nuclear F-actin interactome of Xenopus oocytes reveals an actin-bundling kinesin that is essential for meiotic cytokinesis; EMBO J. 32 1886
17466-45-4, Phalloidin, Phalloidin supplier

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Phalloidin (17466-45-4) is a bicyclic heptapeptide that binds to filamentous actin, promoting and stabilizing polymerization.1,2 Reverses actin destabilization by cytochalasin B2, and modifies branch formation / deformation mediated by Arp2/3 complex3. Immobilized phalloidin can be used for biochemical isolation of F-actin and F-actin binding proteins.4

References/Citations:

  1. Coluccio and Tilney (1984), Phalloidin enhances actin assembly by preventing monomer dissociation; J. Cell Biol. 99 529
  2. Cooper. (1987), Effects of cytochalasin and phalloidin on actin; J. Cell Biol. 105 1473
  3. Mahaffy et al. (2006), Kinetics of the formation and dissociation of actin filament branches mediated by Arp2/3 complex; Biophys. J. 91 3519
  4. Samwer et al. (2013), The nuclear F-actin interactome of Xenopus oocytes reveals an actin-bundling kinesin that is essential for meiotic cytokinesis; EMBO J. 32 1886