Latrunculin A | Inhibits actin polymerization and microfilament organization
NMR (Conforms)
Available Options
| Size : | Price | Quantity | |
|---|---|---|---|
| 100 µg | $98.00 | ||
| 500 µg | $392.00 |
Latrunculin A (76343-93-6) inhibits actin polymerization and disrupts microfilament organization.1 Significantly more potent than cytochalasins in the disruption of microfilamament mediated processes.2 Active in cell culture.3,4
References/Citations:
1) Coue et al. (1987), Inhibition of actin polymerization by latrunculin; FEBS Lett., 213 316
2) Spector et al. (1989), Latrunculins-novel marine macrolides that disrupt microfilament organization and affect cell growth; Cell Motil. Cytoskeleton, 13 127
3) Wang et al. (2005), Differential effects of latrunculin-A on myofibrils in cultures of skeletal muscle cells: Insights into mechanisms of myofibrillogenesis; Cell Motil. Cytoskeleton, 62 35
4) Reggiori et al. (2005), The actin cytoskeleton is required for selective types of autophagy, but not for non-specific autophagy, in the yeast Saccharomyces cerevisiae; Mol. Biol. Cell, 16 5843
5) Asadi et al. (2016) A Genetic Screen for Fission Yeast Gene Deletion Mutants Exhibiting Hypersensitivity to Latrunculin A; G3 Genes Genomes Genetics, 6 3399 [Focus Citation]
6) Belyy et al. (2016) Actin activates Pseudomonas aeruginosa ExoY nucleotidyl cyclase toxin and ExoY-like effector domains from MARTX toxins; Nat. Commun. 7 13582 [Focus Citation]
NMR (Conforms)
Safety Data Sheet:
Product Data Sheet:
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Latrunculin A (76343-93-6) inhibits actin polymerization and disrupts microfilament organization.1 Significantly more potent than cytochalasins in the disruption of microfilamament mediated processes.2 Active in cell culture.3,4
References/Citations:
1) Coue et al. (1987), Inhibition of actin polymerization by latrunculin; FEBS Lett., 213 316
2) Spector et al. (1989), Latrunculins-novel marine macrolides that disrupt microfilament organization and affect cell growth; Cell Motil. Cytoskeleton, 13 127
3) Wang et al. (2005), Differential effects of latrunculin-A on myofibrils in cultures of skeletal muscle cells: Insights into mechanisms of myofibrillogenesis; Cell Motil. Cytoskeleton, 62 35
4) Reggiori et al. (2005), The actin cytoskeleton is required for selective types of autophagy, but not for non-specific autophagy, in the yeast Saccharomyces cerevisiae; Mol. Biol. Cell, 16 5843
5) Asadi et al. (2016) A Genetic Screen for Fission Yeast Gene Deletion Mutants Exhibiting Hypersensitivity to Latrunculin A; G3 Genes Genomes Genetics, 6 3399 [Focus Citation]
6) Belyy et al. (2016) Actin activates Pseudomonas aeruginosa ExoY nucleotidyl cyclase toxin and ExoY-like effector domains from MARTX toxins; Nat. Commun. 7 13582 [Focus Citation]
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