Latrunculin B (CAS: 76343-94-7)

C₂₀H₂₉NO₅S

• Cell permeable marine toxin [1].
• Disrupts microfilament-mediated processes [2].
• Actin polymerization inhibitor in vitro and in vivo by the formation of a 1:1 complex with monomeric G-actin [1, 2, 3].
• Depolymerizes actin filaments (F-actin) [3].
• Less potent than Latrunculin A (Prod. No. AG-CN2-0027). May have fewer unwanted effects than latrunculin A and may be preferred for short-term studies [4, 5].
• Acts via a different mechanism than cytochalasins.

1. Latrunculins: novel marine toxins that disrupt microfilament organization in cultured cells: I. Spector, et al.; Science 219, 493 (1983)
2. Latrunculin inhibits the microfilament-mediated processes during fertilization, cleavage and early development in sea urchins and mice: G. Schatten, et al.; Exp. Cell Res. 166, 191 (1986)
3. Inhibition of actin polymerization by latrunculin: A: M. Coue, et al.; FEBS Lett. 213, 316 (1987)
4. Latrunculins-novel marine macrolides that disrupt microfilament organization and affect cell growth: I. Comparison with cytochalasin D: I. Spector, et al.; Cell Motil. Cytoskeleton 13, 127 (1989)
5. Effects of cytochalasin D and latrunculin B on mechanical properties of cells: T. Wakatsuki, et al.; J. Cell. Sci. 114, 1025 (2001)
6. RNAi screening identifies the armadillo repeat-containing kinesins responsible for microtubule-dependent nuclear positioning in Physcomitrella patens: T. Miki, et al.; Plant Cell Physiol. 56, 737 (2015)
7. Evidence that an unconventional actin can provide essential F-actin function and that a surveillance system monitors F-actin integrity in Chlamydomonas: M. Onishi, et al.; Genetics 202, 977 (2016)