Latrunculin B
Inhibits actin polymerization and microfilament organization / Inhibits actin polymerization and disrupts microfilament organization1. Significantly more potent than cytochalasins in the disruption of microfilamament mediated processes2, causes shortening and thickening of stress fibers. Active in cell culture.3,4 Effective doses vary depending upon cell type but are frequently in the low micromolar range. Note: Latrunculin B is slowly inactivated by fetal bovine serum.
Biochemicals & reagents
76343-94-7
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) Wakatsuki et al. (2001), Effects of cytochalasin D and latrunculin B on mechanical properties of cells; J. Cell. Sci., 114 1025 4) Cha et al. (2004), The lateral mobility of NHE3 on the apical membrane of renal epithelial OK cells is limited by the PDZ domain proteins NHERF1/2 but is dependent on an intact actin cytoskeleton as determined by FRAP; Prog. Clin. Biol. Res., 230 41
-20°C
TARGET: Cytoskeleton -- PATHWAY: Cell cycle