Latrunculin B | Inhibits actin polymerization and microfilament organization
NMR (Conforms)
Available Options
| Size : | Price | Quantity | |
|---|---|---|---|
| 100 µg | $45.00 | ||
| 1 mg | $190.00 |
Latrunculin B (76343-94-7) inhibits actin polymerization and disrupts microfilament organization.1 Significantly more potent than cytochalasins in the disruption of microfilament mediated processes2, causes shortening and thickening of stress fibers. Active in cell culture.3,4 Effective doses for latrunculin B vary depending upon cell type but are frequently in the low micromolar range. Note: Latrunculin B is slowly inactivated by fetal bovine serum.
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) 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 4
5) Herrera (2021), Cell cultures, transfection and treatments. protocols.io https://dx.doi.org/10.17504/
NMR (Conforms)
Safety Data Sheet:
Product Data Sheet:
Materials provided by Focus Biomolecules are for laboratory research use only and are not intended for human or veterinary applications. Please note that we do not sell to individuals and that all orders placed by non-research organizations will incur a $20 restocking/refund fee
Latrunculin B (76343-94-7) inhibits actin polymerization and disrupts microfilament organization.1 Significantly more potent than cytochalasins in the disruption of microfilament mediated processes2, causes shortening and thickening of stress fibers. Active in cell culture.3,4 Effective doses for latrunculin B vary depending upon cell type but are frequently in the low micromolar range. Note: Latrunculin B is slowly inactivated by fetal bovine serum.
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) 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 4
5) Herrera (2021), Cell cultures, transfection and treatments. protocols.io https://dx.doi.org/10.17504/
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