Replaces Prod. #: ALX-350-036
Structurally unique marine toxin. Actin filament modulator. 10- to 100-fold more potent than cytochalasins. Whereas cytochalasin D (Prod. No. BML-T109) induces dissolution of F-actin and stress fiber contraction in fibroblasts in culture, latrunculin B causes a shortening and thickening of stress fibers. Effects on N1E-115 cells (mouse neuroblastoma) at concentrations as low as 90nM (NI43T3 cells, 0.9µM). Maximum effects at 2.5µM. Slowly inactivated by fetal bovine serum. Inhibition of cofilin-actin binding (ED50~50µM)
Product Specification
| Formula: | C20H29NO5S |
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| MW: | 395.5 |
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| Source: | Isolated from Latrunculia magnifica. |
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| CAS: | 76343-94-7 |
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| MI: | 14: 5378 |
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| Purity: | ≥98% (HPLC) |
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| Appearance: | Lyophilized solid. |
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| Solubility: | Soluble in DMSO (25mg/ml) or 100% ethanol (25mg/ml). |
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| Shipping: | Ambient |
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| Long Term Storage: | -20°C |
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Product Literature References
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Application(s): Cell culture and antibodies,
Abstract;
Full Text
Filopodia-based Wnt transport during vertebrate tissue patterning: E. Stanganello, et al; Nat. Commun.
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Application(s): Cell Culture,
Abstract;
The FRA1 kinesin contributes to cortical microtubule-mediated trafficking of cell wall components: C. Zhu, et al.; Plant Physiol.
167, 780 (2015),
Application(s): Cell Culture,
Abstract;
Full Text
Histones trigger sterile inflammation by activating the NLRP3 inflammasome: R. Allam, et al.; Eur. J. Immunol.
43, 3336 (2013),
Abstract;
Full Text
Isolation and characterization of cytoplasmic cofilin-actin rods: L.S. Minamide, et al.; J. Biol. Chem.
285, 5450 (2010),
Abstract;
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: B. Cha, et al.; J. Cell Sci.
117, 3353 (2004),
Abstract;
Full Text
Effects of cytochalasin D and latrunculin B on mechanical properties of cells: T. Wakatsuki, et al.; J. Cell. Sci.
114, 1025 (2001),
Abstract;
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),
Abstract;
Latrunculin A is a potent inhibitor of phagocytosis by macrophages: C.A. de Oliveira & B. Mantovani; Life Sci.
43, 1825 (1988),
Abstract;
Inhibition of actin polymerization by latrunculin: M. Coue, et al.; FEBS Lett.
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Abstract;
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),
Abstract;
Latrunculins: novel marine toxins that disrupt microfilament organization in cultured cells: I. Spector, et al.; Science
219, 493 (1983),
Abstract;
General Literature References
Makrolide aus marinen Organismen: G. Schilling; Labor&more 1.12, 32 (2012),
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