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Latrunculin B

Ultra-pure; inhibits actin polymerization
BML-T110-0001 1 mg Inquire for pricing
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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 Details

Source:Isolated from Latrunculia magnifica.
MI:14: 5378
Purity:≥98% (HPLC)
Appearance:Lyophilized solid.
Solubility:Soluble in DMSO (25mg/ml) or 100% ethanol (25mg/ml).
Long Term Storage:-20°C
Regulatory Status:RUO - Research Use Only
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Product Literature References

Deciphering cell signaling networks with massively multiplexed biosensor barcoding: J-M. Yang, et al.; Cell 184, 6193 (2021), Abstract;
A Role for Nuclear Actin in HDAC 1 and 2 Regulation: L. Serebryannyy, et al.; Sci. Rep. 6, 28460 (2016), Application(s): Cell culture and antibodies, Abstract; Full Text
Dynamic actin cycling through mitochondrial subpopulations locally regulates the fission-fusion balance within mitochondrial networks: A.S. Moore, et al.; Nat. Commun. 7, 12886 (2016), Abstract; Full Text
Filopodia-based Wnt transport during vertebrate tissue patterning: E. Stanganello, et al; Nat. Commun. 6, 5846 (2015), 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. 213, 316 (1987), 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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