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Latrunculin A

Ultra-pure; inhibits actin polymerization
 
BML-T119-0100 100 µg 138.00 USD
 
BML-T119-0500 500 µg 551.00 USD
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Replaces Prod. #: ALX-350-130

Inhibits actin polymerization, microfilament organzation and microfilament-mediated processes. Acts via a different mechanism and 10- to 20-fold more potently than cytochalasins. Inhibits phagocytosis by macrophages. Exposure to 0.2 mg/ml for one hour produces maximal change in cell morphology.

Product Specification

Formula:C22H31NO5S
 
MW:421.6
 
CAS:76343-93-6
 
MI:14: 5378
 
Purity:≥95% (HPLC)
 
Appearance:White to yellow waxy solid.
 
Solubility:Soluble in DMSO (25mg/ml) or 100% ethanol (25mg/ml).
 
Shipping:Ambient
 
Long Term Storage:-20°C
 
Use/Stability:Stable for 1 year after receipt when stored at -20°C. Stock solutions are stable for up to 3 months when stored at -20°C.
 
Handling:Protect from light.
 
Technical Info/Product Notes:Note: Product is not sterile.
 
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Product Literature References

Calcium-mediated actin reset (CaAR) mediates acute cell adaptations: P. Wales, et al.; eLife 5, e19850 (2016), Abstract; Full Text
GEF-H1 is necessary for neutrophil shear stress-induced migration during inflammation: N. Fine, et al.; J. Cell. Biol. 215, 107 (2016), Application(s): Cell treatment, mouse neutrophils, Abstract; Full Text
Calpain-Mediated Degradation of Drebrin by Excitotoxicity In vitro and In vivo: T. Chimura, et al.; PLoS One 10, e0125119 (2015), Application(s): Cell Culture, Abstract; Full Text
Opposite rheological properties of neuronal microcompartments predict axonal vulnerability in brain injury: T. Grevesse, et al.; Sci. Rep. 5, 9475 (2015), Application(s): Cell Culture, Abstract; Full Text
Spontaneous Cdc42 Polarization Independent of GDI-Mediated Extraction and Actin-Based Trafficking: F. O. Bendezú, et al.; PLoS One 31, e1002097 (2015), Application(s): Cell Culture, Abstract; Full Text
Human sperm CRISP2 is released from the acrosome during the acrosome reaction and re-associates at the equatorial segment: W. Nimlamool, et al.; Mol. Reprod. Dev. 80, 488 (2013), Abstract;
Mitochondria localize to the cleavage furrow in mammalian cytokinesis: E.J. Lawrence, et al.; PLoS One 8, e72886 (2013), Abstract; Full Text
The nucleus of endothelial cell as a sensor of blood flow direction: E. Tkachenko, et al.; Biol. Open 2, 1007 (2013), Abstract; Full Text
A role for hippocampal actin rearrangement in object placement memory in female rats: B.S. Nelson, et al.; Neurobiol. Learn. Mem. 98, 284 (2012), Abstract;
Respiratory syncytial virus assembles into structured filamentous virion particles independently of host cytoskeleton and related proteins: F.Y. Shaikh, et al.; PLoS One 7, e40826 (2012), Abstract; Full Text
Glioblastoma motility occurs in the absence of actin polymer: A. Panopoulos, et al.; Mol. Biol. Cell 22, 2212 (2011), Abstract; Full Text
Thymosin beta4 inhibits TNF-alpha-induced NF-kappaB activation, IL-8 expression, and the sensitizing effects by its partners PINCH-1 and ILK: P. Qiu, et al.; FASEB J. 25, 1815 (2011), Abstract; Full Text
Regulation of Distinct Septin Rings in a Single Cell by Elm1p and Gin4p Kinases: B.S. DeMay, et al.; Mol. Biol. Cell 20, 2311 (2009), Abstract;
Latrunculin A depolarizes starfish oocytes: F. Moccia; Comp. Biochem. Physiol. A Mol. Integr. Physiol. 148, 845 (2007), Abstract;
Differential effects of latrunculin-A on myofibrils in cultures of skeletal muscle cells: Insights into mechanisms of myofibrillogenesis: J. Wang, et al.; Cell Motil. Cytoskeleton 62, 35 (2005), Abstract;
Seizures induced by microperfusion of glutamate and glycine in the hippocampus of rats pretreated with latrunculin A: A. Vazquez-Lopez; Neurosci. Lett. 388, 81 (2005), Abstract;
The actin cytoskeleton is required for selective types of autophagy, but not nonspecific autophagy, in the yeast Saccharomyces cerevisiae: F. Reggiori, et al.; Mol. Biol. Cell 16, 5843 (2005), Abstract;
High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A: K.R. Ayscough, et al.; J. Cell Biol. 137, 399 (1997), Abstract; Full Text
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 and B. Mantovani; Life Sci. 43, 1825 (1988), Abstract;
Inhibition of actin polymerization by latrunculin: A: 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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