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Jasplakinolide

F-actin probe
 
ALX-350-275-C050 50 µg 187.00 USD
 
ALX-350-275-C100 100 µg 312.00 USD
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Cell permeable F-actin probe. Induces actin polymerization. Completely inhibits the binding of phalloidin to F-actin. Antifungal and anti-proliferative agent.

Product Specification

Alternative Name:Jaspamide
 
Formula:C36H45BrN4O6
 
MW:709.7
 
Source:Isolated from Jaspis splendens.
 
CAS:102396-24-7
 
Purity:≥97% (HPLC)
 
Identity:Determined by 1H-NMR and ESI-MS.
 
Appearance:Off-white to yellow solid.
 
Solubility:Soluble in 100% ethanol, 83% methanol or DMSO.
 
Shipping:Ambient
 
Long Term Storage:-20°C
 
Handling:Protect from light.
 
350-275
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350-275

Product Literature References

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
Different contributions of clathrin-and caveolae-mediated endocytosis of vascular endothelial cadherin to lipopolysaccharide-induced vascular : Y. Zhang, et al.; PLoS One 9, e106328 (2014), Abstract; Full Text
Mitochondria localize to the cleavage furrow in mammalian cytokinesis: E.J. Lawrence, et al.; PLoS One 8, e72886 (2013), Abstract; Full Text
Gliding motility of Babesia bovis merozoites visualized by time-lapse video microscopy: M. Asada, et al.; PLoS One 7, e35227 (2012), Abstract; Full Text
Actin dynamics counteract membrane tension during clathrin-mediated endocytosis: S. Boulant, et al.; Nat. Cell Biol. 13, 1124 (2011), Abstract;
Dynamic macrophage "probing" is required for the efficient capture of phagocytic targets: R.S. Flannagan, et al.; J. Cell Biol. 191, 1205 (2010), Abstract; Full Text
Rab27a negatively regulates phagocytosis by prolongation of the actin-coating stage around phagosomes: K. Yokoyama, et al.; J. Biol. Chem. 286, 5375 (2010), Abstract;
Dynamics of an F-actin aggresome generated by the actin-stabilizing toxin jasplakinolide: F. Lázaro-Diéguez, et al.; J. Cell Sci. 121, 1415 (2008), Abstract;
A simple model for the cooperative stabilisation of actin filaments by phalloidin and jasplakinolide: B. Visegrády, et al.; FEBS Lett. 579, 6 (2005), Abstract;
A role for the actin cytoskeleton in the initiation and maintenance of store-mediated calcium entry in human platelets. Evidence for conformational coupling: J.A. Rosado, et al.; J. Biol. Chem. 275, 7527 (2000), Abstract; Full Text
Effects of jasplakinolide on the kinetics of actin polymerization. An explanation for certain in vivo observations: M.R. Bubb, et al.;; J. Biol. Chem. 275, 5163 (2000), Abstract; Full Text
Actin stabilization by jasplakinolide enhances apoptosis induced by cytokine deprivation: S.C. Posey & B.E. Bierer; J. Biol. Chem. 274, 4259 (1999), Abstract; Full Text
Role of actin-filament disassembly in lamellipodium protrusion in motile cells revealed using the drug jasplakinolide: L.P. Cramer; Curr. Biol. 9, 1095 (1999), Abstract;
The anti-proliferative agent jasplakinolide rearranges the actin cytoskeleton of plant cells: H. Sawitzky, et al.; Eur. J. Cell Biol. 78, 424 (1999), Abstract;
Jasplakinolide: interaction with radiation and hyperthermia in human prostate carcinoma and Lewis lung carcinoma: H. Takeuchi, et al.; Cancer Chemother. Pharmacol. 42, 491 (1998), Abstract;
Growth modulation and differentiation of acute myeloid leukemia cells by jaspamide: I. Fabian, et al.; Exp. Hematol. 23, 583 (1995), Abstract;
Jasplakinolide's inhibition of the growth of prostate carcinoma cells in vitro with disruption of the actin cytoskeleton: A.M. Senderowicz, et al.; J. Natl. Cancer Inst. 87, 46 (1995), Abstract;
Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin: M.R. Bubb, et al.; J. Biol. Chem. 269, 14869 (1994), Abstract; Full Text
In vitro screening of crude extracts and pure metabolites obtained from marine invertebrates for the treatment of breast cancer: J. Stingl, et al.; Cancer Chemother. Pharmacol. 30, 401 (1992), Abstract;
New class of antifungal agents: jasplakinolide, a cyclodepsipeptide from the marine sponge, Jaspis species: V.R. Scott, et al.; Antimicrob. Agents Chemother. 32, 1154 (1988), Abstract;

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