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F-actin probe
Cell permeable F-actin probe. Induces actin polymerization. Completely inhibits the binding of phalloidin to F-actin. Antifungal and anti-proliferative agent.
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Product Details
| Alternative Name |
Jaspamide |
|---|---|
| Appearance |
Off-white to yellow solid. |
| CAS |
102396-24-7 |
| Formula |
C36H45BrN4O6 |
| Identity |
Determined by 1H-NMR and ESI-MS. |
| MW |
709.7 |
| Purity |
≥97% (HPLC) |
| Solubility |
Soluble in 100% ethanol, 83% methanol or DMSO. |
| Source |
Isolated from Jaspis splendens. |
Handling & Storage
| Use/Stability |
As indicated on product label or CoA when stored as recommended. |
|---|---|
| Handling |
Protect from light. |
| Long Term Storage |
-20°C |
| Shipping |
Ambient Temperature |
| Regulatory Status |
RUO – Research Use Only |
|---|
- Genetic Suppression of Defective Profilin by Attenuated Myosin II Reveals a Potential Role for Myosin II in Actin Dynamics in vivo in fission yeast: P. Zambon, et al.; Mol. Biol. Cell 31, 2107 (2020), Abstract — Full Text
- An Excitable Ras/PI3K/ERK Signaling Network Controls Migration and Oncogenic Transformation in Epithelial Cells: Zhan, H., Bhattacharya, S., et al.; Dev. Cell 54, 608 (2020), Abstract
- 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
- In vitro and in vivo characterization of the actin polymerizing compound chondramide as an angiogenic inhibitor: Menhofer, M. H., Bartel, D., et al.; Cardiovasc. Res. 104, 303 (2014), Abstract
- The HCMV gH/gL/UL128-131 complex triggers the specific cellular activation required for efficient viral internalization into target monocytes: Nogalski, M. T., Chan, G. C., et al.; PLoS Pathog. 9, e1003463 (2013), Application(s): In Vitro, Abstract
- 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
- Differential modulation of the molecular dynamics of the type IIa and IIc sodium phosphate cotransporters by parathyroid hormone: Lanzano, L., Lei, T., et al.; Am. J. Physiol. Cell Physiol. 301, C850 (2011), Abstract
- Actin dynamics counteract membrane tension during clathrin-mediated endocytosis: S. Boulant, et al.; Nat. Cell Biol. 13, 1124 (2011), Abstract
- Rab27a negatively regulates phagocytosis by prolongation of the actin-coating stage around phagosomes: K. Yokoyama, et al.; J. Biol. Chem. 286, 5375 (2010), 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
- PTH-induced internalization of apical membrane NaPi2a: role of actin and myosin VI: Blaine, J., Okamura, K., et al.; Am. J. Physiol. Cell Physiol. 297, C1339 (2009), 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
- 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
- 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
- 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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