佰世凯热销产品——细胞松驰素J；Cytochalasin J；CAS：53760-20-6

CAS：53760-20-6
C17076
Product Name:Cytochalasin J
Synonyms：Deacetylcytochalasin H; Kodocytochalasin 2; Paspalin P II
ChemcialName:2,3,3a,4,5,6,6a,9,10,11,12,15-dodecahydro-6,12,15-trihydroxy-4,10,12-trimethyl-5-methylene-3-(phenylmethyl)-1H-cycloundec[d]isoindol-1-oneMolecular Formula:C₂₈H₃₇NO₄
Formula Weight:451.6
Purity:＞95%
Solubility：Soluble in DMSO or water.
Appearance:White solid.
Short Term Storage：+4°C
Long Term Storage：+4°C
Use/Stability：Stable for at least 1 year after receipt when stored at +4°C.

Biological Activity：
Cytochalasin J is used in actin polymerization studies. Cytochalasins are potent mycotoxins which bind to the barbed end of actin filaments resulting in inhibition of both the association and dissociation of subunits. Used as a tool for cytological research. These fungal toxins are related by their chemical structure characterized by a highly substituted hydrogenated isoindole ring to which is fused a macrocyclic ring. Cytochalasin J is the deacetyl analogue of cytochalasin H and exhibits similar, though less potent, antibacterial, antifungal, nematocidal and antitumor activities.
The cytochalasins are cell-permeable fungal metabolites that inhibit actin polymerization.This interferes with such diverse processes as cell movement, growth, phagocytosis, degranulation, and secretion.Cytochalasin J is a deacetylated analog of cytochalasin H that weakly inhibits actin assembly but significantly alters mitotic spindle microtubule organization and kinetochore structure. Like cytochalasin H, cytochalasin J suppresses the production of reactive oxygen species by stimulated human neutrophils.
Product Specific References：
1. S. L. Brenner and E. D. Korn. The effects of cytochalasins on actin polymerization and actin ATPase provide insights into the mechanism of polymerization. The Journal of Biological Chemisty 255(3) 841-844 (1980).
2. D. C. Lin, K. D. Tobin, M. Grumet, et al. Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation. Journal of Cell Biology 84 455-460 (1980).
3. R. E. Ostlund, Jr., J. T. Leung and S. V. Hajek. Regulation of microtubule assembly in cultured fibroblasts. Journal of Cell Biology 85 386-391 (1980).
4. J. C. Pinder and W. B. Gratzer. Structural and dynamic states of actin in the erythrocyte. Journal of Cell Biology 96(3) 768-775 (1983).
5. R. Flaumenhaft, J. R. Dilks, N. Rozenvayn, et al. The actin cytoskeleton differentially regulates platelet α-granule and dense-granule secretion. Blood 105(10) 3879-3887 (2005).
6. N. Taheri-Talesh, T. Horio, L. Araujo-Bazán, et al. The tip growth apparatus of Aspergillus nidulans. Molecular Biology of the Cell 19 1439-1449 (2008).
7. T. dos Santos, J. Varela, I. Lynch, et al. Effects of transport inhibitors on the cellular uptake of carboxylated polystyrene nanoparticles in different cell lines. PLoS One 6(9) 1-10 (2011).
8. T. D. Nightingale, I. J. White, E. L. Doyle, et al. Actomyosin II contractility expels von Willebrand factor from Weibel-Palade bodies during exocytosis. Journal of Cell Biology 194(4) 613-629 (2011).
9. E. A. Walling, G. A. Krafft and B. R. Ware. Actin assembly activity of cytochalasins and cytochalasin analogs assayed using fluorescence photobleaching recovery. Archives of Biochemistry and Biophysics 264(1) 321-332 (1988).
10. G. A. Wrench and J. A. Snyder. Cytochalasin J treatment significantly alters mitotic spindle microtubule organization and kinetochore structure in PtK1 cells. Cell Motility and the Cytoskeleton 36(2) 112-124 (1997).
11. V. M. Chapla, M. L. Zeraik, V. F. Ximenes, et al. Bioactive secondary metabolites from Phomopsis sp., and endophytic fungus from Senna spectabilis. Molecules 19 6597-6608 (2014).

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