Cytochalasin D

Cytochalasin D is a cell permeable fungal toxin that binds to the barbed end of actin filaments inhibiting both the association and dissociation of subunits. This compound causes the disruption of actin filaments and inhibition of actin polymerization. Cytochalasin D is about 10-fold more effective than cytochalasin B and does not inhibit monosaccharide transport across cell membranes.\n\nSolubility: \nDMSO (25mg/ml)\n\nSterility: \nThis product is not sterile.\n\nMolecular Weight: \n~507.6\n\nStorage and Stability: \nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with DMSO. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

C9093-50

Size

1mg

Form

Supplied as a white lyophilized powder.\n\n

Purity

~98%

References

1. Flanagan, M.D. and S. Lin (1980) Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin. J. Biol. Chem. 255(3):835-838.2. Goddette, D.W. and C. Frieden (1986) Actin polymerization. The mechanism of action of cytochalasin D. J. Biol. Chem. 261(34):15974-15980.3. Cooper, J.A. (1987) Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 105(4):1473-1478.4. Tangkijvanich, P., et al. (2002) Platelet-derived growth factor-BB and lysophosphatidic acid distinctly regulate hepatic myofibroblast migration through focal adhesion kinase. Exp. Cell. Res. 281(1):140-147.5. Goel, H.L., and C.S. Dey (2002) PKC-regulated myogenesis is associated with increased tyrosine phosphorylation of FAK, Cas, and paxillin, formation of Cas-CRK complex, and JNK activation. Differentiation 70(6):257-271.6. Tran, N.L., et al. (2002) Signal transduction from N-cadherin increases Bcl-2. Regulation of the phosphatidylinositol 3-kinase/Akt pathway by homophilic adhesion and actin cytoskeletal organization. J. Biol. Chem. 277(36):32905-32914.