Anisomycin

Protein synthesis inhibitor

Product#:A-520
Sizes:
5 mg
10 mg
50 mg
10 x 1 mg


Anisomycin is a bacterial antibiotic isolated from Streptomyces griseolus, which inhibits protein synthesis, by binding to 60S ribosomal subunits and blocking peptide bond formation, thereby preventing elongation and causing polysome stabilization. This action of Anisomycin monitored the cells for chromosomal DNA degradation and apoptosis.1-5

Anisomycin has been widely used as an extremely potent activator of kinase cascades in mammalian cells, especially the stress-activated protein kinase (SAPK2/p38MAPK), kinase subtypes and p46/54JNK. 6-13

Synergizes with growth factors and phorbol esters, anisomycin superinduce c-fos and c-jun by a number mechanisms, one of which is its ability to act as a potent signalling agonist, producing strong, prolonged activation of the same nuclear responses as epidermal growth factor or tetradecanoyl phorbol acetate.14 Anisomycin stimulated serine phosphorylation of IRS-1 and IRS-2, reduced their ability to interact with the insulin receptor and by that blocked the insulin-induced tyrosine phosphorylation of IRS proteins.15


M.W.:265.3

CAS No.:[22862-76-6]

Structure:
 

Purity:>98%

Bioassay:

 

Anisomycin induces p38 MAPK phosphorylation.
C6 glioma cells were grown to 70% confluence and then
serum starved for 3 h. and then stimulated with various
concentration Anisomycin for 60 min. The cell protein were
resolved by SDS PAGE, probed with Anti-Phospho-p38 MAPK
(upper panel) or with Anti-p38 MAPK (lower panel).


References:

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2.

Jiménez, A. et al. (1979) p. 1-19. In F. E. Hahn (ed.), Antibiotics, vol. 5 part 2. Springer-Verlag, New York, N.Y.

3.

Barbacid, M. et al. (1975) J. Mol. Biol. 93, 449.

4.

Kochi, S.K. et al. (1993) Exp. Cell. Res. 208, 296.

5.

Condorelli, G. et al. (2002) J. Biol. Chem. 277, 11013.

6.

Cano, E. et al. (1994) Mol. Cell. Biol. 14, 7352.

7.

Cano, E. et al. (1995) J. Cell Sci. 108, 3599.

8.

Chen, D. et al. (1996) J. Biol. Chem. 271, 6328.

9.

Ishikawa, Y. and Kitmura, M. (1999) Biochem. Biophys. Res. Commun. 264, 696.

10.

Bogoyevitch, M.A. et al. (1995) J. Biol. Chem. 270, 29710.

11.

Sanchez, et al. (1994) Nature 372, 794.

12.

Dérijard, B. et al. (1994) Cell 76, 1025.

13.

Hibi, M. et al. (1993) Genes Dev. 7, 2135.

14.

Barros, L.F. et al. (1998) Molecular and Cellular Biology 18, 1844.

15.

Hemi, R. et al. (2002) J. Biol. Chem. 277, 8961.
For research purposes only, not for human use.