Cell Signaling Technology

Product Pathways - MAPK Signaling

Anisomycin #2222

Molecular Formula:
C14H19NO4
Molecular Weight:
265.3 g/mol
Purity:
>98%

Directions for Use

Anisomycin is supplied as a lyophilized powder. For a 25 mg/ml stock, reconstitute the 10 mg in 400 µl DMSO. Working concentrations and length of treatments vary depending on the desired effect, but it is typically used at 5-50 µg/ml for 5-60 minutes. Soluble in DMSO or MeOH.

Western Blotting

Western Blotting

Western blot analysis of extracts from 293T cells, treated with Anisomycin (25 μg/ml) for the indicated times, with or without pretreatment with JNK inhibitor SP600125 (50 μM, 40 min; +), using Phospho-JunB (Thr102/Thr104) (D3C6) Rabbit mAb #8053 (upper) or JunB (C37F9) Rabbit mAb #3753 (lower).

Western Blotting

Western Blotting

Western blot analysis of extracts from Jurkat cells, serum-starved overnight, pretreated with the indicated concentrations of SB202190 for 1 hr, and subsequently treated with Anisomycin (25 μg/ml, 30 min; +), using Phospho-p38 MAPK (Thr180/Tyr182) (D3F9) XP® Rabbit mAb #4511 (upper) or p38 MAPK Antibody #9212 (lower).

Structure

Structure

Chemical structure of anisomycin.


Background

Anisomycin, an antibiotic produced by Streptomyces griseolus and S. roseochromogenes, was originally described to inhibit protein-protein synthesis at the translational level (1). More recently, it is has been well characterized to strongly activate the stress kinases SAPK/JNK and p38 MAPK, as well as p70/85 S6 kinase in mammalian cells, which results in the rapid induction of immediate-early (IE) genes, such as c-fos, fosB, c-jun, JunB, and JunD (1). Investigators have demonstrated that anisomycin acts as a potent signaling agonist, synergizing with growth factors and phorbol esters to superinduce these IE genes (1,2). Research studies have demonstrated that anisomycin induces apoptosis in many cancer cell lines (3-5).

  1. Hazzalin, C.A. et al. (1998) Mol Cell Biol 18, 1844-54.
  2. Kardalinou, E. et al. (1994) Mol Cell Biol 14, 1066-74.
  3. Kochi, S.K. and Collier, R.J. (1993) Exp Cell Res 208, 296-302.
  4. Törocsik, B. and Szeberényi, J. (2000) Biochem Biophys Res Commun 278, 550-6.
  5. Curtin, J.F. and Cotter, T.G. (2002) Br J Cancer 87, 1188-94.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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