Catalog Number: 1368
Chemical Name: 9,13-Dihydroxy-8,14,19-trimethoxy-4,10,12,16-tetramethyl-2-azabicyclo[16.3.1]docosa-4,6,10,18,21-pentaene-3,20,22-trione, 9-carbamate
Biological Activity
Selectively inhibits heat shock protein 90 (Hsp90). Binds to the ATP site of Hsp90 (Kd = 1.2 μM) and inhibits its chaperone activity. Consequently inhibits activities of oncogenic kinases (e.g. src, Raf), p53 and steroid receptors. Demonstrates antiproliferative effect on breast cancer stem-like cells.
Technical Data
  • M.Wt:
    560.64
  • Formula:
    C29H40N2O9
  • Solubility:
    Soluble to 10 mM in DMSO
  • Purity:
    >98%
  • Storage:
    Desiccate at -20°C
  • CAS No:
    30562-34-6
The technical data provided above is for guidance only. For batch specific data refer to the Certificate of Analysis. All Tocris products are intended for laboratory research use only.
Background References
  1. Signal-transduction cascades as targets for therapeutic intervention by natural products.
    Cardenas et al.
    Trends Biotechnol., 1998;16:427
  2. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.
    Whitesell et al.
    Proc.Natl.Acad.Sci.U.S.A., 1994;91:8324
  3. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanomycin.
    Roe et al.
    J.Med.Chem., 1999;42:260
  4. Inhibition of heat shock protein (Hsp) 27 potentiates the suppressive effect of Hsp90 inhibitors in targeting breast cancer stem-like cells.
    Lee et al.
    Biochimie., 2012;94:1382
Citations:

The citations listed below are publications that use Tocris products. Selected citations for Geldanamycin include:

3 Citations: Showing 1 - 3
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  1. Hsp90 and hepatobiliary transformation during sea lamprey metamorphosis.
    Authors: Chung-Davidson Et al.
    Nucleic Acids Res 2015;15:47
  2. A novel mechanism of autophagic cell death in dystrophic muscle regulated by P2RX7 receptor large-pore formation and HSP90.
    Authors: Young Et al.
    BMC Dev Biol 2015;11:113
  3. Inhibition of Hsp90 acts synergistically with topoisomerase II poisons to increase the apoptotic killing of cells due to an increase in topoisomerase II mediated DNA damage.
    Authors: Barker Et al.
    Neuroscience 2006;34:1148

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