PU H71
Chemical Name: 6-Amino-8-[(6-iodo-1,3-benzodioxol-5-yl)thio]-N-(1-methylethyl)-9H-purine-9-propanamine
Purity: ≥98%
Biological Activity
PU H71 is a potent inhibitor of heat shock protein 90 (Hsp90) (IC50 = 51 nM in MDA-MB-468 cells). Also inhibits cell growth in a range of breast cancer cell lines (IC50 values are 17, 31, 65, 87 and 140 nM for SKBr3, MCF-7, MDA-MB-468, HCC-1806 and MDA-MB-231 cells respectively). Shown to inhibit cell proliferation and induce apoptosis in triple-negative breast cancer (TNBC) cells.Technical Data
The technical data provided above is for guidance only.
For batch specific data refer to the Certificate of Analysis.
Tocris products are intended for laboratory research use only, unless stated otherwise.
Background References
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Molecular imaging of the efficacy of heat shock protein 90 inhibitors in living subjects
Chan CT, Paulmurugan R, Gheysens OS et al.
Cancer Res -
Identification of potent water soluble purine-scaffold inhibitors of the heat shock protein 90.
He et al.
J.Med.Chem., 2006;49:381 -
Hsp90 inhibitor, PU-H71, a multimodal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models.
Caldas-Lopes et al.
Proc.Natl.Acad.Sci.USA, 2009;106:8368
Product Datasheets
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Citations for PU H71
The citations listed below are publications that use Tocris products. Selected citations for PU H71 include:
4 Citations: Showing 1 - 4
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The interaction between RE1-silencing transcription factor (REST) and heat shock protein 90 as new therapeutic target against Huntington's disease.
Authors: Orozco-Díaz Et al.
PLoS One 2019;14:e0220393
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The sensitivity to Hsp90 inhibitors of both normal and oncogenically transformed cells is determined by the equilibrium between cellular quiescence and activity.
Authors: Echeverría Et al.
PLoS One 2019;14:e0208287
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PU-H71, a novel Hsp90 inhibitor, as a potential cancer-specific sensitizer to carbon-ion beam therapy.
Authors: Li Et al.
J Radiat Res 2016;57:572
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The purine scaffold Hsp90 inhibitor PU-H71 sensitizes cancer cells to heavy ion radiation by inhibiting DNA repair by homologous recombination and non-homologous end joining.
Authors: Lee Et al.
Radiother Oncol 2016;121:162
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