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Chemical Structure : Allopole-A
Catalog No.: PC-21080Not For Human Use, Lab Use Only.
Allopole-A is the first allosteric, specfic inhibitor of the noncatalytic polo-box domain (PBD) of PLK1 (Polo-like kinase 1) with IC50 of 2.5 nM in FP-based assays, Allopole-A is the active form of Allopole.
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Allopole-A is the first allosteric, specfic inhibitor of the noncatalytic polo-box domain (PBD) of PLK1 (Polo-like kinase 1) with IC50 of 2.5 nM in FP-based assays, Allopole-A is the active form of Allopole.
Allopole-A displays no binding affinity for Plk2 and Plk3.
Both F559 and W410 are critical for Allopole-A's Plk1-binding specificity, mutation of Plk1 F559 confers resistance to allopole.
Allopole-A binds to the allosteric W-F pocket occluded by the L2 loop dislodges the loop, consequently stripping several water-mediated interactions critical for phosphoepitope binding.
Allopole-A is sufficient to trigger the dissociation of a phospholigand and to inhibit PBD1-dependent downstream events.
Allopole-A has low cell membrane permeability.
| M.Wt | 312.79 | |
| Formula | C11H9ClN4OS2 | |
| Appearance | Solid | |
| Storage |
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| Solubility |
10 mM in DMSO |
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1. Park JE, et al. Proc Natl Acad Sci U S A. 2023 Aug 29;120(35):e2305037120.
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