For research use only. Not Intended for Therapeutic Use!
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(R)-(-)-JQ1 Enantiomer, the stereoisomer (+)-JQ1, showed no significant interaction with any bromodomain; (+)-JQ1 is an inhibitor for the BET.
Target: BET bromodomain
The (R)-(-)-JQ1 Enantiomer stereoisomer has no appreciable affinity to BET bromodomains, whereas enantiomerically pure (+)-JQ1 binds to BRD4 bromodomains 1 and 2 with Kd values of ~ 50 and 90 nM, respectively.
. Filippakopoulos, Panagis et al. Selective inhibition of BET bromodomains From Nature (London, United Kingdom) (2010), 468(7327), 1067-1073. Abstract Epigenetic proteins are intently pursued targets in ligand discovery. So far, successful efforts have been limited to chromatin modifying enzymes, or so-called epigenetic /'writers/' and /'erasers/'. Potent inhibitors of histone binding modules have not yet been described. Here we report a cell-permeable small molecule (JQ1) that binds competitively to acetyl-lysine recognition motifs, or bromodomains. High potency and specificity towards a subset of human bromodomains is explained by co-crystal structures with bromodomain and extra-terminal (BET) family member BRD4, revealing excellent shape complementarity with the acetyl-lysine binding cavity. Recurrent translocation of BRD4 is observed in a genetically-defined, incurable subtype of human squamous carcinoma. Competitive binding by JQ1 displaces the BRD4 fusion oncoprotein from chromatin, prompting squamous differentiation and specific antiproliferative effects in BRD4-dependent cell lines and patient-derived xenograft models. ...