SCRIPTAID

Scriptaid is a histone deacetylase inhibitor that has an optimal concentration of 6-8 μM in a cell-based assay, is less toxic than trichostatin A, and works in a wide variety of biological systems. It induces cell cycle arrest in colon cancer cells in culture and inhibits tumor growth in vitro and in vivo. Scriptaid also facilitates the cloning of inbred mouse strains produced by somatic cell nuclear transfer.

Histone deacetylase inhibitor. A cell-permeable, relatively non-toxic HDAC inhibitor that facilitates transcriptional activation (TGFβ/Smad4) in both stable and transient receptor assays in a concentration-dependent manner.

Scriptaid has been used in post activation of oocytes and embryo culture.

ChEBI: 6-(1,3-dioxo-2-benzo[de]isoquinolinyl)-N-hydroxyhexanamide is a member of isoquinolines.

Scriptaid is a histone deacetylase (HDAC) inhibitor, which enhances global acetylation of histones. It improves transcriptional activity and protein expression. Scriptaid inhibits tumor growth. It decreases telomerase activity and stimulates glioma cell apoptosis.

Novel histone deacetylase inhibitor. Produces > 100-fold increase in histone acetylation and displays relatively low toxicity.

Histone deacetylase inhibitor with lower toxicity than trichostatin A; used to enhance protein expression.

1) Su?et al.?(2000),?A novel histone deacetylase inhibitor identified by high-throughput transcriptional screening of a compound library; Cancer Res.,?60?3137 2) Huber?et al.?(2011),?Inhibitors of histone deacetylases: correlation between isoform specificity and reactivation of HIV type 1 (HIV-1) from latently infected cells; J. Biol. Chem.,?286?22211 3) Lee?et al.?(2008),?Histone deacetylase inhibitor scriptaid induces cell cycle arrest and epigenetic change in colon cancer cells; J. Oncol.,?33?767 4) Rissi?et al.?(2019),?Inhibition of RNA synthesis during Scriptaid exposure enhances gene reprogramming in SCNT embryos; Reproduction,?157?123 5) Huang?et al.?(2020),?Scriptaid/exercise-induced lysine acetylation is another type of posttranslational modification occurring in titin; J. Appl. Physiol.,?128?276