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Trichostatin A (TSA) (Histone Deacetylase Inhibitor)

Cat no: T8375-05


Supplier: United States Biological
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Trichostatin A is an antifungal antibiotic that is a reversible, potent and specific inhibitor of mammalian histone deacetylase (HDAC) both in vivo and in vitro. Histone deacetylase inhibition causes chromatin relaxation and gene expression modulation. May induce apoptosis. TSA inhibits the eukaryotic cell cycle and induces morphological reversion of transformed cells. It blocks cell cycle progression at G1 phase in Hela Cells. TSA causes accumulation of highly acetylated histones in vivo, while inhibiting the activity of partially purified histone deacetylase in vitro. Applications: Suitable for use in Inhibition of Histone Deacetylation. Other applications not tested. Recommended Dilution: Inhibition of Histone Deacetylation: Incubation of A431 cells with 50-100ng/ml Trichostatin A for 24 hours inhibited deacetylation of histones in vivo, as detected using anti-acetylated Histone H4. The optimal concentration of Trichostatin A should be empirically determined for the type of cells and assay used. Storage and Stability: May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 3-4 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Catalogue number: T8375-05
Size: 1mg
Form: Supplied as a liquid in methanol.
Purity: Highly Purified ((same/more than) 99% by HPLC).
Alternative names: 4,6-Dimethyl-7-[p-dimethylaminophenyl]- 7-oxohepta-2, 4-dienohydroxamic acid)
References: 1. Taunton, et al., Science 272: 408 (1996) 2. Yoshida, Beppu, Exper. Cell Res. 177: 122 (1988). 3. Yoshida, M., et al., Trichostatin A and trapoxin: novel chemical probes for the role of histone acetylation in chromatin structure and function. Bioessays 17: 423-430 (1995). 4. Minucci, S., et al., A histone deacetylase inhibitor potentiates retinoid receptor action in embryonal carcinoma cells. PNAS USA 94: 11,295-11,300 (1997). 5. Brehm, A., et al., Retinoblastoma protein recruits histone deacetylase to repress transcription. Nature 391: 597-601 (1998). 6. Sowa, R., et al., Histone deacetylase inhibitor activates the WAF1/Cip1 gene promoter through the Sp1 sites Biochem. Biophys. Res. Comm. 241: 142-150 (1997). 7. Medina, V., et al., Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): dependence on protein synthesis and synergy with a mitochondrial/cytochrome c-dependent pathway. Cancer Res. 57: 3697-3707 (1997). 8. Kim, M.S., et al., Inhibition of histone deacetylase increases cytotoxicity to anticancer drugs targeting DNA. Cancer Res. 63: 7291-7300 (2003).

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