More than 130 suppliers
ISO certified
In-house tech support
we Connect you
Bio-Connect
ProductsBack/Splitomicin
Chemical Structure
Chemical Structure
Chemical Structure

Splitomicin

Research Use Only
AG-CR1-0088
AdipoGen Life Sciences
Estimated Purity>98%
DownloadMSDS
Product group Chemicals
Molecular Weight198.2
Sign in to order and to see your custom pricing.
Large volume orders?
Order with a bulk request
More than 130 suppliers
ISO certified
In-house tech support

Overview

  • Supplier
    AdipoGen Life Sciences
  • Product Name
    Splitomicin
  • Delivery Days Customer
    10
  • Certification
    Research Use Only
  • Estimated Purity
    >98%
  • Molecular Formula
    C13H10O2
  • Molecular Weight
    198.2
  • Scientific Description
    Chemical. CAS: 5690-03-9. Formula: C13H10O2. MW: 198.2. Potent cell permeable and selective inhibitor of yeast NAD+-dependent histone deacetylase (HDAC) Sir2p. Displays higher activity in vivo than in vitro. Sensitizes mammalian cells to a variety of DNA-damaging agents by abrogating Sir2p activity on p53. Acts by either altering or blocking access to the acetylated histone binding pocket. Shown to have diverse effects also in mammalian cells. - Potent cell permeable and selective inhibitor of yeast NAD+-dependent histone deacetylase (HDAC) Sir2p [1-4]. Displays higher activity in vivo than in vitro [1-4]. Sensitizes mammalian cells to a variety of DNA-damaging agents by abrogating Sir2p activity on p53. Acts by either altering or blocking access to the acetylated histone binding pocket [5]. Shown to have diverse effects also in mammalian cells [6-10].
  • SMILES
    O=C1CCC2=C(O1)C=CC1=CC=CC=C21
  • Storage Instruction
    -20°C,2°C to 8°C
  • UNSPSC
    12352200

References

  • Identification of a small molecule inhibitor of Sir2p: A. Bedalov, et al.; PNAS 98, 15113 (2001)
  • Identification of selective inhibitors of NAD+-dependent deacetylases using phenotypic screens in yeast: M. Hirao, et al.; J. Biol. Chem. 278, 52773 (2003)
  • Inhibitors of Sir2: evaluation of splitomicin analogues: J. Posakony, et al.; J. Med. Chem. 47, 2635 (2004)
  • The Sir 2 family of protein deacetylases: J.M. Denu; Curr. Opin. Chem. Biol. 9, 431 (2005) (Review)
  • Histone deacetylase inhibitor-mediated radiosensitization of human cancer cells: class differences and the potential influence of p53: I.A. Kim, et al.; Clin. Cancer Res. 12, 940 (2006)
  • SIRT1 inhibition alleviates gene silencing in Fragile X mental retardation syndrome: R. Biacsi, et al.; PLoS Genet. 4, e1000017 (2008)
  • Splitomicin suppresses human platelet aggregation via inhibition of cyclic AMP phosphodiesterase and intracellular Ca++ release: F.C. Liu, et al.; Thromb. Res. 124, 199 (2009)
  • Reciprocal roles of SIRT1 and SKIP in the regulation of RAR activity: implication in the retinoic acid-induced neuronal differentiation of P19 cells: M.R. Kang, et al.; Nucleic Acids Res. 38, 822 (2010)
  • Sirt1 inhibition promotes in vivo arterial thrombosis and tissue factor expression in stimulated cells: A. Breitenstein, et al.; Cardiovasc. Res. 89, 464 (2011)
  • Sirtuin-1 targeting promotes Foxp3+ T-regulatory cell function and prolongs allograft survival: U.H. Beier, et al.; Mol. Cell Biol. 31, 1022 (2011)