The peptide is histone H4 (1-25), acetylated at Lys12 and Lys16, trimethylated at Lys20, then C-terminal GSGS linker and biotinylated Lys. The trimethylation of histone H4 at Lys20 is catalyzed by Suv4-20 and is involved in transcriptional silencing and heterochromatin formation in eukaryotes. Studies have shown that histone H4 is first acetylated at Lys16 and then preferentially acetylated at Lys12. Diacetylated histone H4 has been shown to bind to the inhibitory protein TUP1. The acetylation of histone H4 also regulates the formation of heterochromatin by promoting the binding of bromouracil to p300 and the transcription factor TAFII250 and inhibiting the interaction with SIR3. When the peptide purity is greater than 95%, the peptide is dissolved in distilled water at a concentration of 1 mg/ml, and lyophilized again into a powder form.
Hemann, M. and M. Narita. Gene Dev 21, 1 (2007); Carmen, A. et al. J Biol Chem 277, 4778 (2002); Turner, B. et al. FEBS Lett 252, 141 (1989).