unphosphorylated Histone H4 (Tyr-72) Peptide

Chromatin structure is regulated through the activity of core histones (H2A, H2B, H3, and H4) that form the nucleosome. Histone activity is regulated by a variety of post-translational modifications, including acetylation, phosphorylation, and methylation. Histone acetylation and methylation occur primarily at lysine (K) residues in the amino-terminal tail domain. These modifications are important for the regulation of histone deposition, transcriptional activation, DNA replication and repair. Acetylation and methylation of specific lysine residues creates docking sites for DNA repair, transcription, and chromatin regulatory proteins. Methylation of histones may be regulated by phosphorylation events at sites downstream of the N-terminal tail. In histone H4, both EGFR activation and inonizing radiation induce EGFR nuclear translocation and Histone H4 (Tyr-72) phosphorylation, which creates a docking site for Set8 methyltransferase. This promotes K20 methylation in Histone H4 leading to DNA synthesis and repair.

References

*For more information, see UniProt Accession P62805

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