Histone H4 unphosphorylated (Tyr-72)
€155.00
In stock
SKU
ECM-HX5565
Background:
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.
Background References
Jaskelioff, M. & Peterson, C.L. (2003) Nat Cell Biol. 5:395.
Chou, R.H. et al. (2014) Developmental Cell 30:224.
Sequence: Unphosphorylated Histone H4 (Tyr-72) synthetic peptide corresponding to amino acids surrounding Tyr-72 in human histone H4. This site is well conserved in rat and mouse histone H4, but the site is not found in other histone family members.
Specificity: The peptide is an unphosphorylated control peptide for HX5555. The peptide is recommended for use in ELISA and for blocking antibody reactivity in western blot and immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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.
Background References
Jaskelioff, M. & Peterson, C.L. (2003) Nat Cell Biol. 5:395.
Chou, R.H. et al. (2014) Developmental Cell 30:224.
Sequence: Unphosphorylated Histone H4 (Tyr-72) synthetic peptide corresponding to amino acids surrounding Tyr-72 in human histone H4. This site is well conserved in rat and mouse histone H4, but the site is not found in other histone family members.
Specificity: The peptide is an unphosphorylated control peptide for HX5555. The peptide is recommended for use in ELISA and for blocking antibody reactivity in western blot and immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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