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H4-K12ac Catalog Number H4202 Lyophilized Store At -20C Or -80C Chemically synthesized histone H4 protein, corresponding to residues within 1-102 of human histone H4, acetylation at K12. H4K12ac is an epigenetic modification to the DNA packaging protein histone H4. It is a mark that indicates the acetylation at the 12th lysine residue of the histone H4 protein. H4K12ac is involved in learning and memory. It is possible that restoring this modification could reduce age

H4-K8ac Catalog Number H4201 Lyophilized Store At -20C Or -80C Chemically synthesized histone H4 protein, corresponding to residues within 1-102 of human histone H4, acetylation at K8. H4K8ac, representing an epigenetic modification to the DNA packaging protein histone H4, is a mark indicating the acetylation at the 8th lysine residue of the histone H4 protein. It has been implicated in the prevalence of malaria.

H4-K16ac Catalog Number H4203 Lyophilized Store At -20C Or -80C Chemically synthesized histone H4 protein, corresponding to residues within 1-102 of human histone H4, acetylation at K16. H4K16ac is an epigenetic modification to the DNA packaging protein Histone H4. It is a mark that indicates the acetylation at the 16th lysine residue of the histone H4 protein. H4K16ac is unusual in that it has both transcriptional activation AND repression activities. The loss of H4K20me3

Types of histone modification Chromatin architecture, nucleosomal positioning, and ultimately access to DNA for gene transcription, is largely controlled by histone proteins. Each nucleosome is made of two identical subunits, each of which contains four histones: H2A, H2B, H3, and H4. Meanwhile, the H1 protein acts as the linker histone to stabilize internucleosomal DNA and does not form part of the nucleosome itself. Histone proteins undergo post-translational modification

H2A-K15Ub Catalog Number H1402 Store at -20C or -80C Chemically synthesized histone H2A protein (1-129,human) with mono-ubiquitination at K15. Histone modifications are associated with distinct transcription states and serve as heritable epigenetic markers for chromatin structure and function. RNF168-mediated ubiquitination of histone H2A Lys13,15 (H2AK13,15ub) at DNA double-strand breaks (DSBs) is crucial for preventing aberrant DNA repair and maintaining genome stability.