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H4-K20me2 Catalog Number H4101 Lyophilized Store At -20C Or -80C Chemically synthesized histone H4 protein, corresponding to residues within 1-102 of human histone H4, dimethylation at K20. Histone modifications are associated with distinct transcription states and serve as heritable epigenetic markers for chromatin structure and function. H4K20me2 is the most common methylation state on histone H4 and was one of the earliest modified histone residues to be identified back

Human Histone H4,Catalog Number: KS151002,Molecular Weight:1683

H4 Catalog Number H4100 Lyophilized Store At -20C Or -80C This product is an expressed human H4 protein composed of 102 amino acids. Histone H4 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H4 is involved with the structure of the nucleosome of the 'beads on a string' organization. Histone H4 is an important protein in the structure and function of chromatin,

H4-K5ac Catalog Number H4205 Lyophilized Store At -20C Or -80C Chemically synthesized histone H4 protein, corresponding to residues within 1-102 of human histone H4, acetylation at K5. H4K5 is acetylated by TIP60 and CBP/p300 proteins. CAP/p300 open transcriptional start site chromatin by acetylating histones. H4K5ac has also been implicated in epigenetic bookmarking which allows gene expression patterns to be faithfully passed to daughter cells through mitosis. Important

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-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

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-K20ac Catalog Number H4204 Lyophilized Store At -20C Or -80C Chemically synthesized histone H4 protein, corresponding to residues within 1-102 of human histone H4, acetylation at K20. Histone modifications are associated with distinct transcription states and serve as heritable epigenetic markers for chromatin structure and function. H4K20ac is associated with gene repression in human cells. Unlike H3K9me3, a constitutive heterochromatin mark, H4K20ac was less associated

H3K4me2 Catalog Number H3102 Lyophilized Store At -20C Or -80C Chemically synthesized histone H3 protein, corresponding to residues within 1-135 of human histone H3, dimethylation at K4. H3K4me2 is a modification thought to have a role in transcriptional memory. In CD4+ T lymphocytes, H3K4Me2 is present within gene bodies regulating cellular function, but not in those of housekeeping genes, which indicates that the modification has a role in refining the tissue-specificity

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