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H3-K36me3 Catalog Number H3112 Lyophilized Store At -20C Or -80C Chemically synthesized histone H3 protein, corresponding to residues within 1-135 of human histone H3, trimethylation at K36. H3K36me3 can bind chromodomain proteins such as MSL3 hMRG15 and scEaf3. It can bind PWWP proteins such as BRPF1 DNMT3A, HDGF2 and Tudor domains such as PHF19 and PHF1. H3K36me3 is required for homologous recombinational repair of DNA damage such as double-strand breaks. The trimethylati

H3-K36me3 Catalog Number H3113 Lyophilized Store At -20C Or -80C Chemically synthesized histone H3 protein, corresponding to residues within 1-135 of human histone H3, Asymmetric dimethylation at R42. Histone modifications are associated with distinct transcription states and serve as heritable epigenetic markers for chromatin structure and function. H3R42me2a is a histone modification with positive transcriptional effects. Nucleosomes containing H3R42me2a can stimulate

H3-K27me1 Catalog Number H3107 Lyophilized Store At -20C Or -80C Chemically synthesized histone H3 protein, corresponding to residues within 1-135 of human histone H3, monomethylation at K27. H3K27me1 is linked to promotion of transcription and is seen to accumulate in transcribed genes. Histone-histone interactions play a role in this process. Regulation occurs via Setd2-dependent H3K36me3 deposition. H3K27me1 shows an inverse distribution to H3K27me3 that defines the

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