Other Proteins

Histone phosphorylation is a post-translational modification (PTM) wherein a phosphate group is added to a histone protein, predominantly occurring on serine, threonine, and tyrosine residues. In combination with other PTMs, histone phosphorylation constitutes the “histone code,” acting as a language read by proteins to regulate chromatin structure and gene expression. Histone phosphorylation is involved in chromatin remodeling and compaction associated with diverse cellular processes, including DNA damage repair, transcription regulation, cell division, and apoptosis [1]. Recombinant mononucleosomes containing phosphorylated histones can be used to study the biological functions of histone phosphorylation. H3T11phos (histone H3 threonine 11 phosphorylation) Recombinant Nucleosome, Biotinylated consists of 147 base pairs of DNA wrapped around an octamer of core histone proteins (two each of H2A, H2B, H3.2, and H4) to form a nucleosome, the basic repeating unit of chromatin. The 147 b

Histone phosphorylation is a post-translational modification (PTM) wherein a phosphate group is added to a histone protein, predominantly occurring on serine, threonine, and tyrosine residues. In combination with other PTMs, histone phosphorylation constitutes the “histone code,” acting as a language read by proteins to regulate chromatin structure and gene expression. Histone phosphorylation is involved in chromatin remodeling and compaction associated with diverse cellular processes, including DNA damage repair, transcription regulation, cell division, and apoptosis [1]. Histone phosphorylation is also observed on non-canonical histones, particularly H3.3, where it plays roles in transcriptional regulation. Recombinant mononucleosomes containing phosphorylated histones can be used to study the biological functions of histone phosphorylation. H3.3S31phos,K36me3 (histone H3.3 serine 31 phosphorylation, lysine 36 trimethylation) Recombinant Nucleosome, Biotinylated consists of 147 base

Heterotypic nucleosomes, also referred to as “asymmetric nucleosomes,” contain sister histones with distinct histone variants and/or post-translational modifications (PTMs). In homotypic nucleosomes, or “symmetric nucleosomes,” each pair of sister histones bears the same PTM, set of PTMs, or histone variant. Histone-modifying enzymes, chromatin remodelers, and histone chaperones differentially modify sister histones or exchange unique histone variants to form heterotypic nucleosomes. Heterotypic nucleosomes have been found at promoters of developmental genes in undifferentiated embryonic stem cells and transcription start sites (TSSs) of approximately half of the genes in budding yeast [1]. Heterotypic nucleosomes represent an additional layer of the histone code, acting as substrates for multivalent reader proteins, participating in PTM crosstalk mechanisms, and influencing reader protein binding affinity through varying local target concentration. Recombinant heterotypic nucleosomes

Heterotypic nucleosomes, also referred to as “asymmetric nucleosomes,” contain sister histones with distinct histone variants and/or post-translational modifications (PTMs). In homotypic nucleosomes, or “symmetric nucleosomes,” each pair of sister histones bears the same PTM, set of PTMs, or histone variant. Histone-modifying enzymes, chromatin remodelers, and histone chaperones differentially modify sister histones or exchange unique histone variants to form heterotypic nucleosomes. Heterotypic nucleosomes have been found at promoters of developmental genes in undifferentiated embryonic stem cells and transcription start sites (TSSs) of approximately half of the genes in budding yeast [1]. Heterotypic nucleosomes represent an additional layer of the histone code, acting as substrates for multivalent reader proteins, participating in PTM crosstalk mechanisms, and influencing reader protein binding affinity through varying local target concentration. Recombinant heterotypic nucleosomes

Heterotypic nucleosomes, also referred to as “asymmetric nucleosomes,” contain sister histones with distinct histone variants and/or post-translational modifications (PTMs). In homotypic nucleosomes, or “symmetric nucleosomes,” each pair of sister histones bears the same PTM, set of PTMs, or histone variant. Histone-modifying enzymes, chromatin remodelers, and histone chaperones differentially modify sister histones or exchange unique histone variants to form heterotypic nucleosomes. Heterotypic nucleosomes have been found at promoters of developmental genes in undifferentiated embryonic stem cells and transcription start sites (TSSs) of approximately half of the genes in budding yeast [1]. Heterotypic nucleosomes represent an additional layer of the histone code, acting as substrates for multivalent reader proteins, participating in PTM crosstalk mechanisms, and influencing reader protein binding affinity through varying local target concentration. Recombinant heterotypic nucleosomes

Heterotypic nucleosomes, also referred to as “asymmetric nucleosomes,” contain sister histones with distinct histone variants and/or post-translational modifications (PTMs). In homotypic nucleosomes, or “symmetric nucleosomes,” each pair of sister histones bears the same PTM, set of PTMs, or histone variant. Histone-modifying enzymes, chromatin remodelers, and histone chaperones differentially modify sister histones or exchange unique histone variants to form heterotypic nucleosomes. Heterotypic nucleosomes have been found at promoters of developmental genes in undifferentiated embryonic stem cells and transcription start sites (TSSs) of approximately half of the genes in budding yeast [1]. Heterotypic nucleosomes represent an additional layer of the histone code, acting as substrates for multivalent reader proteins, participating in PTM crosstalk mechanisms, and influencing reader protein binding affinity through varying local target concentration. Recombinant heterotypic nucleosomes

Heterotypic nucleosomes, also referred to as “asymmetric nucleosomes,” contain sister histones with distinct histone variants and/or post-translational modifications (PTMs). In homotypic nucleosomes, or “symmetric nucleosomes,” each pair of sister histones bears the same PTM, set of PTMs, or histone variant. Histone-modifying enzymes, chromatin remodelers, and histone chaperones differentially modify sister histones or exchange unique histone variants to form heterotypic nucleosomes. Heterotypic nucleosomes have been found at promoters of developmental genes in undifferentiated embryonic stem cells and transcription start sites (TSSs) of approximately half of the genes in budding yeast [1]. Heterotypic nucleosomes represent an additional layer of the histone code, acting as substrates for multivalent reader proteins, participating in PTM crosstalk mechanisms, and influencing reader protein binding affinity through varying local target concentration. Recombinant heterotypic nucleosomes

The acidic patch is a negatively charged region of the nucleosome surface that serves as a conserved interaction hub for neighboring nucleosomes and chromatin binding proteins, often via salt bridges with arginine anchors [1]. The acidic patch plays a critical role in chromatin condensation and chromatin remodeling [1-3]. Recombinant mononucleosomes containing acidic patch mutations can be used to study the biological functions of the acidic patch. H2AE61A Recombinant Nucleosome with Linker DNA consists of 199 base pairs of DNA wrapped around an octamer core of histone proteins (two each of H2A, H2B, H3.1, and H4) to form a nucleosome, the basic repeating unit of chromatin. The 5’ biotin-TEG DNA consists of a core 147 bp 601 nucleosome assembly sequence [4] flanked by 26 bp linker sequences as underlined below. Histone H2A contains a glutamate-to-alanine (E-to-A) substitution within the acidic patch at position 61 (H2AE61A). H2AE61 resides in the alpha2 helix, forming a key salt bridg

The acidic patch is a negatively charged region of the nucleosome surface that serves as a conserved interaction hub for neighboring nucleosomes and chromatin binding proteins, often via salt bridges with arginine anchors [1]. The acidic patch plays a critical role in chromatin condensation and chromatin remodeling [1-3]. Recombinant mononucleosomes containing acidic patch mutations can be used to study the biological functions of the acidic patch. H2AE92K Recombinant Nucleosome with Linker DNA consists of 199 base pairs of DNA wrapped around an octamer core of histone proteins (two each of H2A, H2B, H3.1, and H4) to form a nucleosome, the basic repeating unit of chromatin. The 5’ biotin-TEG DNA consists of a core 147 bp 601 nucleosome assembly sequence [4] flanked by 26 bp linker sequences as underlined below. Histone H2A contains a glutamate-to-lysine (E-to-K) substitution at position 92 (H2AE92K). H2AE92 resides in the H2A C-terminal extension and mediates chromatin binding with fa