Histone H2A combines with Histone H2B to form the H2A-H2B heterodimer. Two H2A/H2B heterodimers interact with an H3/H4 tetramer to form the histone octamer. (1,2) Histone H2A is also modified by various enzymes and can act as a substrate for them. These modifications have been shown to be important in gene reg4ation.
- New England Biolabs
Histone H1 Human, Recombinant
Histone H1 acts on the linker region of polynucleosome DNA to condense the chromatin into structures of ~30 nm (1). It is not necessary for octamer or nucleosome core particle formation. Eight different Histone H1 proteins have been identified in the human genome (2). Histone H10 is a non replication-dependent histone that is highly expressed […]
EpiMark™ Nucleosome Assembly Kit
The EpiMark™ Nucleosome Assembly Kit is used to make unmodified recombinant human nucleosomes with user-supplied DNA or the provided control DNA. Purified recombinant human Histone H2A/H2B Dimer and Histone H3.1/H4 Tetramer are mixed with DNA at 2 M NaCl. To generate nucleosomes, the salt concentration is lowered by dilution or dialysis allowing each histone tetramer […]
SET7 Methyltransferase
SET7 Methyltransferase methylates lysine 4 (Lys 4) of histone H3. Methylation occurs at the e amino group of lysine residues. Di- and tri- methylation of histone H3 Lys 4 is a hallmark of transcriptionally active chromatin and is globally distributed.
PRMT1 Methyltransferase
PRMT1 is a major protein arginine methyltransferase. It specifically methylates arginine 3 (Arg 3) of H4 in vitro and in vivo. Furthermore, methylation of histone H4 at Arg 3 facilitates transcriptional activation by nuclear hormone receptor. Ordered cooperative functions of PRMT1, p300 and CARM1 in transcriptional activation by p53 is observed on the GADD45 gene […]