Histone H2A (Xenopus, recombinant)

Histone H2A is a core histone that forms a dimer with histone H2B.¹ Two histone H2A/H2B dimers form an octameric nucleosome with a histone H3/H4 tetramer, around which DNA wraps, allowing it to be condensed. Histone H2A can be post-translationally modified via methylation of the arginine at position 3 by protein arginine methyltransferase 1 (PRMT1), PRMT5, or PRMT6, which is associated with both transcriptional activation and repression.² When methylated by PRMT7, it is associated with DNA damage repair. The arginine residue at position 3 of histone H2A is also subject to citrullination by protein arginine deiminase 4 (PAD4). Histone H2A is ubiquitinated by ubiquitin-specific protease 12 (USP12) during the gastrula stage of Xenopus development.³ The post-translational modifications on histone H2A vary between each stage of Xenopus development and are enriched on nucleosomes in Xenopus embryos that contain both active and repressive histone modifications.⁴ Cayman’s Histone H2A (Xenopus, recombinant) protein can be used as a substrate for enzyme activity assays, as well as for Western blot (WB) applications.

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1. Eickbush, T.H., and Moudrianakis, E.N. The histone core complex: An octamer assembled by two sets of protein-protein interactions. Biochemistry 17(23), 4955-4964 (1978).

2. Fuhrmann, J., and Thompson, P.R. Protein arginine methylation and citrullination in epigenetic regulation. ACS Chem. Biol. 11(3), 654-668 (2016).

3. Joo, H.-Y., Jones, A., Yang, C., et al. Regulation of histone H2A and H2B deubiquitination and Xenopus development by USP12 and USP46. The Journal of Biological Chemisty 286(9), 7190-7201 (2011).

4. Wang, W.-L., Anderson, L.C., Nicklay, J.J., et al. Phosphorylation and arginine methylation mark histone H2A prior to deposition during Xenopus laevis development. Epigenetics Chromatin 7, 22 (2014).