AnaSpec, the largest provider of on-demand GO peptides has introduced a wide selection of Histone H1, H2A, H2B, H3 and H4 peptides, especially the H3 peptides. The rapidly expanding Histone H3 GO Peptides include sequences that are acetylated, mono-, di- or tri-methylated, phosphorylated and biotinylated.
Chromatin exist either as the transcriptionally active euchromatin or as the transcriptionally repressed heterchromatin state.1 Post-translational modifications of histone “tails” (amino termini) have been implicated in the conversion between the two states. 1-2 Covalent modifications, such as acetylation, methylation and phosphorylation affect chromatin structure and exquisitely regulate gene expression.3-6 Histone hyperacetylation is correlated with increased transcription, whereas hypoacetylation correlates with transcriptional repression.5 In Histone H3, preferential methylation sites have been shown to be Lys4, Lys9, Lys27 and Lys36, with methylation generally leading to transcriptional suppression. 3,7 Methylation of specific arginine residues in H3 has been shown to correlate with cell fate and potency.8 Phosphorylation at Ser10 (pSer10) is implicated in both transcription and cell division.9
References:
1. Grunstein, M. et al. J. Cell Sci. Suppl. 19, 29 (1995).
2. Strahl, BR and CD Allis, Nature 403, 41 (2000).
3. Strahl, BD. et al. Proc. Natl. Acad. Sci. 96, 14967 (1999).
4. Jenuwein, T. and CD. Allis Science 293, 1074 (2001).
5. Sterner, DE. et al. Microbiol. Mol. Biol. Rev. 64, 435 (2000).
6. Lachner, M. et al. J. Cell Sci. 116, 2117 (2003).
7. Nishioka, K. et al. Genes & Dev. 16, 479 (2002).
8. Torres-Padilla, M-E. et al. Nature 445, 214 (2007).
9. Prigent, C. and S. Dimitrov, J. Cell Sci. 116, 3677 (2003).
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