A large number of the proteins on our antibody database at Novus Biologicals are involved in the posttranslational modification of histones, allowing a diverse number of functions to occur. Myc antibody studies have shown Myc (c-Myc) to have a dual function, being a transcription factor which also regulates histone acetylation.
The N-terminal of core histone proteins can be modified in a number of ways to effect a diverse number of outcomes . For example, transcriptional activation is associated with acetylation by histone acetyl-transferases (HATs), at various lysine positions. The resultant remodelling of the nucleosome, into a more open structure, allows easier access by transcription complexes.
Myc is thought to regulate transcription of around 15% of all genes, and in recent years has also be shown to play an important role in histone acetylation. In 2001, S.R. Frank et al. used ChIP-grade Myc antibody products to study changes in Myc-induced HAT acetylation at seven gene loci, in fibroblast cells. The results suggested that Myc played an indirect role in H4 acetylation, but was insufficient for transcriptional activation to occur.
In recent years, further Myc antibody ChIP studies have clarified the role Myc plays in histone acetylation. It is known that Myc recruits H3/H4 HAT enzymes, locally promoting hyper-acetylation of multiple lysines. However, the mechanism of action and lysines targeted remain unclear.
In 2008, Martinato et al published Myc antibody research identifying at least eight binding sites on H2, 3 and 4 where Myc-induced hyper-acetylation occurs. Based on results from the HATs Tip60 and MYST2, plus other data, it was surmised Myc achieves coordinated histone acetylation at multiple activated promoter sites, by recruiting the Tip60/p400 complex. Tip60, MYST2 and p400 can all be found on our antibody database.
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