The 'epi-genie' is Out of the Bottle: Functional Histone 3 Variants in Human Disease

Fri, 05/11/2012 - 10:26

Discovery of histone variants using highly specific antibodies has led to the emerging notion that alterations in histone modifications and further changes in chromatin structure are induced by exchange of histone variants. Covalent histone modifications and the incorporation of histone variants bring about changes in chromatin structure that in turn alter the gene expression. These modifications can be detected using highly specific antibodies, such as the Epi-Plus™ products from Novus.

Interest in non-allelic histone variants has been renewed, in part because of recent studies of H3 (and other) histone variants. However only in mammals do three non-centromeric histone H3 variants (H3.1, H3.2, and H3.3) exist. Studies have shown that the variants of histone H3 differ primarily in their chromatin deposition patterns and post- translational modifications (1). Additional studies using H3 antibodies have shown that the interplay among deposition of H3 variants likely participates in the functional organization of chromatin. Available literature suggests that dynamic replacement of histone variants plays an important role in genome remodeling during early development and that histone H3 proteins are highly conserved across all eukaryotes and are dynamically modified by post-translational modifications (2). Extreme conservation of known acetylation and methylation sites of lysines and arginines predicts that these post-translational modifications exist across the eukaryotes with canonical chromatin structures (3).

Immunocytochemistry/Immunofluorescence: Histone H3 Immunocytochemistry/Immunofluorescence: Histone H3

In a recent study using Histone H3 antibodies, methylated histone (H3) expressions in unexplained recurrent spontaneous abortion (URSA) and normal early pregnancy was found to be significantly lower (P < 0.0001) in URSA tissues than in controls as determined by immunohistochemistry and western blotting using Histone H3 antibodies (4), suggesting that methylation may cause URSA indicating the need for further work to explore the role of methylation in various disorders including cancer. Novus Biologicals offers a wide variety of study tools including antibodies, lysates, proteins and peptides for your research needs.

  1. PMID: 16212490
  2. PMID: 21998593
  3. PMID: 21910587
  4. PMID: 21606120

Novus Biologicals offers Histone H3 reagents for your research needs including:

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