Antibodies to Histone Modifying Enzymes

Regulation of gene expression is mediated by several mechanisms including DNA methylation, ATP-dependent chromatin remodeling, and posttranslational modifications of histones. One of the major modifications of histones consists of the dynamic acetylation and deacetylation of ε-amino groups of lysine residues present in the tail of core histones.1 The enzymes responsible for this reversible acetylation/deacetylation process are histone acetyltransferases (HATs) and histone deacetylases (HDACs), respectively.2 While HATs act as transcriptional coactivators, HDACs are part of transcriptional corepressor complexes.3

Mammalian HDACs can be divided into three classes according to sequence homology.4 Class I consists of the yeast Rpd3-like proteins HDAC1, HDAC2, HDAC3 and HDAC8. Class II consists of the yeast Hda1-like proteins HDAC4, HDAC5, HDAC6, HDAC7, HDAC9 and HDAC10.5 Class III comprises the yeast Sir2-like proteins. Whereas class I HDACs are ubiquitously expressed, most class II HDACs are tissue-specific. Sir2 is an NAD-dependent histone deacetylase that appears to play an important role in chromatin silencing and life span prolongation through calorie restriction.6

Sigma® has a wide selection of antibodies to many of the histone modifying enzymes. The antibodies are carefully tested to provide high quality performance. These antibodies are valuable tools for scientists working on chromatin remodeling.

Immunohistology of anti-HDAC-1, -2 and -3 on human lymph node

Figure 1. Immunohistology of anti-HDAC-1, -2 and -3 on human lymph node


Immunoblotting using Anti-Histone Deacetylase (HDAC) -1, -2 and -3

Figure 2. Immunoblotting using Anti-Histone Deacetylase (HDAC) -1, -2 and -3


Immunoblotting using Anti-HAT1.

Figure 3. Immunoblotting using Anti-HAT1


Immunoblotting using Anti-Histone Deacetylase 4

Figure 4. Immunoblotting using Anti-Histone Deacetylase 4


Immunoblotting using Anti-Sir2

Figure 5. Immunoblotting using Anti-Sir2




  1. Wang, A.H., et al. Mol. Cell. Biol.19, 7816-7827 (1999).
  2. Grozinger, C.M. et al. Proc. Natl. Acad. Sci. USA96, 4868-4873 (1999).
  3. Fischle, W., et al. Biochem. Cell Biol.79, 337 (2001).
  4. Khochbin, S., et al. Curr. Opin. Genet. Dev.11, 162-166 (2001).
  5. Fischle, W., et al. J. Biol. Chem.274, 11713-11720 (1999).