Anti-CHD3/Mi-2a: Mouse CHD3/Mi-2a Antibody

CHD proteins are characterized by the presence of two tandemly arranged chromodomains. The mammalian CHD family has nine members. The CHD3(Mi-2a)/CHD4 (Mi-2b) subfamily is characterized by the presence of a pair of PHD fingers preceding the chromodomains. These proteins exist in multisubunit complexes with nucleosome remodeling and deacetylation (NuRD) activity. In addition to Chd3 or Chd4, NuRD complexes contain histone deacetylase 1 (HDAC1) and HDAC2, the histone binding proteins RbAp46 and RbAp48, proteins of the MTA and p66 families (MTA1, MTA2, or MTA3 and p66 or p66β), and subunits with methylated DNA binding domains (MBD3). As part of complex, CHD3 directly interacts with HDAC1 and 2, ATR, and TRIM27. It has been suggested that these complexes couple ATP-dependent chromatin remodeling and deacetylation to effect transcriptional repression. However, several studies also implicate a function of CHD3 family members in transcriptional activation.² Complexes related to NuRD exist in Drosophila melanogaster and Caenorhabditis elegans and play important roles during differentiation and cell fate determination. This function is conserved in mammals: an MTA3-containing NuRD complex regulates B-lymphocyte differentiation and is indispensable for BCL-6-mediated repression of plasma cell-specific genes in B lymphocytes. Two different modes of targeting NuRD complexes have been suggested. First, recruitment via interaction with DNA bound transcriptional repressors, such as BCL-6, Hunchback, or Tramtrack 69. Second, direct binding of stoichiometric (MBD3) or associated (MBD2A) MBD proteins to methylated DNA.³ Furthmore, CK2 phosphorylation is a common feature of CHD family ATPases.⁴ CHD proteins play important role in the regulation of gene expression, recombinantion, genome organization, and chromatin structure, as well as their potential activity in RNA processing. In addition, CHD proteins are also implicated in human disease.