HDAC7 is a member of the class II mammalian histone deacetylases, which plays an important role in modulating the eukaryotic chromatin structure. Human HDAC7 is composed of 912 amino acid residues. Although HDAC7 is localized mostly to the cell nucleus, it is also found in the cytoplasm, suggesting nucleo-cytoplasmic shuttling. The histone deacetylase activity of HDAC7 maps to a carboxy-terminal domain and is dependent on interaction with class I HDACs in the nucleus. It is an active component of different transcriptional corepressor complexes that can be recruited to specific promoter regions via interactions with a growing number of sequence specific transcriptional factors. HDAC7 catalyzes removal of acetyl-groups from acetyl-lysines of histones and promotes compaction of chromatin in these regions, leading to the inhibition of gene transcription. Anti-HDAC7 antibodies are ideal for researches interested in Breast Cancer, Cancer, Cell Cycle and Replication, Chromatin Research, Epigenetics, and Histone Deacetylases research.
HDAC7 affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to the N terminal region of human HDAC7.