Background

Histone acetylation and deacetylation, catalyzed by multisubunit complexes, play a key role in the regulation of eukaryotic gene expression. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex. It also interacts with retinoblastoma tumor-suppressor protein and this complex is a key element in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2, it deacetylates p53 and modulates its effect on cell growth and apoptosis.

Images

Western blotting analysis using anti-HDAC1 antibody (Cat#64955). Total cell lysates (20 μg) from various cell lines were loaded and separated by SDS-PAGE. The blot was incubated with anti-HDAC1 antibody (Cat#64955, 1:2,500) and HRP-conjugated goat anti-rabbit secondary antibody (Cat#201, 1:20,000) respectively. Image was developed using NaQ™ ECL Substrate Kit (Cat#716).

Western blotting analysis using anti-HDAC1 antibody (Cat#64955). HDAC1 expression in wild-type (WT) and HDAC1 shRNA knockdown (KD) HeLa cells with 20 μg of total cell lysates. Hsp90 α serves as a loading control. The blot was incubated with anti-HDAC1 antibody (Cat#64955, 1:2,500) and HRP-conjugated goat anti-rabbit secondary antibody (Cat#201, 1:20,000) respectively. Image was developed using NaQ™ ECL Substrate Kit (Cat#716).

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