Anti-Histone Deacetylase 10 (HDAC10) antibody produced in rabbit

Histone deacetylase 10 (HDAC10) is highly expressed in liver, kidney, pancreas and spleen. HDAC10 is similar to HDAC6, both containing a unique putative second catalytic domain not found in other HDACs. HDAC10 is localized to both the nucleus and cytoplasm. Histone deacetylases (HDACs) are competing enzymes, belonging to histone deacetylase family. HDAC10 is a novel member of the class II family of HDACs with a bipartite structure consisting of Hda1p-related catalytic domain at the N-terminal and a leucine-rich domain at the C-terminal. It is present, both in the nucleas and cytoplasm.

synthetic peptide corresponding to amino acid residues 2-16 of human HDAC10 with C-terminal added cysteine, conjugated to KLH.

Anti-Histone Deacetylase 10 (HDAC10) antibody produced in rabbit has been used in western blot analysis and immunofluorescence.

Histone deacetylase 10 (HDAC10) can deacetylate histones, repress transcription and interact with HDAC3. HDAC10 can stimulate lung cancer proliferation via AKT phosphorylation. It is involved in homologous recombination.

The leucine-rich domain on the C-terminal of HDAC8 is responsible for cytoplasmic enrichment. Trichostatin A (TSA), a specific antitumor deacetylase inhibitor is sensitive to the enzymatic activity of HDAC10. HDAC10 attaches to a promoter and represses transcription in the nucleas.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

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