HDAC8 (human, recombinant)

Histone deacetylase 8 (HDAC8) is a class I HDAC that catalyzes the zinc-dependent deacetylation of core histones. It is composed of a single alpha/beta domain with an N-terminal deacetylase active site, which can be disrupted by phosphorylation of a proximal serine. HDAC8 is ubiquitously expressed in human tissues and, unlike most other HDACs, is localized to both the cytosol and nucleus. It associates with other proteins and transcription factors to regulate gene expression. HDAC8 has a flexible active site that can deacetylate lysines from both histone tails and cytosolic proteins. It deacetylates pyruvate kinase M2 (PKM2), inducing its relocalization to the nucleus where it binds beta-catenin and promotes cyclin D1 expression and cell cycle progression in HepG2 hepatocellular carcinoma (HCC) cells. HDAC8 associates with RUNX family transcription factor 1 (RUNX1) and suppresses the expression of RUNX1-regulated genes, which code for proteins involved in cytokine expression, cell differentiation, cell cycle progression, and tumor suppression, in COS-7 cells. Inhibition of HDAC8 decreases tumor volume and increases intratumoral apoptosis without reducing body weight in a neuroblastoma mouse xenograft model. Cayman's HDAC8 (human, recombinant) protein can be used for enzyme activity assay and Western blot applications.Synonyms: Histone Deacetylase 8. Purity: >80% estimated by SDS-PAGE. Source: Active recombinant C-terminal His-tag expressed in E. coli. Amino Acids: 2-377 (full length). MW: 45.3 kDa. Formulation: (Request formulation change), 50 mM Tris, pH 7.5, with 200 mM NaCl, 2.5 mM potassium chloride, 1 mM TCEP, and 25% glycerol. UniProt Accession #: Q9BY41.