Formulation: 50 mM Tris, pH 7.5, with 200 mM NaCl, 2.5 mM potassium chloride, 1 mM TCEP, and 25% glycerol
Purity: ≥80% estimated by SDS-PAGE
Shelf life (days): 180
Notes: Histone deacetylase 8 (HDAC8) is a class I HDAC that catalyzes the zinc-dependent deacetylation of core histones.{14467,14468} It is composed of a single α/β domain with an N-terminal deacetylase active site, which can be disrupted by phosphorylation of a proximal serine.{66421} HDAC8 is ubiquitously expressed in human tissues and, unlike most other HDACs, is localized to both the cytosol and nucleus.{66422} 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.{66421} It deacetylates pyruvate kinase M2 (PKM2), inducing its relocalization to the nucleus where it binds β-catenin and promotes cyclin D1 expression and cell cycle progression in HepG2 hepatocellular carcinoma (HCC) cells.{66423} 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.{66424} Inhibition of HDAC8 decreases tumor volume and increases intratumoral apoptosis without reducing body weight in a neuroblastoma mouse xenograft model.{66426} Cayman’s HDAC8 (human, recombinant) protein can be used for enzyme activity assay and Western blot applications.
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