HDAC8 (human, recombinant)

Histone deacetylase 8 (HDAC8) is a class I HDAC that catalyzes the zinc-dependent deacetylation of core histones.^1,2 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.³ HDAC8 is ubiquitously expressed in human tissues and, unlike most other HDACs, is localized to both the cytosol and nucleus.⁴ 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.³ 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.⁵ 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.⁶ Inhibition of HDAC8 decreases tumor volume and increases intratumoral apoptosis without reducing body weight in a neuroblastoma mouse xenograft model.⁷ Cayman’s HDAC8 (human, recombinant) protein can be used for enzyme activity assay and Western blot applications.

WARNING This product is not for human or veterinary use.

1. Lin, H.Y., Chen, C.S., Lin, S.P., et al. Targeting histone deacetylase in cancer therapy. Med. Res. Rev. 26(4), 397-413 (2006).

2. Huang, L. Targeting histone deacetylases for the treatment of cancer and inflammatory diseases. J. Cell. Physiol. 209(3), 611-616 (2006).

3. Somoza, J.R., Skene, R.J., Katz, B.A., et al. Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases. Structure 12(7), 1325-1334 (2004).

4. Xia, J.-K., Qin, X.-Q., Zhang, L., et al. Roles and regulation of histone acetylation in hepatocellular carcinoma. Front. Genet. 13, 982222 (2022).

5. Zhang, R., Shen, M., Wu, C., et al. HDAC8-dependent deacetylation of PKM2 directs nuclear localization and glycolysis to promote proliferation in hepatocellular carcinoma. Cell Death Dis. 11(12), 1036 (2020).

6. Durst, K.L., Lutterbach, B., Kummalue, T., et al. The inv(16) fusion protein associates with corepressors via a smooth muscle myosin heavy-chain domain. Mol. Cell Biol. 23(2), 607-619 (2003).

7. Rettig, I., Koeneke, E., Trippel, F., et al. Selective inhibition of HDAC8 decreases neuroblastoma growth in vitro and in vivo and enhances retinoic acid-mediated differentiation. Cell Death Dis. 6(2), e1657 (2015).