HDAC8 human recombinant

HDAC8 is phosphorylated in vivo by PKA, resulting in decreased activity and hyperacetylation of HDAC8 targets, such as histones H3 and H4. In addition, HDAC8 can also be inhibited by trichostatin A. HDAC8 has been implicated in acute myeloid leukemia.

Human recombinant HDAC8 expressed in E. Coli

~42 kDa

HDAC deacetylase assays

In liquid containing 10 mM Tris, pH 7.5, 100 mM NaCl, 3 mM MgCl2 and 10% glycerol. Frozen solution.

Unit Definition: 1U = 1 pmol/min at 37°C using a standard flourometric activity assay to measure deacetylation activity

Store at -80°C. The enzyme is stable on ice for 30 to 60 min, but may lose activity with dilution and/or prolonged storage on ice. It is recommended that thawing and addition of the enzyme to assay wells be done within as short a time as possible before start of the assay and that the thawed enzyme be kept on ice throughout. Best performance will be obtained by adding the chilled, undiluted enzyme directly to pre-warmed buffer and proceeding immediately to the addition of pre-warmed substrate. The remaining, unused enzyme should be refrozen quickly by, for example, snap freezing in a dry/ice ethanol bath or liquid nitrogen. The enzyme is stable to at least 4 freeze/thaw cycles. To minimize the number of freeze/thaw cycles, aliquot the HDAC8 into separate tubes before storing at -80°C.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.