Purification of metal-dependent lysine deacetylases with consistently high activity.
Ontology highlight
ABSTRACT:
SUBMITTER: Toro TB
PROVIDER: S-EPMC5624855 | biostudies-literature | 2018 Jan
REPOSITORIES: biostudies-literature
Publications
Purification of metal-dependent lysine deacetylases with consistently high activity.
Toro Tasha B TB Painter Richard G RG Haynes Rashad A RA Glotser Elena Y EY Bratton Melyssa R MR Bryant Jenae R JR Nichols Kyara A KA Matthew-Onabanjo Asia N AN Matthew Ashley N AN Bratcher Derek R DR Perry Chanel D CD Watt Terry J TJ
Protein expression and purification 20170824
Metal-dependent lysine deacetylases (KDACs) are involved in regulation of numerous biological and disease processes through control of post-translational acetylation. Characterization of KDAC activity and substrate identification is complicated by inconsistent activity of prepared enzyme and a range of multi-step purifications. We describe a simplified protocol based on two-step affinity chromatography. The purification method is appropriate for use regardless of expression host, and we demonstr ...[more]
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