Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5515966 | Protein Expression and Purification | 2018 | 6 Pages |
â¢A relatively simple, straightforward, and robust protocol for KDAC purification.â¢Applicable to multiple expression hosts.â¢High yield of highly active, stable enzymes.â¢Enhanced preparation consistency for more reliable characterization.
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 demonstrate purification of several representative members of the KDAC family as well as a selection of mutated variants. The purified proteins are highly active and consistent across preparations.