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Using ImmuneChem’s Anti-Acetyl Lysine (ICP0380) scientists have discovered inducible lysine acetylation in E.coli extracts upon Arabidopsis GCN5-related N-acetyltransferase expression

Scientists who published a paper in Molecular Systems Biology have discovered Inducible Lysine Acetylation in E. coli extracts upon Arabidopsis GCN5-related N-acetyltransferase expression.

Anti-acetyl lysine (ICP0380) Western blot analyses and total protein stains of E. coli cell extracts before (ni) and after (i) plasmid induction with IPTG.

Bienvenut. W. V., Brünje. A., Boyer. J-B., et al. Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning protein acetylation. Mol. Systems Biology. 2020. 16:e9464

Method: 

Anti-acetyl lysine (ICP0380) Western blot analyses and total protein stains of E. coli cell extracts. Cellular protein extracts before and after induction of His6-MBP-GNAT expression were separated on 12% acrylamide gels and immunoblotted by using an anti-acetyl lysine (ICP0380) or stained with Coomassie dye. In the total protein stains, recombinant GNAT protein constructs were highlighted by blue arrowheads. Protein expression before (ni) and after (i) induction with IPTG is indicated. The luminescence signal, indicating acetylated proteins, was usually recorded after 40–120 s. The luminescence for MBP-GNAT4 was additionally recorded for 10 s (indicated by an asterisk).