Recombinant Human NAA50 protein

NAA50. also known as Nat5 or SAN, is a member of the N-terminal acetyltransferase (NAT) family, which catalyzes the transfer of acetyl groups from acetyl-CoA to the α-amino terminus of proteins. This post-translational modification is crucial for regulating protein stability, localization, and interactions. NAA50 is part of the NatE complex, alongside NAA10 and NAA15. and exhibits unique substrate specificity, preferentially acetylating histones and proteins involved in cell division, such as those in the cohesin complex. Its role in mitotic progression and chromosomal segregation highlights its importance in cell cycle regulation.

Recombinant NAA50 protein is engineered for in vitro studies to elucidate its enzymatic mechanisms, structural features, and interactions. Typically produced in bacterial (e.g., *E. coli*) or eukaryotic expression systems, the recombinant protein is purified via affinity chromatography, often utilizing tags like His-tag or GST-tag. Researchers employ it in enzymatic assays to characterize acetylation kinetics, substrate preferences, and inhibitor screening. Structural studies using X-ray crystallography or cryo-EM have revealed its conserved catalytic domain and unique loop regions critical for substrate binding.

Interest in NAA50 extends to disease contexts, particularly cancer, where aberrant N-terminal acetylation is linked to tumor progression. Its dual role in acetylating both histones and non-histone proteins positions it as a potential therapeutic target. Recombinant NAA50 also aids in exploring crosstalk between acetylation and other post-translational modifications, advancing understanding of epigenetic regulation. Overall, this tool bridges molecular biology and translational research, offering insights into cellular homeostasis and disease mechanisms.