NAA40 / Unconjugated /
Product Details
| Description | N-terminal acetylation is one of the most common protein modifications in eukaryotes, occurring on approximately 57% and 84% on yeast and human proteins respectively. There are several N-terminal acetylating enzyme complexes (NatA – NatE). Unlike the other complexes, NatD is composed of a single protein, NAT11, and has recently been described to acetylate the Serine N-termini of histones H2A and H4 in yeast. The role these modifications play is unknown; yeast that do not express NAT11 grow at normal rates and have no observable phenotypes. The role of the human homolog is likewise unknown. | |
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| Conjugate | Unconjugated | |
| Clone | ||
| Target Species | Human, Mouse | |
| Applications | ELISA, WB, IHC | |
| Supplier | Aviva Systems Biology | |
| Catalog # | Sign in to view product details, citations, and spectra | |
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About NAA40
Enables H2A histone acetyltransferase activity; H4 histone acetyltransferase activity; and peptide-serine-N-acetyltransferase activity. Involved in N-terminal protein amino acid acetylation; histone H2A acetylation; and histone H4 acetylation. Located in centriolar satellite; cytosol; and nucleoplasm. [provided by Alliance of Genome Resources, Apr 2022]
Enables H2A histone acetyltransferase activity; H4 histone acetyltransferase activity; and peptide-serine-N-acetyltransferase activity. Involved in N-terminal protein amino acid acetylation; histone H2A acetylation; and histone H4 acetylation. Located in centriolar satellite; cytosol; and nucleoplasm. [provided by Alliance of Genome Resources, Apr 2022]
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