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N-alpha-acetylation is among the most common post-translational protein modifications in eukaryotic cells. Additionally we are shipping ARD1 Homolog, N-Acetyltransferase Antibodies (51) and ARD1 Homolog, N-Acetyltransferase Kits (1) and many more products for this protein.
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The results observed an inverse correlation between the expression of NAA10 and that of miR (show MLXIP Proteins)-342-5p and miR (show MLXIP Proteins)-608 .
Human Naa15 (NATH (show NAA15 Proteins)) and Naa10 (ARD1) form a stable NatA complex which associates with ribosomes and performs co-translational N-terminal acetylation; Naa15 (NATH (show NAA15 Proteins)) and Naa10 (ARD1) are cleaved during apoptosis resulting in decreased acetyltransferase activity
The clinical spectrum of NAA10.
there is no difference in lysine acetylation of substrate proteins with or without Naa10, suggesting that the substrates may be acetylated chemically rather than enzymatically.
Combined high expression of Naa10p, SNCG (show SNCG Proteins) and PRL-3 are associated with lymph node metastasis in breast cancer.
De novo missense mutations in the NAA10 gene cause severe non-syndromic developmental delay in males and females
human ARD1 (show TRIM23 Proteins) variants have different effects on cell proliferation, which may result from distinct subcellular localizations and autoacetylation activities.
Naa10 structure and function. [Review]
Autoacetylation of ARD1 (show TRIM23 Proteins) variants differentially regulates angiogenesis and cell proliferation in an isoform-specific manner.
ARD1 (show TRIM23 Proteins) has a crucial role in the cellular response to oxidative stress as a bona fide regulator of MSRA (show MSRA Proteins).
The lethal Ogden syndrome-associated mutation of Naa10p disrupts its binding to the imprinting control region of H19 (show NCKAP1 Proteins) and Dnmt1 (show DNMT1 Proteins) recruitment.
NAA10 acts as a guard ensuring balanced osteogenesis by fine-tuning Runx2 (show RUNX2 Proteins) signalling in a feedback manner.
ARD1 has a crucial role in the cellular response to oxidative stress as a bona fide regulator of MSRA (show MSR1 Proteins).
mARD1A(225) may be a novel upstream target that blocks VEGFA (show VEGFA Proteins) expression and tumor-related angiogenesis.
Biochemical analysis demonstrated that mNAT1 and its evolutionarily conserved co-subunit, mARD1, assemble to form a functional acetyltransferase.
Mouse ortholog (225) of ARD1 strongly decreased the level of hypoxia inducible factor (HIF)-1 alpha (show HIF1A Proteins) and increased the extent of acetylation, whereas mARD1(235) variants had a much weaker effect on HIF-1 alpha (show HIF1A Proteins) stability and acetylation.
These results indicate that ARD1(235) and ARD1(225) isoforms may have different activities and function in different subcellular compartments of mammalian cells.
N-alpha-acetylation is among the most common post-translational protein modifications in eukaryotic cells. This process involves the transfer of an acetyl group from acetyl-coenzyme A to the alpha-amino group on a nascent polypeptide and is essential for normal cell function. This gene encodes an N-terminal acetyltransferase that functions as the catalytic subunit of the major amino-terminal acetyltransferase A complex. Mutations in this gene are the cause of Ogden syndrome. Alternate splicing results in multiple transcript variants.
ARD1 homolog A, N-acetyltransferase
, N-acetyltransferase ARD1, human homolog of
, N-alpha-acetyltransferase 10
, N-alpha-acetyltransferase 10, NatA catalytic subunit
, N-terminal acetyltransferase complex ARD1 subunit homolog A
, alpha-N-acetyltransferase 1A
, natA catalytic subunit
, N-acetyltransferase ARD1
, N(alpha)-acetyltransferase 10, NatA catalytic subunitNalpha acetyltransferase 10
, N-acetyltransferase ARD1 homolog
, Nalpha acetyltransferase 10