ARD1 Homolog, N-Acetyltransferase Proteins (ARD1A)

N-alpha-acetylation is among the most common post-translational protein modifications in eukaryotic cells. Additionally we are shipping ARD1 Homolog, N-Acetyltransferase Antibodies (50) and ARD1 Homolog, N-Acetyltransferase Kits (3) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
ARD1A 8260 P41227
ARD1A 56292 Q9QY36
Rat ARD1A ARD1A 363518  
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Top ARD1 Homolog, N-Acetyltransferase Proteins at antibodies-online.com

Showing 7 out of 9 products:

Catalog No. Origin Source Conjugate Images Quantity Delivery Price Details
Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg 30 to 35 Days
$5,370.21
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Escherichia coli (E. coli) Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg 30 to 35 Days
$5,370.21
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Baculovirus infected Insect Cells Human GST tag,His tag 100 μg 14 to 16 Days
$440.65
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Wheat germ Human GST tag 10 μg 11 to 12 Days
$414.29
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HEK-293 Cells Human Myc-DYKDDDDK Tag Validation with Western Blot 20 μg 11 Days
$888.80
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Escherichia coli (E. coli) Human His tag 100 μg 15 to 19 Days
$646.15
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Yeast Cow His tag   1 mg 60 to 71 Days
$2,594.17
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ARD1A Proteins by Origin and Source

Origin Expressed in Conjugate
Human , , ,
, , ,
Mouse (Murine)

More Proteins for ARD1 Homolog, N-Acetyltransferase (ARD1A) Interaction Partners

Human ARD1 Homolog, N-Acetyltransferase (ARD1A) interaction partners

  1. Higher NAA10 transcripts were observed in metastatic osteosarcoma tissues and correlated with worse prognosis. Its knockdown and overexpression in osteosarcoma cells respectively led to decreased and increased cell migratory/invasive abilities. Naa10p was directly associated with MMP-2 protein through its acetyltransferase domain maintaining MMP-2 protein stability.

  2. Results show that NAA10 active site is regulated by HYPK inhibiting the activity of N-terminal acetyltransferases A.

  3. A novel NAA10 mutation was identified in three cases of developmental delay, intellectual disability, and hypertrophic cardiomyopathy. Pathogenic NAA10 variant impaired acetyltransferase activity and stability.

  4. Since the FIH-1 dependent hydroxylation of NAA10 occurs oxygen-dependently, NAA10 acetylates HIF-1alpha under normoxia but does not under hypoxia.

  5. In combination with acetylation assays, the HypK N-terminal region is identified as a negative regulator of the NatA acetylation activity

  6. ARD1-mediated Hsp70 acetylation is a regulatory mechanism that temporally balances protein refolding/degradation in response to stress

  7. Negative regulation of Naa10 towards NTN1 and its receptor UNC5B were also detected upon treatment of all-trans retinoid acid, which was often used to induce morphological differentiation.

  8. A novel de novo NAA10 c.332 T>G p.(Val111Gly) missense variant was detected in a girl with mild/moderate non-syndromic intellectual disability. NAA10 V111G displayed reduced monomeric NAT activity and stability, but intact NatA-mediated NAT activity.

  9. Expression of ARD1 increases levels of androgen receptor acetylation and androgen receptor-HSP90 dissociation in a dose dependent manner.

  10. Study reports on a total of 12 affected females with four different de novo missense mutations in NAA10 and one inherited mutation in a familial case due to germline mosaicism, thus further expanding themutational and clinical spectrum associated with NAA10 related N-terminal-acetyltransferase deficiency.

  11. our study illustrated that the expression of Naa10p had a potential value for predicting the progression of OSCC and prognosis of OSCC patients.

  12. The results observed an inverse correlation between the expression of NAA10 and that of miR-342-5p and miR-608 .

  13. Human Naa15 (NATH) and Naa10 (ARD1) form a stable NatA complex which associates with ribosomes and performs co-translational N-terminal acetylation; Naa15 (NATH) and Naa10 (ARD1) are cleaved during apoptosis resulting in decreased acetyltransferase activity

  14. The clinical spectrum of NAA10.

  15. 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.

  16. Combined high expression of Naa10p, SNCG and PRL-3 are associated with lymph node metastasis in breast cancer.

  17. De novo missense mutations in the NAA10 gene cause severe non-syndromic developmental delay in males and females

  18. human ARD1 variants have different effects on cell proliferation, which may result from distinct subcellular localizations and autoacetylation activities.

  19. Naa10 structure and function. [Review]

  20. Autoacetylation of ARD1 variants differentially regulates angiogenesis and cell proliferation in an isoform-specific manner.

Mouse (Murine) ARD1 Homolog, N-Acetyltransferase (ARD1A) interaction partners

  1. Negative regulation of Naa10 towards NTN1 and its receptor UNC5B were also detected upon treatment of all-trans retinoid acid, which was often used to induce morphological differentiation.

  2. The lethal Ogden syndrome-associated mutation of Naa10p disrupts its binding to the imprinting control region of H19 and Dnmt1 recruitment.

  3. NAA10 acts as a guard ensuring balanced osteogenesis by fine-tuning Runx2 signalling in a feedback manner.

  4. ARD1 has a crucial role in the cellular response to oxidative stress as a bona fide regulator of MSRA.

  5. mARD1A(225) may be a novel upstream target that blocks VEGFA expression and tumor-related angiogenesis.

  6. Biochemical analysis demonstrated that mNAT1 and its evolutionarily conserved co-subunit, mARD1, assemble to form a functional acetyltransferase.

  7. Mouse ortholog (225) of ARD1 strongly decreased the level of hypoxia inducible factor (HIF)-1 alpha and increased the extent of acetylation, whereas mARD1(235) variants had a much weaker effect on HIF-1 alpha stability and acetylation.

  8. These results indicate that ARD1(235) and ARD1(225) isoforms may have different activities and function in different subcellular compartments of mammalian cells.

ARD1 Homolog, N-Acetyltransferase (ARD1A) Protein Profile

Protein Summary

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.

Gene names and symbols associated with ARD1A

  • N(alpha)-acetyltransferase 10, NatA catalytic subunit (NAA10)
  • N(alpha)-acetyltransferase 10, NatA catalytic subunit (Naa10)
  • 2310039H09Rik protein
  • Ard1 protein
  • Ard1a protein
  • DXS707 protein
  • NATD protein
  • RGD1565315 protein
  • Te2 protein

Protein level used designations for ARD1A

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

GENE ID SPECIES
8260 Homo sapiens
613636 Bos taurus
100328748 Oryctolagus cuniculus
56292 Mus musculus
363518 Rattus norvegicus
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