Anti-ACY-1/ACY1 Antibody Picoband® fluoro488 Vervoeging

Aminoacylase-1 is an enzyme that in humans is encoded by the ACY1 gene. This gene encodes a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and an acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. This gene is located on chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and this enzyme is the first member of a new family of zinc-binding enzymes. Mutations in this gene cause aminoacylase-1 deficiency, a metabolic disorder characterized by central nervous system defects and increased urinary excretion of N-acetylated amino acids. Alternative splicing of this gene results in multiple transcript variants. Read-through transcription also exists between this gene and the upstream ABHD14A (abhydrolase domain containing 14A) gene, as represented in GeneID:100526760. A related pseudogene has been identified on chromosome 18.

N-alpha-acetyltransferase 15, NatA auxiliary subunit; Gastric cancer antigen Ga19; N-terminal acetyltransferase; NMDA receptor-regulated protein 1; Protein tubedown-1; Tbdn100; NAA15; GA19, NARG1, NATH, TBDN100

ACY1

95

Q03154

Human, Mouse, Rat

No cross-reactivity with other proteins

E.coli-derived human ACY-1/ACY1 recombinant protein (Position: E8-A354) .

Expressed at high levels in testis and in ocular endothelial cells. Also found in brain (corpus callosum), heart, colon, bone marrow and at lower levels in most adult tissues, including thyroid, liver, pancreas, mammary and salivary glands, lung, ovary, urogenital system and upper gastrointestinal tract. Overexpressed in gastric cancer, in papillary thyroid carcinomas and in a Burkitt lymphoma cell line (Daudi) . Specifically suppressed in abnormal proliferating blood vessels in eyes of patients with proliferative diabetic retinopathy. .

Flow Cytometry

Cancer, Cancer Susceptibility, Cardiovascular, Domain Families, Epigenetics and Nuclear Signaling, Hlh/Leucine Zipper, Hypertrophy, Immunology, Innate Immunity, Oncoproteins, Oncoproteins/Suppressors, Proto-Oncogenes, TLR Signaling, Transcription, Transcription Factors

Immunogen affinity purified.

Liquid

Auxillary subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Required to control retinal neovascularization in adult ocular endothelial cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates transcription from the osteocalcin promoter. .

1. Boldog, F., Erlandsson, R., Klein, G., Sumegi, J. Long-range restriction enzyme maps of DNF15S2, D3S2 and c-raf1 loci on the short arm of human chromosome 3. Cancer Genet. Cytogenet. 42: 295-306, 1989. 2. Cook, R. M., Burke, B. J., Buchhagen, D. L., Minna, J. D., Miller, Y. E. Human aminoacylase-1: cloning, sequence, and expression analysis of a chromosome 3p21 gene inactivated in small cell lung cancer. J. Biol. Chem. 268: 17010-17017, 1993. 3. Ferri, L., Funghini, S., Fioravanti, A., Biondi, E. G., la Marca, G., Guerrini, R., Donati, M. A., Morrone, A. Aminoacylase I deficiency due to ACY1 mRNA exon skipping. Clin. Genet. 86: 367-372, 2014.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

101272 MW

6

N-alpha-acetyltransferase 15, NatA auxiliary subunit

Cytoplasm. Nucleus. Mainly cytoplasmic, nuclear in some cases. Present in the free cytosolic and cytoskeleton-bound polysomes, but not in the membrane-bound polysomes.

N-alpha-acetyltransferase 15, NatA auxiliary subunit

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.