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ACY1 Antibody (Center) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q03154 |
|---|---|
| Clone Names | 101008220 |
| Gene ID | 95 |
|---|---|
| Other Names | Aminoacylase-1, ACY-1, N-acyl-L-amino-acid amidohydrolase, ACY1 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | ACY1 |
|---|---|
| Function | Catalyzes the hydrolysis of N-acetylated amino acids to acetate and free amino acids. |
| Cellular Location | Cytoplasm. |
| Tissue Location | Expression is highest in kidney, strong in brain and weaker in placenta and spleen. |
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Background
This gene encodes a cytosolic, homodimeric, zinc-bindingenzyme that catalyzes the hydrolysis of acylated L-amino acids toL-amino acids and an acyl group, and has been postulated tofunction in the catabolism and salvage of acylated amino acids.This gene is located on chromosome 3p21.1, a region reduced tohomozygosity in small-cell lung cancer (SCLC), and its expressionhas been reported to be reduced or undetectable in SCLC cell linesand tumors. The amino acid sequence of human aminoacylase-1 ishighly homologous to the porcine counterpart, and this enzyme isthe first member of a new family of zinc-binding enzymes. Mutationsin this gene cause aminoacylase-1 deficiency, a metabolic disordercharacterized by central nervous system defects and increasedurinary excretion of N-acetylated amino acids. Alternative splicingof this gene results in multiple transcript variants. Read-throughtranscription also exists between this gene and the upstreamABHD14A (abhydrolase domain containing 14A) gene, as represented inGeneID:100526760. A related pseudogene has been identified onchromosome 18.
References
Tylki-Szymanska, A., et al. J. Inherit. Metab. Dis. (2010) In press :Lindner, H.A., et al. Biochemistry 47(14):4266-4275(2008)Sass, J.O., et al. Neurology 68(24):2151-2153(2007)Sass, J.O., et al. Am. J. Hum. Genet. 78(3):401-409(2006)Van Coster, R.N., et al. Biochem. Biophys. Res. Commun. 338(3):1322-1326(2005)
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