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. [provided by RefSeq].
Related Pathway
* Shipping is in business days
* OriGene provides validated application data and protocol, with money back guarantee.
HEK293T cells were transfected with the pCMV6-ENTRY control (Left lane) or pCMV6-ENTRY ACY1 (RC201284, Right lane) cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-ACY1.
HEK293T cells transfected with either RC201284 overexpress plasmid(Red) or empty vector control plasmid(Blue) were immunostained by anti-ACY1 antibody(TA503250), and then analyzed by flow cytometry.
Researchers who bought this antibody have also purchased:
