About Aminoacylase 1
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, Nov 2010]

About PE
Phycoerythrin (PE, R-PE) is a red-emitting fluorescent protein-chromophore complex that can be excited the 488-nm blue, 532-nm green, or 561-nm yellow-green laser with increasing efficiency and captured with a 586/14 nm bandpass filter. PE has an excitation peak at 565 nm and an emission peak at 578 nm. PE is 240kD in size and has an extinction coefficient of ~2x10^6 which makes it one of the brightest fluorophores available and a potent donor upon which to build tandem fluorophores with longer Stoke's Shifts.